Accepted name: 4-acetamidobutyryl-CoA deacetylase
Reaction: 4-acetamidobutanoyl-CoA + H2O = acetate + 4-aminobutanoyl-CoA
Other name(s): aminobutyryl-CoA thiolesterase; deacetylase-thiolesterase
Systematic name: 4-acetamidobutanoyl-CoA amidohydrolase
Comments: The enzyme also hydrolyses 4-aminobutanoyl-CoA to aminobutanoate and coenzyme A.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ohsugi, M., Khan, J., Hensley, C., Chew, S. and Barker, H.A. Metabolism of L-β-lysine by a Pseudomonas. Purification and properties of a deacetylase-thiolesterase utilizing 4-acetamidobutyryl CoA and related compounds. J. Biol. Chem. 256 (1981) 7642-7651. [PMID: 6788773]
Accepted name: peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase
Reaction: Hydrolysis of an N4-(acetyl-β-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-β-D-glucosaminylamine and a peptide containing an aspartate residue
Other name(s): glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase
Systematic name: N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase
Comments: Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26 N4-(β-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 83534-39-8
References:
1. Plummer, T.H., Jr. and Tarentino, A.L. Facile cleavage of complex oligosaccharides from glycopeptides by almond emulsin peptide: N-glycosidase. J. Biol. Chem. 256 (1981) 10243-10246. [PMID: 7287707]
2. Takahashi, N. Demonstration of a new amidase acting on glycopeptides. Biochem. Biophys. Res. Commun. 76 (1977) 1194-1201. [PMID: 901470]
3. Takahashi, N. and Nishibe, H. Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages. J. Biochem. (Tokyo) 84 (1978) 1467-1473. [PMID: 738997]
4. Tarentino, A.L., Gomez, C.M. and Plummer, T.H., Jr. Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. Biochemistry 24 (1985) 4665-4671. [PMID: 4063349]
Accepted name: N-carbamoylputrescine amidase
Reaction: N-carbamoylputrescine + H2O = putrescine + CO2 + NH3
Other name(s): carbamoylputrescine hydrolase; NCP
Systematic name: N-Carbamoylputrescine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 85030-69-9
References:
1. Yanagisawa, H. and Suzuki, Y. Preparation and properties of N-carbamylputrescine amidohydrolase from maize shoots. Phytochemistry 21 (1982) 2201-2203.
Accepted name: allophanate hydrolase
Reaction: urea-1-carboxylate + H2O = 2 CO2 + 2 NH3
For diagram of reaction click here.
Glossary: allophanate = urea-1-carboxylate
Other name(s): allophanate lyase; AtzF; TrzF
Systematic name: urea-1-carboxylate amidohydrolase
Comments: Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate [6].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 79121-96-3
References:
1. Maitz, G.S., Haas, E.M. and Castric, P.A. Purification and properties of the allophanate hydrolase from Chlamydomonas reinhardii. Biochim. Biophys. Acta 714 (1982) 486-491.
2. Roon, R.J. and Levenberg, B. Urea amidolyase. I. Properties of the enzyme from Candida utilis. J. Biol. Chem. 247 (1972) 4107-4113. [PMID: 4556303]
3. Sumrada, R.A. and Cooper, T.G. Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast. J. Biol. Chem. 257 (1982) 9119-9127. [PMID: 6124544]
4. Kanamori, T., Kanou, N., Kusakabe, S., Atomi, H. and Imanaka, T. Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea. FEMS Microbiol. Lett. 245 (2005) 61-65. [PMID: 15796980]
5. Cheng, G., Shapir, N., Sadowsky, M.J. and Wackett, L.P. Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism. Appl. Environ. Microbiol. 71 (2005) 4437-4445. [PMID: 16085834]
6. Shapir, N., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP. J. Bacteriol. 187 (2005) 3731-3738. [PMID: 15901697]
7. Shapir, N., Cheng, G., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth. Appl. Environ. Microbiol. 72 (2006) 2491-2495. [PMID: 16597948]
Accepted name: long-chain-fatty-acyl-glutamate deacylase
Reaction: N-long-chain-fatty-acyl-L-glutamate + H2O = a long-chain carboxylate + L-glutamate
Other name(s): long-chain aminoacylase; long-chain-fatty-acyl-glutamate deacylase; long-chain acylglutamate amidase; N-acyl-D-glutamate deacylase
Systematic name: N-long-chain-fatty-acyl-L-glutamate amidohydrolase
Comments: Does not act on acyl derivates of other amino acids. Optimum chain length of acyl residue is 12 to 16.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 82249-69-2
References:
1. Fukuda, H., Iwade, S. and Kimura, A. A new enzyme: long acyl aminoacylase from Pseudomonas diminuta. J. Biochem. (Tokyo) 91 (1982) 1731-1738. [PMID: 7096313]
Accepted name: N,N-dimethylformamidase
Reaction: N,N-dimethylformamide + H2O = dimethylamine + formate
Other name(s): dimethylformamidase; DMFase
Systematic name: N,N-dimethylformamide amidohydrolase
Comments: An iron protein. Also acts on N-ethylformamide and N-methyl-formamide and, more slowly, on N,N-diethylformamide, N,N-dimethylacetamide and unsubstituted acyl amides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 104645-73-0
References:
1. Schär, H.-P., Holzmann, W., Ramos Tombo, G.M. and Ghisalba, O. Purification and characterization of N,N-dimethylformamidase from Pseudomonas DMF 3/3. Eur. J. Biochem. 158 (1986) 469-475. [PMID: 3732281]
Accepted name: tryptophanamidase
Reaction: L-tryptophanamide + H2O = L-tryptophan + NH3
Other name(s): tryptophan aminopeptidase; L-tryptophan aminopeptidase
Systematic name: L-tryptophanamide amidohydrolase
Comments: Requires Mn2+. Also acts on N-ethylformamide and L-tyrosinamide, and on some tryptophan dipeptides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 76689-19-5
References:
1. Iwayama, A., Kimura, T., Adachi, O. and Ameyama, M. Crystallization and characterization of a novel aminopeptidase from Trichosporon cutaneum. Agric. Biol. Chem. 47 (1983) 2483-2493.
Accepted name: N-benzyloxycarbonylglycine hydrolase
Reaction: N-benzyloxycarbonylglycine + H2O = benzyl alcohol + CO2 + glycine
Other name(s): benzyloxycarbonylglycine hydrolase; Nα-carbobenzoxyamino acid amidohydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase I
Systematic name: N-benzyloxycarbonylglycine urethanehydrolase
Comments: Also acts, more slowly, on N-benzyloxycarbonylalanine, but not on the corresponding derivatives of other amino acids or on N-benzyloxycarbonylpeptides. Requires Co2+ or Zn2+. cf. EC 3.5.1.64 Nα-benzyloxycarbonylleucine hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 91930-69-7
References:
1. Murao, S., Matsumura, E. and Kawano, T. Isolation and characterization of a novel enzyme, Nα-benzyloxycarbonyl amino acid urethane hydrolase, from Streptococcus faecalis R ATCC 8043. Agric. Biol. Chem. 49 (1985) 967-972.
Accepted name: N-carbamoylsarcosine amidase
Reaction: N-carbamoylsarcosine + H2O = sarcosine + CO2 + NH3
For diagram of reaction click here.
Other name(s): carbamoylsarcosine amidase
Systematic name: N-carbamoylsarcosine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 92767-52-7
References:
1. Deeg, R., Roeder, A., Siedel, J., Gauhl, H. and Ziegenhorn, J. Process and reagent for the determination of N-carbamoylsarcosine with the use of a new enzyme. Patent DE3248145, 1982, Chem. Abstr. 101 (1984) 187515.
Accepted name: N-(long-chain-acyl)ethanolamine deacylase
Reaction: N-(long-chain-acyl)ethanolamine + H2O = a long-chain carboxylate + ethanolamine
Other name(s): NAAA (gene name); N-acylethanolamine amidohydrolase; acylethanolamine amidase
Systematic name: N-(long-chain-acyl)ethanolamine amidohydrolase
Comments: This lysosomal enzyme acts best on palmitoyl ethanolamide, with lower activity on other N-(long-chain-acyl)ethanolamines. It is only active at acidic pH. Unlike EC 3.5.1.99, fatty acid amide hydrolase, it does not act on primary amides such as oleamide, and has only a marginal activity with anandamide. The enzyme is translated as an inactive proenzyme, followed by autocatalytic cleavage into two subunits that reassociate to form an active heterodimeric complex.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99283-61-1
References:
1. Ueda, N., Yamanaka, K. and Yamamoto, S. Purification and characterization of an acid amidase selective for N-palmitoylethanolamine, a putative endogenous anti-inflammatory substance. J. Biol. Chem 276 (2001) 35552-35557. [PMID: 11463796]
2. Ueda, N., Yamanaka, K., Terasawa, Y. and Yamamoto, S. An acid amidase hydrolyzing anandamide as an endogenous ligand for cannabinoid receptors. FEBS Lett. 454 (1999) 267-270. [PMID: 10431820]
3. West, J.M., Zvonok, N., Whitten, K.M., Wood, J.T. and Makriyannis, A. Mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase. J Proteome Res 11 (2012) 972-981. [PMID: 22040171]
4. Zhao, L.Y., Tsuboi, K., Okamoto, Y., Nagahata, S. and Ueda, N. Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism. Biochim. Biophys. Acta 1771 (2007) 1397-1405. [PMID: 17980170]
[EC 3.5.1.61 Transferred entry: mimosinase. Now EC 4.3.3.8, mimosinase (EC 3.5.1.61 created 1989, deleted 2022)]
Accepted name: acetylputrescine deacetylase
Reaction: N-acetylputrescine + H2O = acetate + putrescine
Glossary: spermidine
Systematic name: N-acetylputrescine acetylhydrolase
Comments: The enzyme from Micrococcus luteus also acts on N8-acetylspermidine and acetylcadaverine, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 103679-48-7
References:
1. Suzuki, O., Ishikawa, Y., Miyazaki, K., Izu, K. and Matsumoto, T. Acetylputrescine deacetylase from Micrococcus luteus K-11. Biochim. Biophys. Acta 882 (1986) 140-142.
Accepted name: 4-acetamidobutyrate deacetylase
Reaction: 4-acetamidobutanoate + H2O = acetate + 4-aminobutanoate
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Systematic name: 4-acetamidobutanoate amidohydrolase
Comments: Also acts on N-acetyl-β-alanine and 5-acetamidopentanoate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 102347-82-0
References:
1. Haywood, G.W. and Large, P.J. 4-Acetamidobutyrate deacetylase in the yeast Candida boidinii grown on putrescine or spermidine as sole nitrogen source and its probable role in polyamine catabolism. J. Gen. Microbiol. 132 (1986) 7-14.
Accepted name: Nα-benzyloxycarbonylleucine hydrolase
Reaction: Nα-benzyloxycarbonyl-L-leucine + H2O = benzyl alcohol + CO2 + L-leucine
Other name(s): benzyloxycarbonylleucine hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase IV
Systematic name: Nα-benzyloxycarbonyl-L-leucine urethanehydrolase
Comments: Also acts on Nα-t-butoxycarbonyl-L-leucine, and, more slowly, on the corresponding derivatives of L-aspartate, L-methionine, L-glutamate and L-alanine. cf. EC 3.5.1.58 N-benzyloxycarbonylglycine hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 100630-47-5
References:
1. Matsumura, E., Shin, T., Murao, S., Sakaguchi, M. and Kawano, T. A novel enzyme, Nα-benzyloxycarbonyl amino acid urethane hydrolase IV. Agric. Biol. Chem. 49 (1985) 3643-3645.
Accepted name: theanine hydrolase
Reaction: N5-ethyl-L-glutamine + H2O = L-glutamate + ethylamine
Glossary: L-theanine = N5-ethyl-L-glutamine
Systematic name: N5-ethyl-L-glutamine amidohydrolase
Comments: Also acts on other N-alkyl-L-glutamines.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 99533-51-4
References:
1. Tsushida, T. and Takeo, T. An enzyme hydrolyzing L-theanine in tea leaves. Agric. Biol. Chem. 49 (1985) 2913-2917.
Accepted name: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase
Reaction: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate + 2 H2O = acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2
Other name(s): compound B hydrolase; α-hydroxymethyl-α'-(N-acetylaminomethylene)succinic acid hydrolase
Systematic name: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating)
Comments: Involved in the degradation of pyridoxin by Pseudomonas and Arthrobacter.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 95829-26-8
References:
1. Huynh, M.S. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of two N-acetylamidohydrolases. J. Biol. Chem. 260 (1985) 2379-2383. [PMID: 3972793]
Accepted name: 4-methyleneglutaminase
Reaction: 4-methylene-L-glutamine + H2O = 4-methylene-L-glutamate + NH3
Other name(s): 4-methyleneglutamine deamidase; 4-methyleneglutamine amidohydrolase
Systematic name: 4-methylene-L-glutamine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 86855-36-9
References:
1. Ibrahim, S.A., Lea, P.J. and Fowden, L. Preparation and properties of 4-methyleneglutaminase from the leaves of peanut (Arachis hypogaea). Phytochemistry 23 (1984) 1545-1549.
