Continued from EC 3.5.1.51 to EC 3.5.1.138
EC 3.5.2 In Cyclic Amides
EC 3.5.3 In Linear Amidines
Accepted name: barbiturase
Reaction: barbiturate + H2O = 3-oxo-3-ureidopropanoate
For diagram, click here
Glossary: barbiturate = 6-hydroxyuracil
Systematic name: barbiturate amidohydrolase (3-oxo-3-ureidopropanoate-forming)
Comments: Contains zinc and is specific for barbiturate as substrate [3]. Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.1.95 (N-malonylurea hydrolase). It was previously thought that the end-products of the reaction were malonate and urea but this has since been disproved [2]. May be involved in the regulation of pyrimidine metabolism, along with EC 2.4.2.9, uracil phosphoribosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-16-5
References:
1. Hayaishi, O. and Kornberg, A. Metabolism of cytosine, thymine, uracil, and barbituric acid by bacterial enzymes. J. Biol. Chem. 197 (1952) 717-723. [PMID: 12981104]
2. 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]
3. 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: dihydropyrimidinase
Reaction: 5,6-dihydrouracil + H2O = 3-ureidopropanoate
For diagram of reaction click here.
Other name(s): hydantoinase; hydropyrimidine hydrase; hydantoin peptidase; pyrimidine hydrase; D-hydantoinase
Systematic name: 5,6-dihydropyrimidine amidohydrolase
Comments: Also acts on dihydrothymine and hydantoin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9030-74-4
References:
1. Brooks, K.P., Jones, E.A., Kim, B.-D. and Sander, E.G. Bovine liver dihydropyrimidine amidohydrolase: purification, properties, and characterization as a zinc metalloenzyme. Arch. Biochem. Biophys. 226 (1983) 469-483. [PMID: 6639068]
2. Eadie, G.S., Bernheim, F. and Bernheim, J.L.C. Metabolism of cytosine, thymidine, uracil and barbituric acid by bacterial enzymes. J. Biol. Chem. 181 (1949) 449-458. [PMID: 15393763]
Accepted name: dihydroorotase
Reaction: (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
For diagram click here.
Other name(s): carbamoylaspartic dehydrase; dihydroorotate hydrolase
Systematic name: (S)-dihydroorotate amidohydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9024-93-5
References:
1. Cooper, C. and Wilson, D.W. Biosynthesis of pyrimidines. Fed. Proc. 13 (1954) 194 only.
2. Lieberman, I. and Kornberg, A. Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. II. Dihydroorotic acid, ureidosuccinic acid, and 5-carboxymethylhydantoin. J. Biol. Chem. 207 (1954) 911-924.
Accepted name: carboxymethylhydantoinase
Reaction: L-5-carboxymethylhydantoin + H2O = N-carbamoyl-L-aspartate
Other name(s): hydantoin hydrolase
Systematic name: L-5-carboxymethylhydantoin amidohydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9025-14-3
References:
1. Lieberman, I. and Kornberg, A. Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. II. Dihydroorotic acid, ureidosuccinic acid, and 5-carboxymethylhydantoin. J. Biol. Chem. 207 (1954) 911-924.
Accepted name: allantoinase
Reaction: (S)-allantoin + H2O = allantoate
For diagram click here.
Systematic name: (S)-allantoin amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-20-1
References:
1. Florkin, M. and Duchateau-Bosson, G. Microdosage photométrique de l'allantoïne en solutions pures et dans l'urine. Enzymologia 9 (1940) 5-9.
Accepted name: β-lactamase
Reaction: A β-lactam + H2O = a substituted β-amino acid
For diagram click here.
Other name(s): penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I; penicillinase II; β-lactamase I; β-lactamase II; β-lactamase III; β-lactamase A; β-lactamase B; β-lactamase C; β-lactamase AME I; cephalosporin-β-lactamase
Systematic name: β-lactam hydrolase
Comments: A group of enzymes of varying specificity hydrolysing β-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9073-60-3
References:
1. Citri, N. Penicillinase and other β-lactamases, in Boyer, P.D. (Ed.), The Enzymes, 3rd edn., vol. 4, Academic Press, New York, 1971, pp. 23-46.