Accepted name: N-formylglutamate deformylase
Reaction: N-formyl-L-glutamate + H2O = formate + L-glutamate
For diagram click here.
Other name(s): β-citryl-L-glutamate hydrolase; formylglutamate deformylase; N-formylglutamate hydrolase; β-citrylglutamate amidase; β-citryl-L-glutamate amidohydrolase; β-citryl-L-glutamate amidase; β-citrylglutamate amidase; β-citryl-L-glutamate-hydrolyzing enzyme
Systematic name: N-formyl-L-glutamate amidohydrolase
Comments: The animal enzyme also acts on β-citryl-L-glutamate and β-citryl-L-glutamine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 97286-12-9
References:
1. Hu, L., Mulfinger, L.M. and Phillips, A.T. Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida. J. Bacteriol. 169 (1987) 4696-4702. [PMID: 3308850]
2. Miyake, M., Innami, T. and Kakimoto, Y. A β-citryl-L-glutamate-hydrolysing enzyme in rat testes. Biochim. Biophys. Acta 760 (1983) 206-214. [PMID: 6414521]
Accepted name: glycosphingolipid deacylase
Reaction: Hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives
Other name(s): glycosphingolipid ceramide deacylase
Systematic name: glycosphingolipid amidohydrolase
Comments: Does not act on sphingolipids such as ceramide. Not identical with EC 3.5.1.23 ceramidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122544-53-0
References:
1. Hirabayashi, Y., Kimura, M., Matsumoto, M., Yamamoto, K., Kadowaki, S. and Tochikura, T. A novel glycosphingolipid hydrolyzing enzyme, glycosphingolipid ceramide deacylase, which cleaves the linkage between the fatty acid and sphingosine base in glycosphingolipids. J. Biochem. (Tokyo) 103 (1988) 1-4. [PMID: 3360750]
Accepted name: aculeacin-A deacylase
Reaction: Hydrolysis of the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side-chain
Other name(s): aculeacin A acylase
Systematic name: aculeacin-A amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 121479-50-3
References:
1. Takeshima, H., Inokoshi, J., Takada, Y., Tanaka, H. and Omura, S. A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: purification and characterization. J. Biochem. (Tokyo) 105 (1989) 606-610. [PMID: 2760018]
Accepted name: N-feruloylglycine deacylase
Reaction: N-feruloylglycine + H2O = ferulate + glycine
Other name(s): N-feruloylglycine hydrolase
Systematic name: N-feruloylglycine amidohydrolase
Comments: Hydrolyses a range of L-amino acids from the cinnamoyl and substituted cinnamoyl series. Not identical with EC 3.5.1.14 N-acyl-aliphatic-L-amino acid amidohydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 118731-84-3
References:
1. Martens, M., Cottenie-Ruysschaert, M., Hanselaer, R., De Cooman, L., CASteele, K.V. and Van Sumere, F. N-Feruloylglycine amidohydrolase from barley seeds and isolated barley embryos. Phytochemistry 27 (1988) 2457-2463.
2. Martens, M., Cottenie-Ruysschaert, M., Hanselaer, R., De Cooman, L., CASteele, K.V. and Van Sumere, F. Characteristics and specificity of purified N-feruloylglycine amidohydrolase from isolated barley embryos. Phytochemistry 27 (1988) 2465-2475.
Accepted name: D-benzoylarginine-4-nitroanilide amidase
Reaction: N-benzoyl-D-arginine-4-nitroanilide + H2O = N-benzoyl-D-arginine + 4-nitroaniline
Other name(s): benzoyl-D-arginine arylamidase; D-BAPA-ase
Systematic name: N-benzoyl-D-arginine-4-nitroanilide amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 119345-26-5
References:
1. Gofshtein-Gandman, L.V., Keynan, A. and Milner, Y. Bacteria of the genus Bacillus have a hydrolase stereospecific to the D isomer of benzoyl-arginine-p-nitroanilide. J. Bacteriol. 170 (1988) 5895-5900. [PMID: 3142860]
Accepted name: carnitinamidase
Reaction: L-carnitinamide + H2O = L-carnitine + NH3
Other name(s): L-carnitinamidase; carnitine amidase; L-carnitine amidase
Systematic name: L-carnitinamide amidohydrolase
Comments: Does not act on D-carnitinamide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 117444-04-9
References:
1. Nakayama, K., Honda, H., Ogawa, Y., Ozawa, T. and Ota, T. Method for producing carnitine, L-carnitinamide hydrolase and method for producing same. Patent DE3728321, 1988, Chem. Abstr. 109 (1988) 228738.
Accepted name: chenodeoxycholoyltaurine hydrolase
Reaction: chenodeoxycholoyltaurine + H2O = chenodeoxycholate + taurine
Glossary: chenodeoxycholate = 3α,7α-dihydroxy-5β-cholan-24-oate
Systematic name: chenodeoxycholoyltaurine amidohydrolase
Comments: Some other taurine conjugates are hydrolysed, but not glycine conjugates of bile acids.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 125752-75-2
References:
1. Kawamoto, K., Horibe, I. and Uchida, K. Purification and characterization of a new hydrolase for conjugated bile acids, chenodeoxycholyltaurine hydrolase, from Bacteroides vulgatus. J. Biochem. (Tokyo) 106 (1989) 1049-1053. [PMID: 2628421]
Accepted name: urethanase
Reaction: urethane + H2O = ethanol + CO2 + NH3
Other name(s): urethane hydrolase
Systematic name: urethane amidohydrolase (decarboxylating)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122007-70-9
References:
1. Kobashi, K., Takebe, S. and Sakai, T. Urethane-hydrolyzing enzyme from Citrobacter sp. Chem. Pharm. Bull. 38 (1990) 1326-1328. [PMID: 2393957]
Accepted name: arylalkyl acylamidase
Reaction: N-acetylarylalkylamine + H2O = arylalkylamine + acetate
Other name(s): aralkyl acylamidase
Systematic name: N-acetylarylalkylamine amidohydrolase
Comments: identified in Pseudomonas putida. Strict specificity for N-acetyl arylalkylamines, including N-acetyl-2-phenylethylamine, N-acetyl-3-phenylpropylamine, N-acetyldopamine, N-acetyl-serotonin and melatonin. It also accepts arylalkyl acetates but not acetanilide derivatives, which are common substrates of EC 3.5.1.13, aryl acylamidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Shimizu, S., Ogawa, J., Chung, M.C.-M., Yamada, H. Purification and characterization of a novel enzyme, arylalkyl acylamidase, from Pseudomonas putida Sc2. Eur. J. Biochem. 209 (1992) 375-382. [PMID: 1396711]
Accepted name: N-carbamoyl-D-amino-acid hydrolase
Reaction: an N-carbamoyl-D-amino acid + H2O = a D-amino acid + NH3 + CO2
Other name(s): D-N-carbamoylase; N-carbamoylase (ambiguous); N-carbamoyl-D-amino acid hydrolase
Systematic name: N-carbamoyl-D-amino-acid amidohydrolase
Comments: This enzyme, along with EC 3.5.1.87 (N-carbamoyl-L-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [2]. It has strict stereospecificity for N-carbamoyl-D-amino acids and does not act upon the corresponding L-amino acids or on the N-formyl amino acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and -ureidopropanoate, which are substrates for other amidohydrolases.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 71768-08-6
References:
1. Ogawa, J., Shimizu, S., Yamada, H. N-Carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c; purification and characterization. Eur. J. Biochem. 212 (1993) 685-691. [PMID: 8462543]
2. Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559-563. [PMID: 11849938]
Accepted name: glutathionylspermidine amidase
Reaction: glutathionylspermidine + H2O = glutathione + spermidine
For diagram of reaction click here.
Glossary: spermidine
Other name(s): glutathionylspermidine amidohydrolase (spermidine-forming)
Systematic name: γ-L-glutamyl-L-cysteinyl-glycine:spermidine amidase
Comments: spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 171040-71-4
References:
1. Bollinger, J.M., Kwon, D.S., Huisman, G.W., Kolter, R., Walsh, C.T. Glutathionylspermidine metabolism in E. coli. Purification, cloning, overproduction and characterization of a bifunctional glutathionylspermidine synthetase/amidase. J. Biol. Chem. 270 (1995) 14031-14041. [PMID: 7775463]
Accepted name: phthalyl amidase
Reaction: a phthalylamide + H2O = phthalic acid + a substituted amine
Systematic name: phthalyl-amide amidohydrolase
Comments: in the entry, "phthalyl" is used to mean "2-carboxybenzoyl". The enzyme from Xanthobacter agilis hydrolyses phthalylated amino acids, peptides, β-lactams, aromatic and aliphatic amines. The substituent on nitrogen may be an alkyl group, but may also be complex, giving an amino acid or peptide derivative. Substitutions on the phthalyl ring include 6-F, 6-NH2, 3-OH, and a nitrogen in the aromatic ring ortho to the carboxy group attached to the amine. No cofactors are required
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 169150-79-2
References:
1. Briggs, B.S., Kreuzman, A.J., Whitesitt, C., Yeh, W.K., Zmijewski, M. Discovery, purification, and properties of o-phthalyl amidase from Xanthobacter agilis. J. Mol. Catal., B Enzym. 2 (1996) 53-69.
2. Black, T.D., Briggs, B.S., Evans, R., Muth, W.L., Vangala, S., Zmijewski, M.J. o-Phthalyl amidase in the synthesis of Loracarbef: process development using this novel biocatalyst. Biotechnol. Lett. 18 (1996) 875-880.
3. Costello, C., Kreuzman, A., Zmijewski, M. Selective deprotection of phthalyl protected proteins. Tetrahedron Lett. 37 (1996) 7469-7472.
4. Briggs, B.S., Zmijewski, M.J. Enzyme from microbial source: phthalyl amidase. Patent US5445959, 1995. Chem. Abstr. 123 (1995) 250104 (PDF).
[EC 3.5.1.80 Deleted entry: identical to EC 3.5.1.25, N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.80 created 1999, deleted 2002)]
Accepted name: N-acyl-D-amino-acid deacylase
Reaction: N-acyl-D-amino acid + H2O = a carboxylate + D-amino acid
Systematic name: N-acyl-D-amino acid amidohydrolase
Comments: The enzyme from Alcaligenes denitrificans subsp. xylosoxydans and Alcaligenes xylosoxydans subsp. xylosoxydans has wide specificity; hydrolyses N-acyl derivative of neutral D-amino acids. Used in separating D- and L-amino acids. Requires zinc.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 65979-42-2
References:
1. Wakayama, M., Katsuno, Y., Hayashi, S., Miyamoto, Y., Sakai, K. and Moriguchi, M. Cloning and sequencing of a gene encoding D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 and expression of the gene in Escherichia coli. Biosci. Biotechnol. Biochem. 59 (1995) 2115-2119. [PMID: 8541651]
2. Wakayama, M., Hayashi, S., Yatsuda, Y., Katsuno, Y., Sakai, K. and Moriguchi, M. Overproduction of D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 in Escherichia coli and its purification. Protein Expr. Purif. 7 (1996) 395-399. [PMID: 8776758]
Accepted name: N-acyl-D-glutamate deacylase
Reaction: N-acyl-D-glutamate + H2O = a carboxylate + D-glutamate
Systematic name: N-acyl-D-glutamate amidohydrolase
Comments: the enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans and Pseudomonas sp. is specific for N-acyl-D-glutamate. Requires zinc.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 82249-69-2
References:
1. Wakayama, M., Ahshika, T., Miyamoto, Y., Yoshikawa, T., Sonoda, Y., Sakai, K. and Moriguchi, M. Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. J. Biochem. (Tokyo) 118 (1995) 204-209. [PMID: 8537313]
2. Wakayama, M., Miura, Y., Oshima, K., Sakai, K. and Moriguchi, M. Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1. Biosci. Biotechnol. Biochem. 59 (1995) 1489-1492. [PMID: 7549100]
3. Wakayama, M., Tsutsumi, T., Yada, H., Sakai, K. and Moriguchi, M. Chemical modification of histidine residue of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. 5f-1. Biosci. Biotechnol. Biochem. 60 (1996) 650-653. [PMID: 8829533]
Accepted name: N-acyl-D-aspartate deacylase
Reaction: N-acyl-D-aspartate + H2O = a carboxylate + D-aspartate
Systematic name: N-acyl-D-aspartate amidohydrolase
Comments: the enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans is specific for N-acyl-D-aspartate. Requires zinc.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9031-86-1
References:
1. Moriguchi, M., Sakai, K., Katsuno, Y., Maki, T., Wakayama, M. Purification and characterization of novel N-acyl-D-aspartate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. Biosci. Biotechnol. Biochem. 57 (1993) 1145-1148. [PMID: 7763985]
2. Wakayama, M., Watanabe, E., Takenaka, Y., Miyamoto, Y., Tau, Y., Sakai, K., Moriguchi, M. Cloning, expression and nucleotide sequence of the N-acyl-D-aspartate amidohydrolase gene from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. J. Ferment. Bioeng. 80 (1995) 311-317.
Accepted name: biuret amidohydrolase
Reaction: biuret + H2O = urea-1-carboxylate + NH3
For diagram of reaction click here.
Glossary: biuret = imidodicarbonic diamide
allophanate = urea-1-carboxylate
Other name(s): biuH (gene name)
Systematic name: biuret amidohydrolase
Comments: The enzyme, characterized from the bacterium Rhizobium leguminosarum bv. viciae 3841, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazide herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The substrate, biuret, forms by the spontaneous decarboxylation of 1-carboxybiuret in the absence of EC 3.5.1.131, 1-carboxybiuret hydrolase.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, ExplorEnz, KEGG, MetaCyc, PDB, CAS registry number: 95567-88-7
References:
1. Cameron, S.M., Durchschein, K., Richman, J.E., Sadowsky, M.J. and Wackett, L.P. A new family of biuret hydrolases involved in s-triazine ring metabolism. ACS Catal. 2011 (2011) 1075-1082. [PMID: 21897878]
2. Esquirol, L., Peat, T.S., Wilding, M., Lucent, D., French, N.G., Hartley, C.J., Newman, J. and Scott, C. Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminosarum bv. viciae 3841. PLoS One 13 (2018) e0192736. [PMID: 29425231]
3. Esquirol, L., Peat, T.S., Wilding, M., Liu, J.W., French, N.G., Hartley, C.J., Onagi, H., Nebl, T., Easton, C.J., Newman, J. and Scott, C. An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. J. Biol. Chem 293 (2018) 7880-7891. [PMID: 29523689]
Accepted name: (S)-N-acetyl-1-phenylethylamine hydrolase
Reaction: N-acetylphenylethylamine + H2O = phenylethylamine + acetate
Other name: (S)-N-acetyl-1-phenylethylamine amidohydrolase
Systematic name: (S)-N-acetylphenylethylamine:H2O hydrolase
Comments: Inhibited by phenylmethanesulfonyl fluoride. Some related acetylated compounds are hydrolysed with variable enantiomeric selectivities.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 192230-94-7
References:
1. Brunella, A., Graf, M., Kittelmann, M., Lauma, K. and Ghisalba, O. Production, purification, and characterization of a highly enantioselective (S)-N-acetyl-1-phenylethyl amidohydrolase from Rhodococcus. Appl. Microbiol. Biotechnol. 47 (1997) 515-520.
Accepted name: mandelamide amidase
Reaction: (R)-mandelamide + H2O = (R)-mandelate + NH3
Glossary: (R)-mandelate = (R)-2-hydroxy-2-phenylacetate
Other name(s): Pseudomonas mandelamide hydrolase
Systematic name: mandelamide hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yamamoto, K., Oishi, K., Fujimatsu, I. and Komatsu, K. Production of R-(–)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750. Appl. Environ. Microbiol. 57 (1991) 3028-3032. [PMID: 1660699]
Accepted name: N-carbamoyl-L-amino-acid hydrolase
Reaction: an N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O = an L-2-amino acid + NH3 + CO2
Other name(s): N-carbamyl L-amino acid amidohydrolase; N-carbamoyl-L-amino acid amidohydrolase; L-N-carbamoylase; N-carbamoylase (ambiguous)
Systematic name: N-carbamoyl-L-amino-acid amidohydrolase
Comments: This enzyme, along with EC 3.5.1.77 (N-carbamoyl-D-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [3]. The enzyme from Alcaligenes xylosoxidans has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan. The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyse N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents [2]. The enzyme is inactive on derivatives of D-amino acids. In addition to N-carbamoyl L-amino acids, the enzyme can also hydrolyse formyl and acetyl derivatives to varying degrees [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Ogawa, J., Miyake, H. and Shimizu, S. Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans. Appl. Microbiol. Biotechnol. 43 (1995) 1039-1043. [PMID: 8590654]
2. Martínez-Rodríguez, S., Clemente-Jiménez, J.M., Rodríguez-Vico, F. and Las Heras-Vázquez, F.J. Molecular cloning and biochemical characterization of L-N-carbamoylase from Sinorhizobium meliloti CECT4114. J. Mol. Microbiol. Biotechnol. 9 (2005) 16-25. [PMID: 16254442]
3. Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559-563. [PMID: 11849938]
Accepted name: peptide deformylase
Reaction: formyl-L-methionyl peptide + H2O = formate + methionyl peptide
Systematic name: formyl-L-methionyl peptide amidohydrolase
Comments: Requires iron(II). Also requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Differs in substrate specifity from EC 3.5.1.27 (N-formylmethionylaminoacyl-tRNA deformylase) and EC 3.5.1.31 (formylmethionine deformylase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 369636-51-1
References:
1. Adams, J.M. On the release of the formyl group from nascent protein. J. Mol. Biol. 33 (1968) 571-589. [PMID: 4973445]
2. Mazel, D., Pochet, S. and Marliere, P. Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation. EMBO J. 13 (1994) 914-923. [PMID: 8112305]
3. Chan, M.K., Gong, W., Rajagopalan, P.T.R., Hao, B., Tsai, C.M. and Pei, D. Crystal structure of the Escherichia coli peptide deformylase. Biochemistry 36 (1997) 13904-13909. [PMID: 9374869]
4. Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A.F.V. Structure of peptide deformylase and identification of the substrate binding site. J. Biol. Chem. 273 (1998) 11413-11416. [PMID: 9565550]
5. Becker, A., Schlichting, I., Kabsch, W., Groche, D., Schultz, S. and Wagner, A.F. Iron center, substrate recognition, and mechanism of peptide deformylase. Nat. Struct. Biol. 5 (1998) 1053-1058. [PMID: 9846875]
6. Rajagopalan, P.T.R., Yu, X.C. and Pei, D. Peptide deformylase: a new type of mononuclear iron protein. J. Am. Chem. Soc. 119 (1997) 12418-12419.
7. Groche, D., Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A.F.V. Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site. Biochem. Biophys. Res. Commun. 246 (1998) 342-346. [PMID: 9610360]
8. Rajagopalan, P.T.R., Grimme, S. and Pei, D. Characterization of cobalt(II)-substituted peptide deformylase: function of the metal ion and the catalytic residue Glu-133. Biochemistry 39 (2000) 779-790. [PMID: 10651644]
9. Hu, Y.J., Wei, Y., Zhou, Y., Rajagopalan, P.T.R. and Pei, D. Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library. Biochemistry 38 (1999) 643-650. [PMID: 9888804]
10. Ragasu, S., Mouchet, P., Lazennec, C., Dive, V. and Meinnel, T. Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin. J. Mol. Biol. 289 (1999) 1445-1457. [PMID: 10373378]
11. Giglione, C., Pierre, M. and Meinnel, T. Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents. Mol. Microbiol. 36 (2000) 1197-1205. [PMID: 10931273]
12. Pei, D. Peptide deformylase: a target for novel antibiotics? Emerging Therapeutic Targets 5 (2001) 23-40.
Accepted name: N-acetylglucosaminylphosphatidylinositol deacetylase
Reaction: 6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
For diagram click here.
Other name(s): N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase; N-acetylglucosaminylphosphatidylinositol de-N-acetylase; GlcNAc-PI de-N-acetylase; GlcNAc-PI deacetylase; acetylglucosaminylphosphatidylinositol deacetylase
Systematic name: 6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol acetylhydrolase
Comments: Involved in the second step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. The enzyme appears to be composed of a single subunit (PIG-L in mammalian cells and GPI12 in yeast). In some species, the long-chain sn-1-acyl group of the phosphatidyl group is replaced by a long-chain alkyl or alk-1-enyl group.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122191-30-4
References:
1. Doering, T.L., Masteron, W.J., Englund, P.T. and Hart, G.W. Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine. J. Biol. Chem. 264 (1989) 11168-11173. [PMID: 2525555]
2. Nakamura, N., Inoue, N., Watanabe, R., Takahashi, M., Takeda, J., Stevens, V.L. and Kinoshita, T. Expression cloning of PIG-L, a candidate N-acetylglucosaminyl-phosphatidylinositol deacetylase. J. Biol. Chem. 272 (1997) 15834-15840. [PMID: 9188481]
3. Watanabe, R., Ohishi, K., Maeda, Y., Nakamura, N. and Kinoshita, T. Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem. J. 339 (1999) 185-192. [PMID: 10085243]
4. Smith, T.K, Crossman, A., Borissow, C.N., Paterson, M.J., Dix, A., Brimacombe, J.S. and Ferguson, M.A.J. Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors. EMBO J. 20 (2001) 3322-3332. [PMID: 11432820]
Accepted name: adenosylcobinamide hydrolase
Reaction: adenosylcobinamide + H2O = adenosylcobyric acid + (R)-1-aminopropan-2-ol
For diagram click here.
Other name(s): CbiZ; AdoCbi amidohydrolase
Systematic name: adenosylcobinamide amidohydrolase
Comments: Involved in the salvage pathway of cobinamide in archaea. Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps. First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10, adenosylcobinamide-phosphate synthase (CbiB).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 905988-16-1
References:
1. Woodson, J.D. and Escalante-Semerena, J.C. CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 precursor cobinamide in archaea. Proc. Natl. Acad. Sci. USA 101 (2004) 3591-3596. [PMID: 14990804]
Accepted name: N-substituted formamide deformylase
Reaction: N-benzylformamide + H2O = formate + benzylamine
For diagram click here.
Other name(s): NfdA
Systematic name: N-benzylformamide amidohydrolase
Comments: Zinc is a cofactor. While N-benzylformamide is the best substrate, the enzyme from Arthrobacter pascens can also act on the N-substituted formamides N-butylformamide, N-allylformamide, N-[2-(cyclohex-1-enyl)ethyl]formamide and N-(1-phenylethyl)formamide, but much more slowly. Amides of other acids do not act as substrates.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 115299-95-1
References:
1. Fukatsu, H., Hashimoto, Y., Goda, M., Higashibata, H. and Kobayashi, M. Amine-synthesizing enzyme N-substituted formamide deformylase: screening, purification, characterization, and gene cloning. Proc. Natl. Acad. Sci. USA 101 (2004) 13726-13731. [PMID: 15358859]
Accepted name: pantetheine hydrolase
Reaction: (R)-pantetheine + H2O = (R)-pantothenate + 2-aminoethanethiol
Other name(s): pantetheinase; vanin; vanin-1
Systematic name: (R)-pantetheine amidohydrolase
Comments: The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol, a potent anti-oxidant [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 56093-18-6
References:
1. Duprè, S. and Cavallini, D. Purification and properties of pantetheinase from horse kidney. Methods Enzymol. 62 (1979) 262-267. [PMID: 440106]
2. Duprè, S., Chiaraluce, R., Nardini, M., Cannella, C., Ricci, G. and Cavallini, D. Continuous spectrophotometric assay of pantetheinase activity. Anal. Biochem. 142 (1984) 175-181. [PMID: 6549111]
3. Maras, B., Barra, D., Duprè, S. and Pitari, G. Is pantetheinase the actual identity of mouse and human vanin-1 proteins? FEBS Lett. 461 (1999) 149-152. [PMID: 10567687]
4. Aurrand-Lions, M., Galland, F., Bazin, H., Zakharyev, V.M., Imhof, B.A. and Naquet, P. Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing. Immunity 5 (1996) 391-405. [PMID: 8934567]
5. Pitari, G., Malergue, F., Martin, F., Philippe, J.M., Massucci, M.T., Chabret, C., Maras, B., Dupre, S., Naquet, P. and Galland, F. Pantetheinase activity of membrane-bound vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice. FEBS Lett. 483 (2000) 149-154. [PMID: 11042271]
6. Martin, F., Malergue, F., Pitari, G., Philippe, J.M., Philips, S., Chabret, C., Granjeaud, S., Mattei, M.G., Mungall, A.J., Naquet, P. and Galland, F. Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes. Immunogenetics 53 (2001) 296-306. [PMID: 11491533]
7. Pace, H.C. and Brenner, C. The nitrilase superfamily: classification, structure and function. Genome Biol. 2 (2001) 0001.1-001.9. [PMID: 11380987]
Accepted name: glutaryl-7-aminocephalosporanic-acid acylase
Reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate
For diagram click here.