2. Hennessey, T.D. and Richmond, M.H. The purification and some properties of a β-lactamase (cephalosporinase) synthesized by Enterobacter cloacae. Biochem. J. 109 (1968) 469-473. [PMID: 5685878]
3. Kuwabara, S. Purification and properties of two extracellular β-lactamases from Bacillus cereus 569-H. Biochem. J. 118 (1970) 457-465. [PMID: 4990588]
4. Pollock, M.R. Penicillinase, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 269-278.
5. Pollock, M.R., Torriani, A.-M. and Tridgell, E.G. Crystalline bacterial penicillinase. Biochem. J. 62 (1956) 387-391.
6. Ross, G.W. and Boulton, M.G. Purification of β-lactamases on QAE-sephadex. Biochim. Biophys. Acta 309 (1973) 430-439. [PMID: 4731970]
Accepted name: imidazolonepropionase
Reaction: (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O = N-formimidoyl-L-glutamate + H+
For diagram click here.
Other name(s): 4(5)-imidazolone-5(4)-propionic acid hydrolase; imidazolone propionic acid hydrolase
Systematic name: 3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9024-91-3
References:
1. Rao, D.R. and Greenberg, D.M. Studies on the enzymic decomposition of urocanic acid. IV. Purification and properties of 4(5)-imidazolone-5(4)-propionic acid hydrolase. J. Biol. Chem. 236 (1961) 1758-1763.
2. Snyder, S.H., Silva, O.L. and Kies, M.W. The mammalian metabolism of L-histidine. IV. Purification and properties of imidazolone propionic acid hydrolase. J. Biol. Chem. 236 (1961) 2996-2998.
[EC 3.5.2.8 Deleted entry: cephalosporinase. Now included with EC 3.5.2.6 β-lactamase (EC 3.5.2.8 created 1972, deleted 1978)]
Accepted name: 5-oxoprolinase (ATP-hydrolysing)
Reaction: ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate
Other name(s): pyroglutamase (ATP-hydrolysing); oxoprolinase; pyroglutamase; 5-oxoprolinase; pyroglutamate hydrolase; pyroglutamic hydrolase; L-pyroglutamate hydrolase; 5-oxo-L-prolinase; pyroglutamase
Systematic name: 5-oxo-L-proline amidohydrolase (ATP-hydrolysing)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9075-46-1
References:
1. van der Werf, P., Orlowski, M. and Meister, A. Enzymatic conversion of 5-oxo-L-proline (L-pyrrolidone carboxylate) to L-glutamate coupled with cleavage of adenosine triphosphate to adenosine diphosphate, a reaction in the γ-glutamyl cycle. Proc. Natl. Acad. Sci. USA 68 (1971) 2982-2985. [PMID: 5289242]
Accepted name: creatininase
Reaction: creatinine + H2O = creatine
Other name(s): creatinine hydrolase
Systematic name: creatinine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-13-2
References:
1. Tsuru, D., Oka, I. and Yoshimoto, T. Creatinine decomposing enzymes in Pseudomonas putida. Agric. Biol. Chem. 40 (1976) 1011-1018.
Accepted name: L-lysine-lactamase
Reaction: (S)-2-aminohexano-6-lactam + H2O = L-lysine
Glossary: (S)-2-aminohexano-6-lactam = L-lysine 1,6-lactam
Other name(s): L-α-aminocaprolactam hydrolase; L-lysinamidase; L-lysine-1,6-lactam lactamhydrolase
Systematic name: (S)-2-aminohexano-6-lactam lactamhydrolase
Comments: Also hydrolyses L-lysinamide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 52652-61-6
References:
1. Fukumura, T., Talbot, G., Misono, H., Teremura, Y., Kato, K. and Soda, K. Purification and properties of a novel enzyme, L-α-amino-ε-caprolactamase from Cryptococcus laurentii. FEBS Lett. 89 (1978) 298-300. [PMID: 26602]
2. Shvyadas, V.K., Galaev, I.Yu. and Kozlova, E.V. Preparation and characterization of L-α-aminocaprolactam hydrolase from cells of Cryptococcus laurentii. Biochemistry (Moscow) 49 (1984) 1268-1273.