Other name(s): 7β-(4-carboxybutanamido)cephalosporanic acid acylase; cephalosporin C acylase; glutaryl-7-ACA acylase; CA; GCA; GA; cephalosporin acylase; glutaryl-7-aminocephalosporanic acid acylase; GL-7-ACA acylase
Systematic name: (7R)-7-(4-carboxybutanamido)cephalosporanate amidohydrolase
Comments: Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. It reacts only weakly with cephalosporin C.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 56645-46-6
References:
1. Ishii, Y., Saito, Y., Fujimura, T., Sasaki, H., Noguchi, Y., Yamada, H., Niwa, M. and Shimomura, K. High-level production, chemical modification and site-directed mutagenesis of a cephalosporin C acylase from Pseudomonas strain N176. Eur. J. Biochem. 230 (1995) 773-778. [PMID: 7607251]
2. Kinoshita, T., Tada, T., Saito, Y., Ishii, Y., Sato, A. and Murata, M. Crystallization and preliminary X-ray analysis of cephalosporin C acylase from Pseudomonas sp. strain N176. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 458-459. [PMID: 10739919]
3. Monti, D., Carrea, G., Riva, S., Baldaro, E. and Frare, G. Characterization of an industrial biocatalyst: immobilized glutaryl-7-ACA acylase. Biotechnol. Bioeng. 70 (2000) 239-244. [PMID: 10972935]
4. Kwon, T.H., Rhee, S., Lee, Y.S., Park, S.S. and Kim, K.H. Crystallization and preliminary X-ray diffraction analysis of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas sp. GK16. J. Struct. Biol. 131 (2000) 79-81. [PMID: 10945972]
5. Kim, Y., Yoon, K.-H., Khang, Y., Turley, S. and Hol, W.G.J. The 2.0 Å crystal structure of cephalosporin acylase. Structure Fold Des. 8 (2000) 1059-1068. [PMID: 11080627]
6. Huang, X., Zeng, R., Ding, X., Mao, X., Ding, Y., Rao, Z., Xie, Y., Jiang, W. and Zhao, G. Affinity alkylation of the Trp-B4 residue of the β-subunit of the glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp. 130. J. Biol. Chem. 277 (2002) 10256-10264. [PMID: 11782466]
7. Kim, J.K., Yang, I.S., Rhee, S., Dauter, Z., Lee, Y.S., Park, S.S. and Kim, K.H. Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation. Biochemistry 42 (2003) 4084-4093. [PMID: 12680762]
Accepted name: γ-glutamyl-γ-aminobutyrate hydrolase
Reaction: 4-(γ-L-glutamylamino)butanoate + H2O = 4-aminobutanoate + L-glutamate
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Other name(s): γ-glutamyl-GABA hydrolase; PuuD; YcjL; 4-(γ-glutamylamino)butanoate amidohydrolase
Systematic name: 4-(γ-L-glutamylamino)butanoate amidohydrolase
Comments: Forms part of a putrescine-utilizing pathway in Escherichia coli, in which it has been hypothesized that putrescine is first glutamylated to form γ-glutamylputrescine, which is oxidized to 4-(γ-glutamylamino)butanal and then to 4-(γ-glutamylamino)butanoate. The enzyme can also catalyse the reactions of EC 3.5.1.35 (D-glutaminase) and EC 3.5.1.65 (theanine hydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kurihara, S., Oda, S., Kato, K., Kim, H.G., Koyanagi, T., Kumagai, H. and Suzuki, H. A novel putrescine utilization pathway involves γ-glutamylated intermediates of Escherichia coli K-12. J. Biol. Chem. 280 (2005) 4602-4608. [PMID: 15590624]
Accepted name: N-malonylurea hydrolase
Reaction: 3-oxo-3-ureidopropanoate + H2O = malonate + urea
For diagram, click here
Other name(s): ureidomalonase
Systematic name: 3-oxo-3-ureidopropanoate amidohydrolase (urea- and malonate-forming)
Comments: Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.2.1 (barbiturase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 368888-22-6
References:
1. Soong, C.L., Ogawa, J. and Shimizu, S. Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase. Biochem. Biophys. Res. Commun. 286 (2001) 222-226. [PMID: 11485332]
2. Soong, C.L., Ogawa, J., Sakuradani, E. and Shimizu, S. Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism. J. Biol. Chem. 277 (2002) 7051-7058. [PMID: 11748240]
Accepted name: succinylglutamate desuccinylase
Reaction: N-succinyl-L-glutamate + H2O = succinate + L-glutamate
For diagram, click here
Other name(s): N2-succinylglutamate desuccinylase; SGDS; AstE
Systematic name: N-succinyl-L-glutamate amidohydrolase
Comments: Requires Co2+ for maximal activity [1]. N2-Acetylglutamate is not a substrate. This is the final enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 99676-40-1
References:
1. Vander Wauven, C. and Stalon, V. Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia. J. Bacteriol. 164 (1985) 882-886. [PMID: 2865249]
2. Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 50 (1986) 314-352. [PMID: 3534538]
3. Itoh, Y. Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa. J. Bacteriol. 179 (1997) 7280-7290. [PMID: 9393691]
4. Schneider, B.L., Kiupakis, A.K. and Reitzer, L.J. Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J. Bacteriol. 180 (1998) 4278-4286. [PMID: 9696779]
Accepted name: acyl-homoserine-lactone acylase
Reaction: an N-acyl-L-homoserine lactone + H2O = L-homoserine lactone + a carboxylate
Other name(s): acyl-homoserine lactone acylase; AHL-acylase; AiiD; N-acyl-homoserine lactone acylase; PA2385 protein; quorum-quenching AHL acylase; quorum-quenching enzyme; PvdQ; QuiP
Systematic name: N-acyl-L-homoserine-lactone amidohydrolase
Comments: Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes. Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL-signalling and the expression of virulence genes in quorum-sensing bacteria. This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine lactone ring of AHL-dependent quorum-sensing signal molecules. It has broad specificity for AHLs with side changes ranging in length from 11 to 14 carbons. Substituents at the 3′-position, as found in N-(3-oxododecanoyl)-L-homoserine lactone, do not affect this activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Sio, C.F., Otten, L.G., Cool, R.H., Diggle, S.P., Braun, P.G., Bos, R., Daykin, M., Cámara, M., Williams, P. and Quax, W.J. Quorum quenching by an N-acyl-homoserine lactone acylase from Pseudomonas aeruginosa PAO1. Infect. Immun. 74 (2006) 1673-1682. [PMID: 16495538]
2. Lin, Y.H., Xu, J.L., Hu, J., Wang, L.H., Ong, S.L., Leadbetter, J.R. and Zhang, L.H. Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes. Mol. Microbiol. 47 (2003) 849-860. [PMID: 12535081]
Accepted name: histone deacetylase
Reaction: Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
Other name(s): HDAC
Systematic name: histone amidohydrolase
Comments: A class of enzymes that remove acetyl groups from N6-acetyl-lysine residues on a histone. The reaction of this enzyme is opposite to that of EC 2.3.1.48, histone acetyltransferase. Histone deacetylases (HDACs) can be organized into three classes, HDAC1, HDAC2 and HDAC3, depending on sequence similarity and domain organization. Histone acetylation plays an important role in regulation of gene expression. In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation [4]. May be identical to EC 3.5.1.17, acyl-lysine deacylase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Krieger, D.E., Levine, R., Merrifield, R.B., Vidali, G. and Allfrey, V.G. Chemical studies of histone acetylation. Substrate specificity of a histone deacetylase from calf thymus nuclei. J. Biol. Chem. 249 (1974) 332-334. [PMID: 4855628]
2. Sanchez del Pino, M.M., Lopez-Rodas, G., Sendra, R. and Tordera, V. Properties of the yeast nuclear histone deacetylase. Biochem. J. 303 (1994) 723-729. [PMID: 7980438]
3. Ouaissi, M. and Ouaissi, A. Histone deacetylase enzymes as potential drug targets in cancer and parasitic diseases. J. Biomed. Biotechnol. 2006 (2006) 13474 only. [PMID: 16883049]
4. Song, Y.M., Kim, Y.S., Kim, D., Lee, D.S. and Kwon, H.J. Cloning, expression, and biochemical characterization of a new histone deacetylase-like protein from Thermus caldophilus GK24. Biochem. Biophys. Res. Commun. 361 (2007) 55-61. [PMID: 17632079]
5. Finnin, M.S., Donigian, J.R., Cohen, A., Richon, V.M., Rifkind, R.A., Marks, P.A., Breslow, R. and Pavletich, N.P. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401 (1999) 188-193. [PMID: 10490031]
6. Phiel, C.J., Zhang, F., Huang, E.Y., Guenther, M.G., Lazar, M.A. and Klein, P.S. Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. J. Biol. Chem. 276 (2001) 36734-36741. [PMID: 11473107]
7. de Ruijter, A.J., van Gennip, A.H., Caron, H.N., Kemp, S. and van Kuilenburg, A.B. Histone deacetylases (HDACs): characterization of the classical HDAC family. Biochem. J. 370 (2003) 737-749. [PMID: 12429021]
Accepted name: fatty acid amide hydrolase
Reaction: (1) anandamide + H2O = arachidonic acid + ethanolamine
(2) oleamide + H2O = oleic acid + NH3
Glossary: anandamide = (5Z,8Z,11Z,14Z)-N-(2-hydroxyethyl)icosa-5,8,11,14-tetraenamide
Other name(s): FAAH; oleamide hydrolase; anandamide amidohydrolase
Systematic name: fatty acylamide amidohydrolase
Comments: Integral membrane protein, the enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide, occurs in mammalia.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Boger, D.L., Fecik, R.A., Patterson, J.E., Miyauchi, H., Patricelli, M.P. and Cravatt, B.F. Fatty acid amide hydrolase substrate specificity. Bioorg. Med. Chem. Lett. 10 (2000) 2613-2616. [PMID: 11128635]
2. Patricelli, M.P., Lashuel, H.A., Giang, D.K., Kelly, J.W. and Cravatt, B.F. Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization. Biochemistry 37 (1998) 15177-15187. [PMID: 9790682]
3. Patricelli, M.P. and Cravatt, B.F. Characterization and manipulation of the acyl chain selectivity of fatty acid amide hydrolase. Biochemistry 40 (2001) 6107-6115. [PMID: 11352748]
Accepted name: (R)-amidase
Reaction: (1) (R)-piperazine-2-carboxamide + H2O = (R)-piperazine-2-carboxylate + NH3
(2) β-alaninamide + H2O = β-alanine + NH3
Other name(s): R-stereospecific amidase; R-amidase
Systematic name: (R)-piperazine-2-carboxamide amidohydrolase
Comments: In addition (R)-piperidine-3-carboxamide is hydrolysed to (R)-piperidine-3-carboxylic acid and NH3, and (R)-N-tert-butylpiperazine-2-carboxamide is hydrolysed to (R)-piperazine-2-carboxylic acid and tert-butylamine with lower activity. The enzyme does not act on the other amide substrates which are hydrolysed by EC 3.5.1.4 (amidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Komeda, H., Harada, H., Washika, S., Sakamoto, T., Ueda, M. and Asano, Y. A novel R-stereoselective amidase from Pseudomonas sp. MCI3434 acting on piperazine-2-tert-butylcarboxamide. Eur. J. Biochem. 271 (2004) 1580-1590. [PMID: 15066183]
Accepted name: L-proline amide hydrolase
Reaction: (1) (S)-piperidine-2-carboxamide + H2O = (S)-piperidine-2-carboxylate + NH3
(2) L-prolinamide + H2O = L-proline + NH3
Glossary: L-pipecolate = piperidine-2-carboxylate
Other name(s): S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase; LaaA; L-amino acid amidase
Systematic name: (S)-piperidine-2-carboxamide amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Komeda, H., Harada, H., Washika, S., Sakamoto, T., Ueda, M. and Asano, Y. S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase from Pseudomonas azotoformans IAM 1603 is a novel L-amino acid amidase. Eur. J. Biochem. 271 (2004) 1465-1475. [PMID: 15066172]
Accepted name: 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase
Reaction: 2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + formate
Other name(s): ArfB
Systematic name: 2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one amidohydrolase
Comments: The enzyme catalyses the second step in archaeal riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin biosynthesis. The first step is catalysed by EC 3.5.4.29 (GTP cyclohydrolase IIa). The bacterial enzyme, EC 3.5.4.25 (GTP cyclohydrolase II) catalyses both reactions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Grochowski, L.L., Xu, H. and White, R.H. An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin. Biochemistry 48 (2009) 4181-4188. [PMID: 19309161]
Accepted name: N-acetyl-1D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase
Reaction: 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol + H2O = 1-O-(2-amino-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol + acetate
For diagram of reaction click here
Glossary: mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol
Other name(s): MshB
Systematic name: 1-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol acetylhydrolase
Comments: This enzyme is considered the key enzyme and rate limiting step in the mycothiol biosynthesis pathway [1]. In addition to acetylase activity, the enzyme possesses weak activity of EC 3.5.1.115, mycothiol S-conjugate amidase, and shares sequence similarity with that enzyme [2]. The enzyme requires a divalent transition metal ion for activity, believed to be Zn2+ [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Rawat, M., Kovacevic, S., Billman-Jacobe, H. and Av-Gay, Y. Inactivation of mshB, a key gene in the mycothiol biosynthesis pathway in Mycobacterium smegmatis. Microbiology 149 (2003) 1341-1349. [PMID: 12724395]
2. Newton, G.L., Av-Gay, Y. and Fahey, R.C. N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis. J. Bacteriol. 182 (2000) 6958-6963. [PMID: 11092856]
3. Maynes, J.T., Garen, C., Cherney, M.M., Newton, G., Arad, D., Av-Gay, Y., Fahey, R.C. and James, M.N. The crystal structure of 1-D-myo-inosityl 2-acetamido-2-deoxy-α-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold. J. Biol. Chem. 278 (2003) 47166-47170. [PMID: 12958317]
Accepted name: peptidoglycan-N-acetylglucosamine deacetylase
Reaction: peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate
Other name(s): HP310; PgdA; SpPgdA; BC1960; peptidoglycan deacetylase; N-acetylglucosamine deacetylase; peptidoglycan GlcNAc deacetylase; peptidoglycan N-acetylglucosamine deacetylase; PG N-deacetylase
Systematic name: peptidoglycan-N-acetylglucosamine amidohydrolase
Comments: Modification of peptidoglycan by N-deacetylation is an important factor in virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis [4-6]. The enzyme from Streptococcus pneumoniae is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Psylinakis, E., Boneca, I.G., Mavromatis, K., Deli, A., Hayhurst, E., Foster, S.J., Varum, K.M. and Bouriotis, V. Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis. J. Biol. Chem. 280 (2005) 30856-30863. [PMID: 15961396]
2. Tsalafouta, A., Psylinakis, E., Kapetaniou, E.G., Kotsifaki, D., Deli, A., Roidis, A., Bouriotis, V. and Kokkinidis, M. Purification, crystallization and preliminary X-ray analysis of the peptidoglycan N-acetylglucosamine deacetylase BC1960 from Bacillus cereus in the presence of its substrate (GlcNAc)6. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 203-205. [PMID: 18323609]
3. Blair, D.E., Schuttelkopf, A.W., MacRae, J.I. and van Aalten, D.M. Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor. Proc. Natl. Acad. Sci. USA 102 (2005) 15429-15434. [PMID: 16221761]
4. Wang, G., Olczak, A., Forsberg, L.S. and Maier, R.J. Oxidative stress-induced peptidoglycan deacetylase in Helicobacter pylori. J. Biol. Chem. 284 (2009) 6790-6800. [PMID: 19147492]
5. Popowska, M., Kusio, M., Szymanska, P. and Markiewicz, Z. Inactivation of the wall-associated de-N-acetylase (PgdA) of Listeria monocytogenes results in greater susceptibility of the cells to induced autolysis. J Microbiol Biotechnol 19 (2009) 932-945. [PMID: 19809250]
6. Fittipaldi, N., Sekizaki, T., Takamatsu, D., de la Cruz Domínguez-Punaro, M., Harel, J., Bui, N.K., Vollmer, W. and Gottschalk, M. Significant contribution of the pgdA gene to the virulence of Streptococcus suis. Mol. Microbiol. 70 (2008) 1120-1135. [PMID: 18990186]
Accepted name: chitin disaccharide deacetylase
Reaction: N,N′-diacetylchitobiose + H2O = N-acetyl-β-D-glucosaminyl-(1→4)-D-glucosamine + acetate
Other name(s): chitobiose amidohydolase; COD; chitin oligosaccharide deacetylase; chitin oligosaccharide amidohydolase
Systematic name: 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]-2-deoxy-D-glucopyranose acetylhydrolase
Comments: Chitin oligosaccharide deacetylase is a key enzyme in the chitin catabolic cascade of chitinolytic Vibrio strains. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio parahaemolyticus [2]. In contrast to EC 3.5.1.41 (chitin deacetylase) this enzyme is specific for the chitin disaccharide [1,3]. It also deacetylates the chitin trisaccharide with lower efficiency [3]. No activity with higher polymers of GlcNAc [1,3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kadokura, K., Rokutani, A., Yamamoto, M., Ikegami, T., Sugita, H., Itoi, S., Hakamata, W., Oku, T. and Nishio, T. Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin. Appl. Microbiol. Biotechnol. 75 (2007) 357-365. [PMID: 17334758]
2. Hirano, T., Kadokura, K., Ikegami, T., Shigeta, Y., Kumaki, Y., Hakamata, W., Oku, T. and Nishio, T. Heterodisaccharide 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a specific inducer of chitinolytic enzyme production in Vibrios harboring chitin oligosaccharide deacetylase genes. Glycobiology 19 (2009) 1046-1053. [PMID: 19553519]
3. Ohishi, K., Yamagishi, M., Ohta, T., Motosugi, M., Izumida, H., Sano, H., Adachi, K., Miwa, T. Purification and properties of two deacetylases produced by Vibrio alginolyticus H-8. Biosci. Biotechnol. Biochem. 61 (1997) 1113-1117.
4. Ohishi, K., Murase, K., Ohta, T. and Etoh, H. Cloning and sequencing of the deacetylase gene from Vibrio alginolyticus H-8. J. Biosci. Bioeng. 90 (2000) 561-563. [PMID: 16232910]
Accepted name: N-formylmaleamate deformylase
Reaction: N-formylmaleamic acid + H2O = maleamate + formate
Other name(s): NicD
Systematic name: N-formylmaleamic acid amidohydrolase
Comments: The reaction is involved in the aerobic catabolism of nicotinic acid.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Jimenez, J.I., Canales, A., Jimenez-Barbero, J., Ginalski, K., Rychlewski, L., Garcia, J.L. and Diaz, E. Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440. Proc. Natl. Acad. Sci. USA 105 (2008) 11329-11334. [PMID: 18678916]
Accepted name: maleamate amidohydrolase
Reaction: maleamate + H2O = maleate + NH3
Other name(s): NicF
Systematic name: maleamate amidohydrolase
Comments: The reaction is involved in the aerobic catabolism of nicotinic acid.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Jimenez, J.I., Canales, A., Jimenez-Barbero, J., Ginalski, K., Rychlewski, L., Garcia, J.L. and Diaz, E. Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440. Proc. Natl. Acad. Sci. USA 105 (2008) 11329-11334. [PMID: 18678916]
Accepted name: UDP-3-O-acyl-N-acetylglucosamine deacetylase
Reaction: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-α-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine + acetate
For diagram of reaction click here
Other name(s): LpxC protein; LpxC enzyme; LpxC deacetylase; deacetylase LpxC; UDP-3-O-acyl-GlcNAc deacetylase; UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase; UDP-(3-O-acyl)-N-acetylglucosamine deacetylase; UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase; UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase; UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine amidohydrolase
Systematic name: UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-α-D-glucosamine amidohydrolase
Comments: A zinc protein. The enzyme catalyses a committed step in the biosynthesis of lipid A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Hernick, M., Gennadios, H.A., Whittington, D.A., Rusche, K.M., Christianson, D.W. and Fierke, C.A. UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism. J. Biol. Chem. 280 (2005) 16969-16978. [PMID: 15705580]
2. Jackman, J.E., Raetz, C.R. and Fierke, C.A. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme. Biochemistry 38 (1999) 1902-1911. [PMID: 10026271]
3. Hyland, S.A., Eveland, S.S. and Anderson, M.S. Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway. J. Bacteriol. 179 (1997) 2029-2037. [PMID: 9068651]
4. Wang, W., Maniar, M., Jain, R., Jacobs, J., Trias, J. and Yuan, Z. A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase. Anal. Biochem. 290 (2001) 338-346. [PMID: 11237337]
5. Whittington, D.A., Rusche, K.M., Shin, H., Fierke, C.A. and Christianson, D.W. Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 8146-8150. [PMID: 12819349]
6. Mochalkin, I., Knafels, J.D. and Lightle, S. Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor. Protein Sci. 17 (2008) 450-457. [PMID: 18287278]
Accepted name: sphingomyelin deacylase
Reaction: (1) an N-acyl-sphingosylphosphorylcholine + H2O = a fatty acid + sphingosylphosphorylcholine
(2) a D-glucosyl-N-acylsphingosine + H2O = a fatty acid + D-glucosyl-sphingosine
Glossary: sphingomyelin = N-acyl-sphingosylphosphorylcholine
D-glucosyl-N-acylsphingosine = glucosylceramide
Other name(s): SM deacylase; GcSM deacylase; glucosylceramide sphingomyelin deacylase; sphingomyelin glucosylceramide deacylase; SM glucosylceramide GCer deacylase; SM-GCer deacylase; SMGCer deacylase
Systematic name: N-acyl-sphingosylphosphorylcholine amidohydrolase
Comments: The enzyme is involved in the sphingolipid metabolism in the epidermis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hara, J., Higuchi, K., Okamoto, R., Kawashima, M. and Imokawa, G. High-expression of sphingomyelin deacylase is an important determinant of ceramide deficiency leading to barrier disruption in atopic dermatitis. J. Invest. Dermatol. 115 (2000) 406-413. [PMID: 10951276]
2. Higuchi, K., Hara, J., Okamoto, R., Kawashima, M. and Imokawa, G. The skin of atopic dermatitis patients contains a novel enzyme, glucosylceramide sphingomyelin deacylase, which cleaves the N-acyl linkage of sphingomyelin and glucosylceramide. Biochem. J. 350 (2000) 747-756. [PMID: 10970788]
3. Ishibashi, M., Arikawa, J., Okamoto, R., Kawashima, M., Takagi, Y., Ohguchi, K. and Imokawa, G. Abnormal expression of the novel epidermal enzyme, glucosylceramide deacylase, and the accumulation of its enzymatic reaction product, glucosylsphingosine, in the skin of patients with atopic dermatitis. Lab. Invest. 83 (2003) 397-408. [PMID: 12649340]
Accepted name: ureidoacrylate amidohydrolase
Reaction: (1) (Z)-3-ureidoacrylate + H2O = (Z)-3-aminoacrylate + CO2 + NH3 (overall reaction)
(1a) (Z)-3-ureidoacrylate + H2O = (Z)-3-aminoacrylate + carbamate
(1b) carbamate = CO2 + NH3 (spontaneous)
(2) (Z)-2-methylureidoacrylate + H2O = (Z)-2-methylaminoacrylate + CO2 + NH3 (overall reaction)
(2a) (Z)-2-methylureidoacrylate + H2O = (Z)-2-methylaminoacrylate + carbamate
(2b) carbamate = CO2 + NH3 (spontaneous)
For diagram of reaction click here.