Accepted name: 6-aminohexanoate-cyclic-dimer hydrolase
Reaction: 1,8-diazacyclotetradecane-2,9-dione + H2O = N-(6-aminohexanoyl)-6-aminohexanoate
Systematic name: 1,8-diazacyclotetradecane-2,9-dione lactamhydrolase
Comments: The cyclic dimer of 6-aminohexanoate is converted to the linear dimer.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 60976-29-6
References:
1. Kinoshita, S., Negoro, S., Muramatsu, M., Bisaria, V.S., Sawada, S. and Okada, H. 6-Aminohexanoic acid cyclic dimer hydrolase. A new cyclic amide hydrolase produced by Achromobacter guttatus KI74. Eur. J. Biochem. 80 (1977) 489-495. [PMID: 923591]
Accepted name: 2,5-dioxopiperazine hydrolase
Reaction: 2,5-dioxopiperazine + H2O = glycylglycine
Other name(s): cyclo(Gly-Gly) hydrolase; cyclo(glycylglycine) hydrolase
Systematic name: 2,5-dioxopiperazine amidohydrolase
Comments: Highly specific; does not hydrolyse other dioxopiperazines, glycylglycine, proteins or barbiturates.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 97599-45-6
References:
1. Suzuki, Y. and Uchida, K. Multiple forms of α-glycosidase from pig duodenum. Agric. Biol. Chem. 49 (1985) 1573-1581.
Accepted name: N-methylhydantoinase (ATP-hydrolysing)
Reaction: ATP + N-methylhydantoin + 2 H2O = ADP + phosphate + N-carbamoylsarcosine
For diagram of reaction click here.
Glossary: N-methylhydantoin = N-methylimidazolidine-2,4-dione
Other name(s): N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase; N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing)
Systematic name: N-methylhydantoin amidohydrolase (ATP-hydrolysing)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 100785-00-0
References:
1. Kim, J.M., Shimizu, S. and Yamada, H. Amidohydrolysis of N-methylhydantoin coupled with ATP hydrolysis. Biochem. Biophys. Res. Commun. 142 (1987) 1006-1012. [PMID: 3827889]
Accepted name: cyanuric acid amidohydrolase
Reaction: cyanuric acid + H2O = 1-carboxybiuret
For diagram of reaction click here.
Glossary: cyanuric acid = 1,3,5-triazine-2,4,6(1H,3H,5H)-trione = 2,4,6-trihydroxy-s-triazine
1-carboxybiuret = N-[(carbamoylamino)carbonyl]carbamate
Other name(s): atzD (gene name); trzD (gene name)
Systematic name: cyanuric acid amidohydrolase
Comments: The enzyme catalyses the ring cleavage 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 enzyme is highly specific for cyanuric acid. The product was initially thought to be bioret, but was later shown to be 1-carboxybioret.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 132965-78-7
References:
1. Eaton, R.W. and Karns, J.S. Cloning and comparison of the DNA encoding ammelide aminohydrolase and cyanuric acid amidohydrolase from three s-triazine-degrading bacterial strains. J. Bacteriol. 173 (1991) 1363-1366. [PMID: 1991731]
2. Eaton, R.W. and Karns, J.S. Cloning and analysis of s-triazine catabolic genes from Pseudomonas sp. strain NRRLB-12227. J. Bacteriol. 173 (1991) 1215-1222. [PMID: 1846859]
3. Karns, J.S. Gene sequence and properties of an s-triazine ring-cleavage enzyme from Pseudomonas sp. strain NRRLB-12227. Appl. Environ. Microbiol. 65 (1999) 3512-3517. [PMID: 10427042]
4. Fruchey, I., Shapir, N., Sadowsky, M.J. and Wackett, L.P. On the origins of cyanuric acid hydrolase: purification, substrates, and prevalence of AtzD from Pseudomonas sp. strain ADP. Appl. Environ. Microbiol. 69 (2003) 3653-3657. [PMID: 12788776]
5. 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: maleimide hydrolase
Reaction: maleimide + H2O = maleamic acid
Other name(s): imidase; cyclic imide hydrolase; cyclic-imide amidohydrolase (decyclicizing) [misprint]; cyclic-imide amidohydrolase (decyclizing)
Systematic name: cyclic-imide amidohydrolase (ring-opening)
Comment: Succinimide and glutarimide, and sulfur-containing cyclic imides, such as rhodanine, can also act as substrates for the enzyme from Blastobacter sp. A17p-4. The reverse, cyclization, reaction is also catalysed, but much more slowly. It has lower activity towards cyclic ureides, which are the substrates of EC 3.5.2.2, dihydropyrimidinase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9030-74-4
References:
1. Ogawa, J., Soong, C.L., Honda, M. and Shimizu, S. Imidase, a new dihydropyrimidinase-like enzyme involved in the metabolism of cyclic imides. Eur. J. Biochem. 243 (1997) 322-327. [PMID: 9030755]
Accepted name: hydroxyisourate hydrolase
Reaction: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
For diagram click here.