Glossary: (Z)-3-ureidoacrylate = (2Z)-3-(carbamoylamino)prop-2-enoate
(Z)-2-methylureidoacrylate = (2Z)-3-(carbamoylamino)-2-methylprop-2-enoate
Other name(s): rutB (gene name); peroxyureidoacrylate/ureidoacrylate amidohydrolase
Systematic name: (Z)-3-ureidoacrylate amidohydrolase
Comments: The enzyme participates in the Rut pyrimidine catabolic pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kim, K.S., Pelton, J.G., Inwood, W.B., Andersen, U., Kustu, S. and Wemmer, D.E. The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems. J. Bacteriol. 192 (2010) 4089-4102. [PMID: 20400551]
Accepted name: 2-oxoglutaramate amidase
Reaction: 2-oxoglutaramate + H2O = 2-oxoglutarate + NH3
Glossary: 2-oxoglutaramate = 2-ketoglutaramate = 5-amino-2,5-dioxopentanoate
Other name(s): ω-amidase (ambiguous)
Systematic name: 5-amino-2,5-dioxopentanoate amidohydrolase
Comments: The enzyme, which is highly specific for its substrate, participates in the nicotine degradation pathway of several Gram-positive bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Cobzaru, C., Ganas, P., Mihasan, M., Schleberger, P. and Brandsch, R. Homologous gene clusters of nicotine catabolism, including a new ω-amidase for α-ketoglutaramate, in species of three genera of Gram-positive bacteria. Res. Microbiol. 162 (2011) 285-291. [PMID: 21288482]
Accepted name: 2'-N-acetylparomamine deacetylase
Reaction: 2'-N-acetylparomamine + H2O = paromamine + acetate
For diagram of reaction click here.
Glossary: paromamine = (1R)-O4-(2-amino-2-deoxy-α-D-glucopyranosyl)-2-deoxy-streptamine
Other name(s): btrD (gene name); neoL (gene name); kanN (gene name)
Systematic name: 2'-N-acetylparomamine hydrolase (acetate-forming)
Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. The enzyme from the bacterium Streptomyces fradiae can also accept 2'''-acetyl-6'''-hydroxyneomycin C as substrate, cf. EC 3.5.1.113, 2'''-acetyl-6'''-hydroxyneomycin C deacetylase [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Truman, A.W., Huang, F., Llewellyn, N.M. and Spencer, J.B. Characterization of the enzyme BtrD from Bacillus circulans and revision of its functional assignment in the biosynthesis of butirosin. Angew. Chem. Int. Ed. Engl. 46 (2007) 1462-1464. [PMID: 17226887]
2. Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem. 9 (2008) 865-869. [PMID: 18311744]
Accepted name: 2'''-acetyl-6'''-hydroxyneomycin C deacetylase
Reaction: 2'''-acetyl-6'''-deamino-6'''-hydroxyneomycin C + H2O = 6'''-deamino-6'''-hydroxyneomycin C + acetate
For diagram of reaction click here.
Other name(s): neoL (gene name)
Systematic name: 2'''-acetyl-6'''-hydroxyneomycin C hydrolase (acetate-forming)
Comments: Involved in the biosynthetic pathway of aminoglycoside antibiotics of the neomycin family. The enzyme from the bacterium Streptomyces fradiae also catalyses EC 3.5.1.112, 2'-N-acetylparomamine deacetylase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem. 9 (2008) 865-869. [PMID: 18311744]
Accepted name: N-acyl-aromatic-L-amino acid amidohydrolase
Reaction: (1) an N-acyl-aromatic-L-amino acid + H2O = an aromatic-L-amino acid + a carboxylate
(2) an N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate
Glossary: N-acetyl-L-cysteine-S-conjugate = mercapturic acid
Other name(s): aminoacylase 3; aminoacylase III; ACY3 (gene name)
Systematic name: N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)
Comments: This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It preferentially deacetylates Nα-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase. The enzyme is significantly activated by Co2+ and Ni2+ [3]. Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase and EC 3.5.1.15, aspartoacylase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Pushkin, A., Carpenito, G., Abuladze, N., Newman, D., Tsuprun, V., Ryazantsev, S., Motemoturu, S., Sassani, P., Solovieva, N., Dukkipati, R. and Kurtz, I. Structural characterization, tissue distribution, and functional expression of murine aminoacylase III. Am. J. Physiol. Cell Physiol. 286 (2004) C848-C856. [PMID: 14656720]
2. Newman, D., Abuladze, N., Scholz, K., Dekant, W., Tsuprun, V., Ryazantsev, S., Bondar, G., Sassani, P., Kurtz, I. and Pushkin, A. Specificity of aminoacylase III-mediated deacetylation of mercapturic acids. Drug Metab. Dispos. 35 (2007) 43-50. [PMID: 17012540]
3. Tsirulnikov, K., Abuladze, N., Newman, D., Ryazantsev, S., Wolak, T., Magilnick, N., Koag, M.C., Kurtz, I. and Pushkin, A. Mouse aminoacylase 3: a metalloenzyme activated by cobalt and nickel. Biochim. Biophys. Acta 1794 (2009) 1049-1057. [PMID: 19362172]
4. Hsieh, J.M., Tsirulnikov, K., Sawaya, M.R., Magilnick, N., Abuladze, N., Kurtz, I., Abramson, J. and Pushkin, A. Structures of aminoacylase 3 in complex with acetylated substrates. Proc. Natl. Acad. Sci. USA 107 (2010) 17962-17967. [PMID: 20921362]
5. Tsirulnikov, K., Abuladze, N., Bragin, A., Faull, K., Cascio, D., Damoiseaux, R., Schibler, M.J. and Pushkin, A. Inhibition of aminoacylase 3 protects rat brain cortex neuronal cells from the toxicity of 4-hydroxy-2-nonenal mercapturate and 4-hydroxy-2-nonenal. Toxicol. Appl. Pharmacol. 263 (2012) 303-314. [PMID: 22819785]
Accepted name: mycothiol S-conjugate amidase
Reaction: a mycothiol S-conjugate + H2O = an N-acetyl L-cysteine-S-conjugate + 1-O-(2-amino-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol
Glossary: mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol
N-acetyl L-cysteine-S-conjugate = mercapturic acid
Other name(s): MCA
Systematic name: mycothiol S-conjugate 1D-myo-inositol 2-amino-2-deoxy-α-D-glucopyranosyl-hydrolase
Comments: The enzyme that is found in actinomycetes is involved in the detoxification of oxidizing agents and electrophilic antibiotics. The enzyme has low activity with 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol as substrate (cf. EC 3.5.1.103, N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase) [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Newton, G.L., Av-Gay, Y. and Fahey, R.C. A novel mycothiol-dependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase. Biochemistry 39 (2000) 10739-10746. [PMID: 10978158]
2. Steffek, M., Newton, G.L., Av-Gay, Y. and Fahey, R.C. Characterization of Mycobacterium tuberculosis mycothiol S-conjugate amidase. Biochemistry 42 (2003) 12067-12076. [PMID: 14556638]
Accepted name: ureidoglycolate amidohydrolase
Reaction: (S)-ureidoglycolate + H2O = glyoxylate + 2 NH3 + CO2
For diagram of reaction click here.
Other name(s): ureidoglycolate hydrolase; UAH (gene name)
Systematic name: (S)-ureidoglycolate amidohydrolase (decarboxylating)
Comments: This plant enzyme is involved in the degradation of ureidoglycolate, an intermediate of purine degradation. Not to be confused with EC 4.3.2.3, ureidoglycolate lyase, which releases urea rather than ammonia.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Winkler, R.G., Blevins, D.G. and Randall, D.D. Ureide catabolism in soybeans. III. Ureidoglycolate amidohydrolase and allantoate amidohydrolase are activities of an allantoate degrading enzyme complex. Plant Physiol. 86 (1988) 1084-1088. [PMID: 16666035]
2. Wells, X.E. and Lees, E.M. Ureidoglycolate amidohydrolase from developing French bean fruits (Phaseolus vulgaris [L.].). Arch. Biochem. Biophys. 287 (1991) 151-159. [PMID: 1910298]
3. Werner, A.K., Romeis, T. and Witte, C.P. Ureide catabolism in Arabidopsis thaliana and Escherichia coli. Nat. Chem. Biol. 6 (2010) 19-21. [PMID: 19935661]
Accepted name: 6-aminohexanoate-oligomer endohydrolase
Reaction: [N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
Other name(s): endo-type 6-aminohexanoate oligomer hydrolase; Ahx endo-type-oligomer hydrolase; 6-aminohexanoate oligomer hydrolase; Ahx-oligomer hydrolase; nylon hydrolase; nylon-oligomer hydrolase; NylC; nylon-6 hydrolase (ambiguous)
Systematic name: 6-aminohexanoate oligomer endoamidohydrolase
Comments: The enzyme is involved in degradation of nylon-6 oligomers. It degrades linear or cyclic oligomers of poly(6-aminohexanoate) with a degree of polymerization greater than three (n-> 3) by endo-type cleavage, to oligomers of a length of two or more (2 ≤ x-< n). It shows negligible activity with N-(6-aminohexanoyl)-6-aminohexanoate (cf. EC 3.5.1.46, 6-aminohexanoate-oligomer exo hydrolase) or with 1,8-diazacyclotetradecane-2,9-dione (cf. EC 3.5.2.12, 6-aminohexanoate-cyclic-dimer hydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kakudo, S., Negoro, S., Urabe, I. and Okada, H. Nylon oligomer degradation gene, nylC, on plasmid pOAD2 from a Flavobacterium strain encodes endo-type 6-aminohexanoate oligomer hydrolase: purification and characterization of the nylC gene product. Appl. Environ. Microbiol. 59 (1993) 3978-3980. [PMID: 8285701]
2. Yasuhira, K., Tanaka, Y., Shibata, H., Kawashima, Y., Ohara, A., Kato, D., Takeo, M. and Negoro, S. 6-Aminohexanoate oligomer hydrolases from the alkalophilic bacteria Agromyces sp. strain KY5R and Kocuria sp. strain KY2. Appl. Environ. Microbiol. 73 (2007) 7099-7102. [PMID: 17827307]
3. Negoro, S., Shibata, N., Tanaka, Y., Yasuhira, K., Shibata, H., Hashimoto, H., Lee, Y.H., Oshima, S., Santa, R., Oshima, S., Mochiji, K., Goto, Y., Ikegami, T., Nagai, K., Kato, D., Takeo, M. and Higuchi, Y. Three-dimensional structure of nylon hydrolase and mechanism of nylon-6 hydrolysis. J. Biol. Chem. 287 (2012) 5079-5090. [PMID: 22187439]
Accepted name: γ-glutamyl hercynylcysteine S-oxide hydrolase
Reaction: γ-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O = S-(hercyn-2-yl)-L-cysteine S-oxide + L-glutamate
For diagram of reaction click here.