Other name(s): HIUHase; 5-hydroxyisourate hydrolase
Systematic name: 5-hydroxyisourate amidohydrolase
Comments: The reaction is the first stage in the conversion of 5-hydroxyisourate into S-allantoin. This reaction will also occur spontaneously but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 255885-20-2
References:
1. Raychaudhuri, A. and Tipton, P.A. A familiar motif in a new context: the catalytic mechanism of hydroxyisourate hydrolase. Biochemistry 42 (2003) 6848-6852.[PMID: 12779339]
2. Raychaudhuri, A. and Tipton, P.A. Cloning and expression of the gene for soybean hydroxyisourate hydrolase. Localization and implications for function and mechanism. Plant Physiol. 130 (2002) 2061-2068. [PMID: 12481089]
3. Sarma, A.D., Serfozo, P., Kahn, K. and Tipton, P.A. Identification and purification of hydroxyisourate hydrolase, a novel ureide-metabolizing enzyme. J. Biol. Chem. 274 (1999) 33863-33865. [PMID: 10567345]
Accepted name: enamidase
Reaction: 6-oxo-1,4,5,6-tetrahydronicotinate + 2 H2O = 2-formylglutarate + NH3
For diagram click here.
Systematic name: 6-oxo-1,4,5,6-tetrahydronicotinate amidohydrolase
Comments: Contains iron and Zn2+. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 1.1.1.291 (2-hydroxymethylglutarate dehydrogenase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Δ-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Alhapel, A., Darley, D.J., Wagener, N., Eckel, E., Elsner, N. and Pierik, A.J. Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri. Proc. Natl. Acad. Sci. USA 103 (2006) 12341-12346. [PMID: 16894175]
Accepted name: streptothricin hydrolase
Reaction: streptothricin-F + H2O = streptothricin-F acid
Other name(s): sttH (gene name)
Systematic name: streptothricin-F hydrolase
Comments: The enzyme also catalyses the hydrolysis of streptothricin-D to streptothricin-D acid [1]. The enzyme is responsible for streptothricin resistance in Streptomyces albulus and Streptomyces noursei [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Maruyama, C. and Hamano, Y. The biological function of the bacterial isochorismatase-like hydrolase SttH. Biosci. Biotechnol. Biochem. 73 (2009) 2494-2500. [PMID: 19897889]
2. Hamano, Y., Matsuura, N., Kitamura, M. and Takagi, H. A novel enzyme conferring streptothricin resistance alters the toxicity of streptothricin D from broad-spectrum to bacteria-specific. J. Biol. Chem. 281 (2006) 16842-16848. [PMID: 16641084]
Accepted name: isatin hydrolase
Reaction: isatin + H2O = isatinate
Glossary: isatin = 1H-indole-2,3-dione
isatinate = 2-(2-aminophenyl)-2-oxoacetate
Systematic name: isatin amidohydrolase
Comments: Requires Mn2+. This enzyme, found in several bacterial species, is involved in the degradation of indole-3-acetic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Sommer, M.R. and Jochimsen, B. Identification of enzymes involved in indole-3-acetic acid degradation. Plant Soil 186 (1996) 143-149.
2. Bjerregaard-Andersen, K., Sommer, T., Jensen, J.K., Jochimsen, B., Etzerodt, M. and Morth, J.P. A proton wire and water channel revealed in the crystal structure of isatin hydrolase. J. Biol. Chem. 289 (2014) 21351-21359. [PMID: 24917679]
Accepted name: arginase
Reaction: L-arginine + H2O = L-ornithine + urea
For diagram click here.
Other name(s): arginine amidinase; canavanase; L-arginase; arginine transamidinase
Systematic name: L-arginine amidinohydrolase
Comments: Also hydrolyses α-N-substituted L-arginines and canavanine.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9000-96-8
References:
1. Bach, S.J. and Killip, J.D. Studies on the purification and the kinetic properties of arginase from beef, sheep and horse liver.Biochim. Biophys. Acta 47 (1961) 336-343.
2. Cabello, J., Basilio, C. and Prajoux, V. Kinetic properties of erythrocyte- and liver arginase. Biochim. Biophys. Acta 48 (1961) 148-152.
3. Dumitru, I.F. Study of L-arginine amidinohydrolase from vegetable origin. Purification, crystallization and molecular weight. Acta Vitamin. Enzymol. 27 (1973) 207-210.
4. Greenberg, D.M. Arginase, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 257-267.
5. Greenberg, D.M., Bagot, A.E. and Roholt, O.A. Liver arginase. III. Properties of highly purified arginase. Arch. Biochem. Biophys. 62 (1956) 446-453.
Accepted name: guanidinoacetase
Reaction: guanidinoacetate + H2O = glycine + urea
Other name(s): glycocyaminase
Systematic name: guanidinoacetate amidinohydrolase
Comments: Requires Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9024-92-4
References:
1. Roche, J., Lacombe, G. and Girard, H. Sur la spécificité de certaines déguanidases bactériennes génératrices d'urée et sur l'argininedihydrolase. Biochim. Biophys. Acta 6 (1950) 210-216.
2. Yorifuji, T., Tamai, H. and Usami, H. Purification, crystallization and properties of Mn2+ dependent guanidoacetate amidinohydrolase from a Pseudomonas. Agric. Biol. Chem. 41 (1977) 959-966.
Accepted name: creatinase
Reaction: creatine + H2O = sarcosine + urea
For diagram of reaction click here.
Systematic name: creatine amidinohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37340-58-2
References:
1. Roche, J., Lacombe, G. and Girard, H. Sur la spécificité de certaines déguanidases bactériennes génératrices d'urée et sur l'argininedihydrolase. Biochim. Biophys. Acta 6 (1950) 210-216.
2. Yoshimoto, T., Oka, I. and Tsuru, D. Purification, crystallization, and some properties of creatine amidinohydrolase from Pseudomonas putida. J. Biochem. (Tokyo) 79 (1976) 1381-1383. [PMID: 8443]
Accepted name: allantoicase
Reaction: allantoate + H2O = (S)-ureidoglycolate + urea
For diagram click here.
Systematic name: allantoate amidinohydrolase
Comments: Also hydrolyses (R)-ureidoglycolate to glyoxylate and urea.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9025-21-2
References:
1. Florkin, M. and Duchateau-Bosson, G. Microdosage photométrique de l'allantoïne en solutions pures et dans l'urine. Enzymologia 9 (1940) 5-9.
2. Trijbels, F. and Vogels, G.D. Allantoicase and ureidoglycolase in Pseudomonas and Penicillium species. Biochim. Biophys. Acta 118 (1966) 387-395. [PMID: 4960174]
3. van der Drift, C. and Vogels, G.D. Effect of metal and hydrogen ions on the activity and stability of allantoicase. Biochim. Biophys. Acta 198 (1971) 339-352.
4. s'Gravenmade, E.J., van der Drift, C. and Vogels, G.D. Hydrolysis, racemization and absolute configuration of ureidoglycolate, a substrate of allantoicase. Biochim. Biophys. Acta 198 (1971) 569-582.
Accepted name: formimidoylaspartate deiminase
Reaction:N-formimidoyl-L-aspartate + H2O = N-formyl-L-aspartate + NH3
Other name(s): formiminoaspartate deiminase
Systematic name:N-formimidoyl-L-aspartate iminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9025-07-4
References:
1. Hayaishi, O., Tabor, H. and Hayaishi, T. N-Formimino-L-aspartic acid as an intermediate in the enzymic conversion of imidazoleacetic acid to formylaspartic acid. J. Biol. Chem. 227 (1957) 161-180.