Glossary: hercynine = Nα,Nα,Nα-trimethyl-L-histidine = 3-(1H-imidazol-5-yl)-2-(trimethylamino)propanoate
S-(hercyn-2-yl)-L-cysteine S-oxide = S-(N,N,N-trimethyl-L-histidin-2-yl)-L-cysteine S-oxide
Other name(s): EgtC
Systematic name: γ-glutamyl-S-(hercyn-2-yl)cysteine S-oxide amidohydrolase
Comments: The enzyme is part of the biosynthesis pathway of ergothioneine in mycobacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Seebeck, F.P. In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. J. Am. Chem. Soc. 132 (2010) 6632-6633. [PMID: 20420449]
Accepted name: Pup amidohydrolase
Reaction: [prokaryotic ubiquitin-like protein]-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + NH3
Other name(s): dop (gene name); Pup deamidase; depupylase/deamidase; DPUP; depupylase
Systematic name: [prokaryotic ubiquitin-like protein]-L-glutamine amidohydrolase
Comments: The enzyme has been characterized from the bacterium Mycobacterium tuberculosis. It catalyses the hydrolysis of the amido group of the C-terminal glutamine of prokaryotic ubiquitin-like protein (Pup), thus activating it for ligation to target proteins, a process catalysed by EC 6.3.1.19, prokaryotic ubiquitin-like protein ligase. The reaction requires ATP as cofactor but not its hydrolysis.The enzyme also catalyses the hydrolytic cleavage of the bond formed by the ligase, between an ε-amino group of a lysine residue of the target protein and the γ-carboxylate of the C-terminal glutamate of the prokaryotic ubiquitin-like protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Striebel, F., Imkamp, F., Sutter, M., Steiner, M., Mamedov, A. and Weber-Ban, E. Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat. Struct. Mol. Biol. 16 (2009) 647-651. [PMID: 19448618]
2. Burns, K.E., Cerda-Maira, F.A., Wang, T., Li, H., Bishai, W.R. and Darwin, K.H. "Depupylation" of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates. Mol. Cell 39 (2010) 821-827. [PMID: 20705495]
3. Striebel, F., Imkamp, F., Özcelik, D. and Weber-Ban, E. Pupylation as a signal for proteasomal degradation in bacteria. Biochim. Biophys. Acta 1843 (2014) 103-113. [PMID: 23557784]
[EC 3.5.1.120 Transferred entry: 2-aminomuconate deaminase (2-hydroxymuconate-forming). Now EC 3.5.99.11, 2-aminomuconate deaminase (2-hydroxymuconate-forming) (EC 3.5.1.120 created 2016, deleted 2017)]
Accepted name: protein N-terminal asparagine amidohydrolase
Reaction: N-terminal L-asparaginyl-[protein] + H2O = N-terminal L-aspartyl-[protein] + NH3
Other name(s): NTAN1 (gene name)
Systematic name: protein N-terminal asparagine amidohydrolase
Comments: This enzyme participates in the eukaryotic ubiquitin-dependent Arg/N-end rule pathway of protein degradation, promoting the turnover of intracellular proteins that initiate with Met-Asn. Following the acetylation and removal of the initiator methionine, the exposed N-terminal asparagine is deaminated, resulting in its conversion to L-aspartate. The latter serves as a substrate for EC 2.3.2.8, arginyltransferase, making the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Stewart, A.E., Arfin, S.M. and Bradshaw, R.A. Protein NH2-terminal asparagine deamidase. Isolation and characterization of a new enzyme. J. Biol. Chem. 269 (1994) 23509-23517. [PMID: 8089117]
2. Grigoryev, S., Stewart, A.E., Kwon, Y.T., Arfin, S.M., Bradshaw, R.A., Jenkins, N.A., Copeland, N.G. and Varshavsky, A. A mouse amidase specific for N-terminal asparagine. The gene, the enzyme, and their function in the N-end rule pathway. J. Biol. Chem. 271 (1996) 28521-28532. [PMID: 8910481]
3. Cantor, J.R., Stone, E.M. and Georgiou, G. Expression and biochemical characterization of the human enzyme N-terminal asparagine amidohydrolase. Biochemistry 50 (2011) 3025-3033. [PMID: 21375249]
Accepted name: protein N-terminal glutamine amidohydrolase
Reaction: N-terminal L-glutaminyl-[protein] + H2O = N-terminal L-glutamyl-[protein] + NH3
Other name(s): NTAQ1 (gene name)
Systematic name: protein N-terminal glutamine amidohydrolase
Comments: This enzyme participates in the eukaryotic ubiquitin-dependent Arg/N-end rule pathway of protein degradation, promoting the turnover of intracellular proteins that initiate with Met-Gln. Following the acetylation and removal of the initiator methionine, the exposed N-terminal glutamine is deaminated, resulting in its conversion to L-glutamate. The latter serves as a substrate for EC 2.3.2.8, arginyltransferase, making the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Wang, H., Piatkov, K.I., Brower, C.S. and Varshavsky, A. Glutamine-specific N-terminal amidase, a component of the N-end rule pathway. Mol. Cell 34 (2009) 686-695. [PMID: 19560421]
Accepted name: γ-glutamylanilide hydrolase
Reaction: N5-phenyl-L-glutamine + H2O = L-glutamate + aniline
Glossary: γ-glutamylanilide = N5-phenyl-L-glutamine
Other name(s): atdA2 (gene name)
Systematic name: N5-phenyl-L-glutamine amidohydrolase
Comments: The enzyme, characterized from the bacterium Acinetobacter sp. YAA, catalyses the opposite reaction from that catalysed by EC 6.3.1.18, γ-glutamylanilide synthase, which is part of an aniline degradation pathway. Its purpose is likely to maintain a low concentration of N5-phenyl-L-glutamine, which is potentially toxic.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Takeo, M., Ohara, A., Sakae, S., Okamoto, Y., Kitamura, C., Kato, D. and Negoro, S. Function of a glutamine synthetase-like protein in bacterial aniline oxidation via γ-glutamylanilide. J. Bacteriol. 195 (2013) 4406-4414. [PMID: 23893114]
Accepted name: protein deglycase
Reaction: (1) an Nω-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O = a [protein]-L-arginine + (R)-lactate
(2) an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + (R)-lactate
(3) an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O = a [protein]-L-cysteine + (R)-lactate
Glossary: 2-oxopropanal = methylglyoxal
Other name(s): PARK7 (gene name); DJ-1 protein; yhbO (gene name); yajL (gene name); glyoxylase III (incorrect)
Systematic name: a [protein]-L-amino acid-1-hydroxypropan-2-one hydrolase [(R)-lactate-forming]
Comments: The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively [3,4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Misra, K., Banerjee, A.B., Ray, S. and Ray, M. Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione. Biochem. J. 305 (1995) 999-1003. [PMID: 7848303]
2. Subedi, K.P., Choi, D., Kim, I., Min, B. and Park, C. Hsp31 of Escherichia coli K-12 is glyoxalase III. Mol. Microbiol. 81 (2011) 926-936. [PMID: 21696459]
3. Richarme, G., Mihoub, M., Dairou, J., Bui, L.C., Leger, T. and Lamouri, A. Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues. J. Biol. Chem. 290 (2015) 1885-1897. [PMID: 25416785]
4. Mihoub, M., Abdallah, J., Gontero, B., Dairou, J. and Richarme, G. The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal. Biochem. Biophys. Res. Commun. 463 (2015) 1305-1310. [PMID: 26102038]
5. Abdallah, J., Mihoub, M., Gautier, V. and Richarme, G. The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal. Biochem. Biophys. Res. Commun. 470 (2016) 282-286. [PMID: 26774339]
Accepted name: N2-acetyl-L-2,4-diaminobutanoate deacetylase
Reaction: (2S)-2-acetamido-4-aminobutanoate + H2O = L-2,4-diaminobutanoate + acetate
Other name(s): doeB (gene name)
Systematic name: (2S)-2-acetamido-4-aminobutanoate amidohydrolase
Comments: The enzyme, found in bacteria, has no activity with (2S)-2-acetamido-4-aminobutanoate (cf. EC 3.5.4.44, ectoine hydrolase).
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Schwibbert, K., Marin-Sanguino, A., Bagyan, I., Heidrich, G., Lentzen, G., Seitz, H., Rampp, M., Schuster, S.C., Klenk, H.P., Pfeiffer, F., Oesterhelt, D. and Kunte, H.J. A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581 T. Environ. Microbiol. 13 (2011) 1973-1994. [PMID: 20849449]
Accepted name: oxamate amidohydrolase
Reaction: oxamate + H2O = oxalate + NH3
Other name(s): HpxW
Systematic name: oxamate amidohydrolase
Comments: The enzyme has been characterized from the bacterium Klebsiella pneumoniae.
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Hicks, K.A. and Ealick, S.E. Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway. Acta Crystallogr D Struct Biol 72 (2016) 808-816. [PMID: 27303801]
Accepted name: jasmonoyl-L-amino acid hydrolase
Reaction: a jasmonoyl-L-amino acid + H2O = jasmonate + an L-amino acid
Glossary: tuberonic acid = 12-hydroxyjasmonate = {(1R,2R)-2-[(2Z)-5-hydroxypent-2-enyl]-3-oxo-cyclopentyl}acetate
jasmonate = {(1R,2R)-3-oxo-2-[(2Z)-pent-2-enyl]cyclopentyl}acetate
Other name(s): IAR3 (gene name); ILL4 (gene name); ILL6 (gene name)
Systematic name: jasmonoyl-L amino acid amidohydrolase
Comments: This entry includes a family of enzymes that recyle jasmonoyl-amino acid conjugates back to jasmonates. The enzymes from Arabidopsis thaliana have been shown to also act on 12-hydroxyjasmonoyl-L-isoleucine, generating tuberonic acid.
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Widemann, E., Miesch, L., Lugan, R., Holder, E., Heinrich, C., Aubert, Y., Miesch, M., Pinot, F. and Heitz, T. The amidohydrolases IAR3 and ILL6 contribute to jasmonoyl-isoleucine hormone turnover and generate 12-hydroxyjasmonic acid upon wounding in Arabidopsis leaves. J. Biol. Chem. 288 (2013) 31701-31714. [PMID: 24052260]
Accepted name: deaminated glutathione amidase
Reaction: N-(4-oxoglutaryl)-L-cysteinylglycine + H2O = 2-oxoglutarate + L-cysteinylglycine
Glossary: N-(4-oxoglutaryl)-L-cysteinylglycine = deaminated glutathione
Other name(s): dGSH deaminase; NIT1 (gene name)
Systematic name: N-(4-oxoglutaryl)-L-cysteinylglycine amidohydrolase
Comments: The enzyme, present in animals, fungi and bacteria, is involved in clearing cells of the toxic compound deaminated glutathione, which can be produced as an unwanted side product by several transaminases.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Peracchi, A., Veiga-da-Cunha, M., Kuhara, T., Ellens, K.W., Paczia, N., Stroobant, V., Seliga, A.K., Marlaire, S., Jaisson, S., Bommer, G.T., Sun, J., Huebner, K., Linster, C.L., Cooper, A.JL. and Van Schaftingen, E. Nit1 is a metabolite repair enzyme that hydrolyzes deaminated glutathione. Proc. Natl Acad. Sci. USA 114 (2017) E3233-E3242. [PMID: 28373563]
Accepted name: N5-(cytidine 5'-diphosphoramidyl)-L-glutamine hydrolase
Reaction: N5-(cytidine 5'-diphosphoramidyl)-L-glutamine + H2O = cytidine 5'-diphosphoramidate + L-glutamate
Other name(s): N5-(cytidine 5'-diphosphoramidyl)-L-glutamine deacylase
Systematic name: N5-(cytidine 5'-diphosphoramidyl)-L-glutamine amidohydrolase
Comments: The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium's capsular polysaccharides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Taylor, Z.W., Brown, H.A., Holden, H.M. and Raushel, F.M. Biosynthesis of nucleoside diphosphoramidates in Campylobacter jejuni. Biochemistry 56 (2017) 6079-6082. [PMID: 29023101]
Accepted name: [lysine-biosynthesis-protein LysW]-lysine/ornithine hydrolase
Reaction: (1) [lysine-biosynthesis-protein LysW]-C-terminal-γ-(L-ornithyl)-L-glutamate + H2O = [lysine-biosynthesis-protein LysW]-C-terminal-L-glutamate + L-ornithine
(2) [lysine-biosynthesis-protein LysW]-C-terminal-γ-(L-lysyl)-L-glutamate + H2O = [lysine-biosynthesis-protein LysW]-C-terminal-L-glutamate + L-lysine
Other name(s): lysK (gene name)
Systematic name: [lysine-biosynthesis-protein LysW]-C-terminal-γ-(L-ornithyl/L-lysyl)-L-glutamate amidohydrolase
Comments: The enzyme participates in an L-lysine biosynthetic pathways in certain species of archaea and bacteria. In some organisms the enzyme also catalyses the activity of EC 3.5.1.132, [amino group carrier protein]-ornithine hydrolase.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Horie, A., Tomita, T., Saiki, A., Kono, H., Taka, H., Mineki, R., Fujimura, T., Nishiyama, C., Kuzuyama, T. and Nishiyama, M. Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat. Chem. Biol. 5 (2009) 673-679. [PMID: 19620981]
2. Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277-283. [PMID: 23434852]
3. Yoshida, A., Tomita, T., Atomi, H., Kuzuyama, T. and Nishiyama, M. Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system. J. Biol. Chem. 291 (2016) 21630-21643. [PMID: 27566549]
4. Fujita, S., Cho, S.H., Yoshida, A., Hasebe, F., Tomita, T., Kuzuyama, T. and Nishiyama, M. Crystal structure of LysK, an enzyme catalyzing the last step of lysine biosynthesis in Thermus thermophilus, in complex with lysine: insight into the mechanism for recognition of the amino-group carrier protein, LysW. Biochem. Biophys. Res. Commun. 491 (2017) 409-415. [PMID: 28720495]
Accepted name: 1-carboxybiuret hydrolase
Reaction: 1-carboxybiuret + H2O = urea-1,3-dicarboxylate + NH3
For diagram of reaction click here.