Accepted name: arginine deiminase
Reaction: L-arginine + H2O = L-citrulline + NH3
Other name(s): arginine dihydrolase; citrulline iminase; L-arginine deiminase
Systematic name: L-arginine iminohydrolase
Comments: Also acts on canavanine.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-98-9
References:
1. Oginsky, E.L. and Gehrig, R.F. The arginine dihydrolase system of Streptococcus faecalis. II. Properties of arginine desimidase. J. Biol. Chem. 198 (1952) 799-805.
2. Petrack, B., Sullivan, L. and Ratner, S. Behavior of purified arginine desiminase from S. faecalis. Arch. Biochem. Biophys. 69 (1957) 186-197.
3. Ratner, S. Urea synthesis and metabolism of arginine and citrulline. Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 319-387.
Accepted name: guanidinobutyrase
Reaction: 4-guanidinobutanoate + H2O = 4-aminobutanoate + urea
For diagram, click here
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Other name(s): γ-guanidobutyrase; 4-guanidinobutyrate amidinobutyrase; γ-guanidinobutyrate amidinohydrolase; G-Base; GBH; guanidinobutyrate ureahydrolase
Systematic name: 4-guanidinobutanoate amidinohydrolase
Comments: Requires Mn2+. Also acts, very slowly, on 5-guanidinopentanoate and 6-guanidinohexanoate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9013-69-8
References:
1. Mora, J., Tarrab, R., Martuscelli, J. and Soberón, G. Characteristics of arginases from ureotelic and non-ureotelic animals. Biochem. J. 96 (1965) 588-594. [PMID: 5862400]
2. Thoai, N.V., Thome-Beau, F. and Olomucki, A. [Induction and specificity of enzymes of the new catabolic arginine pathway]. Biochim. Biophys. Acta 115 (1966) 73-80. [PMID: 5936244]
3. Yorifuji, T., Kato, M., Kobayashi, T., Ozaki, S. and Ueno, S. 4-Guanidinobutyrate amidinohydrolase from Pseudomonas sp ATCC 14676: purification to homogeneity and properties. Agric. Biol. Chem. 44 (1980) 1127-1134.
4. Yorifuji, T., Kobayashi, T., Tabuchi, A., Shiritani, Y. and Yonaha, K. Distribution of amidinohydrolases among Pseudomonas and comparative studies of some purified enzymes by one-dimensional peptide mapping. Agric. Biol. Chem. 47 (1983) 2825-2830.
Accepted name: formimidoylglutamase
Reaction: N-formimidoyl-L-glutamate + H2O = L-glutamate + formamide
For diagram click here.
Other name(s): formiminoglutamase; N-formiminoglutamate hydrolase; N-formimino-L-glutamate formiminohydrolase
Systematic name: N-formimidoyl-L-glutamate formimidoylhydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9054-92-6
References:
1. Kaminskas, E., Kimhi, Y. and Magasanik, B. Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus subtilis, two enzymes of the histidine degradation pathway. J. Biol. Chem. 245 (1970) 3536-3544. [PMID: 4990470]
2. Lund, P. and Magasanik, B. N-Formimino-L-glutamate formiminohydrolase of Aerobacter aerogenes. J. Biol. Chem. 240 (1965) 4316-4319. [PMID: 5845833]
Accepted name: allantoate deiminase
Reaction: allantoate + H2O = (S)-ureidoglycine + NH3 + CO2
For diagram click here.
Other name(s): allantoate amidohydrolase
Systematic name: allantoate amidinohydrolase (decarboxylating)
Comments: This enzyme is part of the ureide pathway, which permits certain organisms to recycle the nitrogen in purine compounds. This enzyme, which liberates ammonia from allantoate, is present in plants and bacteria. In plants it is localized in the endoplasmic reticulum. Requires manganese.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37289-13-7
References:
1. Vogels, G.D. Reversible activation of allantoate amidohydrolase by acid-pretreatment and other properties of the enzyme. Biochim. Biophys. Acta 113 (1966) 277-291. [PMID: 5328936]
2. Serventi, F., Ramazzina, I., Lamberto, I., Puggioni, V., Gatti, R. and Percudani, R. Chemical basis of nitrogen recovery through the ureide pathway: formation and hydrolysis of S-ureidoglycine in plants and bacteria. ACS Chem Biol 5 (2010) 203-214. [PMID: 20038185]
Accepted name: D-arginase
Reaction: D-arginine + H2O = D-ornithine + urea
Systematic name: D-arginine amidinohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37289-14-8
References:
1. Nadai, Y. Arginase. II. Distribution and properties of D-arginase. J. Biochem. (Tokyo) 45 (1958) 1011-1020.
Accepted name: agmatinase
Reaction: agmatine + H2O = putrescine + urea
For diagram click here.
Glossary: agmatine = (4-aminobutyl)guanidine
Other name(s): agmatine ureohydrolase; SpeB
Systematic name: agmatine amidinohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37289-16-0
References:
1. Hirshfeld, I.N., Rosenfeld, H.J., Leifer, Z. and Maas, W.K. Isolation and characterization of a mutant of Escherichia coli blocked in the synthesis of putrescine. J. Bacteriol. 101 (1970) 725-730. [PMID: 4908780]
2. Vicente, C. and Legaz, M.E. Preparation and properties of agmatine amidinohydrolase of Evernia prunastri. Physiol. Plant. 55 (1982) 335-339.
Accepted name: agmatine deiminase
Reaction: agmatine + H2O = N-carbamoylputrescine + NH3
Glossary: agmatine = (4-aminobutyl)guanidine
Other name(s): agmatine amidinohydrolase
Systematic name: agmatine iminohydrolase
Comments: The plant enzyme also catalyses the reactions of EC 2.1.3.3 (ornithine carbamoyltransferase), EC 2.1.3.6 (putrescine carbamoyltransferase) and EC 2.7.2.2 (carbamate kinase), thus functioning as a putrescine synthase, converting agmatine and ornithine into putrescine and citrulline, respectively.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37289-17-1
References:
1. Smith, T.A. Agmatine iminohydrolase in maize. Phytochemistry 8 (1969) 2111-2117.
2. Srivenugopal, K.S. and Adiga, P.R. Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase). J. Biol. Chem. 256 (1981) 9532-9541. [PMID: 6895223]
Accepted name: formimidoylglutamate deiminase
Reaction:N-formimidoyl-L-glutamate + H2O = N-formyl-L-glutamate + NH3
For diagram click here.
Other name(s): formiminoglutamate deiminase; formiminoglutamic iminohydrolase
Systematic name:N-formimidoyl-L-glutamate iminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9054-85-7
References:
1. Wickner, R.B. and Tabor, H. N-Formimino-L-glutamate iminohydrolase (Pseudomonas sp.). Methods Enzymol. 17B (1971) 80-84.
Accepted name: amidinoaspartase
Reaction: N-amidino-L-aspartate + H2O = L-aspartate + urea
Other name(s): amidinoaspartic amidinohydrolase
Systematic name: N-amidino-L-aspartate amidinohydrolase
Comments: Also acts slowly on N-amidino-L-glutamate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37325-60-3
References:
1. Milstien S. and Goldman, P. Metabolism of guanidinosuccinic acid. I. Characterization of a specific amidino hydrolase from Pseudomonas chlororaphis. J. Biol. Chem. 247 (1972) 6280-6283. [PMID: 4651648]
Accepted name: protein-arginine deiminase
Reaction: protein L-arginine + H2O = protein L-citrulline + NH3
Other name(s): peptidylarginine deiminase; PAD
Systematic name: protein-L-arginine iminohydrolase
Comments: Also acts on N-acyl-L-arginine and, more slowly, on L-arginine esters.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 75536-80-0
References:
1. Fujisaki, M. and Sugawara, K. Properties of peptidylarginine deiminase from the epidermis of newborn rats. J. Biochem. (Tokyo) 89 (1981) 257-263. [PMID: 7217033]
Accepted name: methylguanidinase
Reaction: methylguanidine + H2O = methylamine + urea
Other name(s): methylguanidine hydrolase
Systematic name: methylguanidine amidinohydrolase
Comments: Acts on some other alkylguanidines, but very slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 73200-93-8
References:
1. Nakajima, M., Shirokane, Y. and Mizusawa, K. A new amidinohydrolase, methylguanidine amidinohydrolase from Alcaligenes sp. N-42. FEBS Lett. 110 (1980) 43-46. [PMID: 7353662]
Accepted name: guanidinopropionase
Reaction: 3-guanidinopropanoate + H2O = β-alanine + urea
Other name(s): GPase; GPH
Systematic name: 3-guanidinopropanoate amidinopropionase
Comments: Requires Mn2+. Also acts, more slowly, on taurocyamine and 4-guanidinobutanoate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 68821-77-2
References:
1. Yorifuji, T., Sugai, I., Matsumoto, H. and Tabuchi, A. Characterization of 3-guanidinopropionate amidinohydrolase from Pseudomonas aeruginosa and a comparative study with 4- guanidinobutyrate amidinohydrolase from another Pseudomonas. Agric. Biol. Chem. 46 (1982) 1361-1363.