Glossary: carboxybiuret = carbamoylcarbamoylcarbamic acid
Other name(s): atzEG (gene names)
Systematic name: 1-carboxybiuret amidohydrolase
Comments: The enzyme, characterized from the bacterium Pseudomonas sp. ADP, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazine herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The enzyme is a heterotetramer composed of a catalytic subunit (AtzE) and an accessory subunit (AtzG) that stabilizes the complex.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Esquirol, L., Peat, T.S., Wilding, M., Liu, J.W., French, N.G., Hartley, C.J., Onagi, H., Nebl, T., Easton, C.J., Newman, J. and Scott, C. An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. J. Biol. Chem 293 (2018) 7880-7891. [PMID: 29523689]
Accepted name: [amino group carrier protein]-ornithine hydrolase
Reaction: [amino group carrier protein]-C-terminal-γ-(L-ornithyl)-L-glutamate + H2O = [amino group carrier protein]-C-terminal-L-glutamate + L-ornithine
Other name(s): lysK (gene name)
Systematic name: [amino group carrier protein]-C-terminal-γ-L-ornithyl-L-glutamate amidohydrolase
Comments: The enzyme participates in an L-arginine biosynthetic pathways in certain species of archaea and bacteria. In all cases known so far the enzyme also catalyses the activity of EC 3.5.1.130, [amino group carrier protein]-lysine hydrolase.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:
References:
1. Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277-283. [PMID: 23434852]
2. Yoshida, A., Tomita, T., Atomi, H., Kuzuyama, T. and Nishiyama, M. Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system. J. Biol. Chem. 291 (2016) 21630-21643. [PMID: 27566549]
Accepted name: Nα-acyl-L-glutamine aminoacylase
Reaction: an Nα-acyl-L-glutamine + H2O = L-glutamine + a carboxylate
Other name(s): agaA (gene name); axillary malodor releasing enzyme; AMRE
Systematic name: Nα-acyl-L-glutamine amidohydrolase (carboxylate-forming)
Comments: Requires Zn2+. The enzyme, characterized from the bacterium Corynebacterium sp. Ax20, hydrolyses odorless Nα-acyl-L-glutamine conjugates of short- and medium-chain fatty acids, releasing axillary malodor compounds. While the enzyme is highly specific for the L-glutamine moiety, it is quite promiscuous regarding the acyl moiety. The two most common products of the enzyme's activity in axillary secretions are (2E)-3-methylhex-2-enoate and 3-hydroxy-3-methylhexanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Natsch, A., Gfeller, H., Gygax, P., Schmid, J. and Acuna, G. A specific bacterial aminoacylase cleaves odorant precursors secreted in the human axilla. J. Biol. Chem. 278 (2003) 5718-5727. [PMID: 12468539]
2. Natsch, A., Gfeller, H., Gygax, P. and Schmid, J. Isolation of a bacterial enzyme releasing axillary malodor and its use as a screening target for novel deodorant formulations. Int J Cosmet Sci 27 (2005) 115-122. [PMID: 18492161]
3. Natsch, A., Derrer, S., Flachsmann, F. and Schmid, J. A broad diversity of volatile carboxylic acids, released by a bacterial aminoacylase from axilla secretions, as candidate molecules for the determination of human-body odor type. Chem. Biodivers. 3 (2006) 1-20. [PMID: 17193210]
Accepted name: (indol-3-yl)acetyl-L-aspartate hydrolase
Reaction: (indol-3-yl)acetyl-L-aspartate + H2O = (indol-3-yl)acetate + L-aspartate
Other name(s): indole-3-acetyl-L-aspartate hydrolase; iaaspH (gene name)
Systematic name: (indol-3-yl)acetyl-L-aspartate amidohydrolase
Comments: The enzyme, isolated from the bacterium Pantoea agglomerans, is specific for its substrate and does not act efficiently on other indole-3-acetate conjugates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Chou, J.C., Kuleck, G.A., Cohen, J.D. and Mulbry, W.W. Partial purification and characterization of an inducible indole-3-acetyl-L-aspartic acid hydrolase from enterobacter agglomerans. Plant Physiol. 112 (1996) 1281-1287. [PMID: 12226446]
2. Chou, J.C., Mulbry, W.W. and Cohen, J.D. The gene for indole-3-acetyl-L-aspartic acid hydrolase from Enterobacter agglomerans: molecular cloning, nucleotide sequence, and expression in Escherichia coli. Mol. Gen. Genet. 259 (1998) 172-178. [PMID: 9747708]
Accepted name: N4-acetylcytidine amidohydrolase
Reaction: N4-acetylcytidine + H2O = cytidine + acetate
Other name(s): yqfB (gene name)
Systematic name: N4-acetylcytidine amidohydrolase
Comments: The enzyme from the bacterium Escherichia coli is one of the smallest known monomeric amidohydrolases (103-amino acids). The enzyme is active towards a wide range of N4-acylcytosines/cytidines, but is by far most active against N4-acetylcytidine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Shen, Y., Atreya, H.S., Liu, G. and Szyperski, T. G-matrix Fourier transform NOESY-based protocol for high-quality protein structure determination. J. Am. Chem. Soc. 127 (2005) 9085-9099. [PMID: 15969587]
2. Stanislauskiene, R., Laurynenas, A., Rutkiene, R., Aucynaite, A., Tauraite, D., Meskiene, R., Urbeliene, N., Kaupinis, A., Valius, M., Kaliniene, L. and Meskys, R. YqfB protein from Escherichia coli: an atypical amidohydrolase active towards N4-acylcytosine derivatives. Sci. Rep. 10 (2020) 788. [PMID: 31964920]
Accepted name: N,N'-diacetylchitobiose non-reducing end deacetylase
Reaction: N,N'-diacetylchitobiose + H2O = β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine + acetate
Other name(s): diacetylchitobiose deacetylase (ambiguous); cda (gene name)
Systematic name: N,N'-diacetylchitobiose non-reducing end acetylhydrolase
Comments: The enzyme, characterized from the archaeons Thermococcus kodakarensis and Pyrococcus horikoshii, deacetylates the non-reducing residue of N,N'-diacetylchitobiose, the end product of the archaeal chitinase, to produce β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine. This is in contrast to EC 3.5.1.105, chitin disaccharide deacetylase, which deacetylates N,N'-diacetylchitobiose at the reducing residue to produce N-acetyl-β-D-glucosaminyl-(1→4)-D-glucosamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Tanaka, T., Fukui, T., Fujiwara, S., Atomi, H. and Imanaka, T. Concerted action of diacetylchitobiose deacetylase and exo-β-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Biol. Chem. 279 (2004) 30021-30027. [PMID: 15136574]
2. Mine, S., Ikegami, T., Kawasaki, K., Nakamura, T. and Uegaki, K. Expression, refolding, and purification of active diacetylchitobiose deacetylase from Pyrococcus horikoshii. Protein Expr. Purif. 84 (2012) 265-269. [PMID: 22713621]
3. Nakamura, T., Yonezawa, Y., Tsuchiya, Y., Niiyama, M., Ida, K., Oshima, M., Morita, J. and Uegaki, K. Substrate recognition of N,N'-diacetylchitobiose deacetylase from Pyrococcus horikoshii. J. Struct. Biol. 195 (2016) S1047-8477(. [PMID: 27456364]
Accepted name: N-methylcarbamate hydrolase
Reaction: an N-methyl carbamate ester + H2O = an alcohol + methylamine + CO2
Glossary: carbaryl = N-methyl-1-naphthyl carbamate
Other name(s): mcbA (gene name); cehA (gene name); cfdJ (gene name); carbaryl hydrolase; carbofuran hydrolase
Systematic name: N-methyl carbamate ester hydrolase
Comments: The enzyme catalyses the first step in the degradation of several carbamate insecticides such as carbaryl, carbofuran, isoprocarb, propoxur, aldicarb and oxamyl. It catalyses the cleavage of the ester bond to release N-methylcarbamate, which spontaneously hydrolyses to methylamine and CO2. The enzymes from several Gram-negative bacteria were shown to be located in the periplasm.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Mulbry, W.W. and Eaton, R.W. Purification and characterization of the N-methylcarbamate hydrolase from Pseudomonas strain CRL-OK. Appl. Environ. Microbiol. 57 (1991) 3679-3682. [PMID: 1785941]
2. Hayatsu, M. and Nagata, T. Purification and characterization of carbaryl hydrolase from Blastobacter sp. strain M501. Appl. Environ. Microbiol. 59 (1993) 2121-2125. [PMID: 16348989]
3. Chapalmadugu, S. and Chaudhry, G.R. Isolation of a constitutively expressed enzyme for hydrolysis of carbaryl in Pseudomonas aeruginosa, J. Bacteriol. 175 (1993) 6711-6716. [PMID: 8407847]
4. Hayatsu, M., Mizutani, A., Hashimoto, M., Sato, K. and Hayano, K. Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100. FEMS Microbiol. Lett. 201 (2001) 99-103. [PMID: 11445174]
5. Hashimoto, M., Fukui, M., Hayano, K. and Hayatsu, M. Nucleotide sequence and genetic structure of a novel carbaryl hydrolase gene (cehA) from Rhizobium sp. strain AC100. Appl. Environ. Microbiol. 68 (2002) 1220-1227. [PMID: 11872471]
6. Zhang, Q., Liu, Y. and Liu, Y.H. Purification and characterization of a novel carbaryl hydrolase from Aspergillus niger PY168. FEMS Microbiol. Lett. 228 (2003) 39-44. [PMID: 14612234]
7. Ozturk, B., Ghequire, M., Nguyen, T.P., De Mot, R., Wattiez, R. and Springael, D. Expanded insecticide catabolic activity gained by a single nucleotide substitution in a bacterial carbamate hydrolase gene. Environ. Microbiol. 18 (2016) 4878-4887. [PMID: 27312345]
8. Kamini, Shetty, D., Trivedi, V.D., Varunjikar, M. and Phale, P.S. Compartmentalization of the carbaryl degradation pathway: molecular characterization of inducible periplasmic carbaryl hydrolase from Pseudomonas spp. Appl. Environ. Microbiol. 84 (2018) e02115-17 . [PMID: 29079626]
9. Yan, X., Jin, W., Wu, G., Jiang, W., Yang, Z., Ji, J., Qiu, J., He, J., Jiang, J. and Hong, Q. Hydrolase CehA and monooxygenase CfdC are responsible for carbofuran degradation in Sphingomonas sp. strain CDS-1. Appl. Environ. Microbiol. 84 (2018) . [PMID: 29884759]
10. Jiang, W., Gao, Q., Zhang, L., Wang, H., Zhang, M., Liu, X., Zhou, Y., Ke, Z., Wu, C., Qiu, J. and Hong, Q. Identification of the key amino acid sites of the carbofuran hydrolase CehA from a newly isolated carbofuran-degrading strain Sphingbium sp. CFD-1. Ecotoxicol Environ Saf 189 (2020) 109938. [PMID: 31759739]
Accepted name: lipoamidase
Reaction: a [lipoyl-carrier protein]-N6-[(R)-lipoyl]-L-lysine + H2O = a [lipoyl-carrier protein]-L-lysine + (R)-lipoate
Other name(s): pyruvate dehydrogenase inactivase
Systematic name: [lipoyl-carrier protein]-N6-[(R)-lipoyl]-L-lysine amidohydrolase
Comments: The enzyme, characterized from the bacterium Enterococcus faecalis, is a member of the Ser-Ser-Lys triad amidohydrolase family. cf. EC 2.3.1.313, NAD-dependent lipoamidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Reed, L.J., Koike, M., Levitch, M.E., Leach, F.R. Studies on the nature and reactions of protein-bound lipoic acid. J. Biol. Chem. 232 (1958) 143-158. [PMID: 13549405]
2. Suzuki, K, Reed L.J. Lipoamidase. J. Biol. Chem. 238 (1963) 4021-4025. [PMID: 14086741]
3. Jiang, Y. and Cronan, J.E. Expression cloning and demonstration of Enterococcus faecalis lipoamidase (pyruvate dehydrogenase inactivase) as a Ser-Ser-Lys triad amidohydrolase. J. Biol. Chem. 280 (2005) 2244-2256. [PMID: 15528186]