Accepted name: dimethylargininase
Reaction: Nω,Nω'-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline
Other name(s): dimethylarginine dimethylaminohydrolase; NG,NG-dimethylarginine dimethylaminohydrolase; NG,NG-dimethyl-L-arginine dimethylamidohydrolase; ω,ωÕ-di-N-methyl-L-arginine dimethylamidohydrolase
Systematic name: Nω,Nω'-dimethyl-L-arginine dimethylamidohydrolase
Comments: Also acts on Nω-methyl-L-arginine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 123644-75-7
References:
1. Ogawa, T., Kimoto, M. and Sasaoka, K. Purification and properties of a new enzyme, NG, NG-dimethylarginine dimethylaminohydrolase, from rat kidney. J. Biol. Chem. 264 (1989) 10205-10209. [PMID: 2722865]
[EC 3.5.3.19 Transferred entry: ureidoglycolate hydrolase. Now classified as EC 3.5.1.116, ureidoglycolate amidohydrolase (EC 3.5.3.19 created 1992, deleted 2013)]
Accepted name: diguanidinobutanase
Reaction: 1,4-diguanidinobutane + H2O = agmatine + urea
Glossary: agmatine = (4-aminobutyl)guanidine
Systematic name: 1,4-diguanidinobutane amidinohydrolase
Comments: Other diguanidinoalkanes with 3 to 10 methylene groups can also act, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 125268-65-7
References:
1. Yorifuji, T., Kaneoke, M., Shimizu, E., Shiota, K. and Matsuo, R. Degradation of α,ω-diguanidinoalkanes and a novel enzyme, diguanidinobutane amidohydrolase, in Pseudomonas putida. Agric. Biol. Chem. 53 (1989) 3003-3009.
Accepted name: methylenediurea deaminase
Reaction: (1a) NH2-CO-NH-CH2-NH-CO-NH2 + H2O = N-(carboxyaminomethyl)urea + NH3
(1b) N-(carboxyaminomethyl)urea = N-(aminomethyl)urea + CO2 (spontaneous)
(1c) N-(aminomethyl)urea + H2O = N-(hydroxymethyl)urea + NH3 (spontaneous)
Other name(s): methylenediurease
Systematic name: methylenediurea aminohydrolase
Comments: The methylenediurea is hydrolysed and decarboxylated to give an aminated methylurea, which then spontaneously hydrolyses to hydroxymethylurea. The enzyme from Ochrobactrum anthropi also hydrolyses dimethylenetriurea and trimethylenetetraurea as well as ureidoglycolate, which is hydrolysed to urea and glyoxylate, and allantoate, which is hydrolysed to ureidoglycolate, ammonia and carbon dioxide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 205830-62-2
References:
1. Jahns, T., Schepp, R., Kaltwasser, H. Purification and characterisation of an enzyme from a strain of Ochrobactrum anthropi that degrades condensation products of urea and formaldehyde (ureaform). Can. J. Microbiol. 43 (1997) 1111-1117.
Accepted name: proclavaminate amidinohydrolase
Reaction: amidinoproclavaminate + H2O = proclavaminate + urea
For diagram click here.
Other name(s): PAH; proclavaminate amidino hydrolase
Systematic name: amidinoproclavaminate amidinohydrolase
Comments: Forms part of the pathway for the biosythesis of the β-lactamase inhibitor clavulanate in Streptomyces clavuligerus. It carries out an intermediary reaction between the first reaction of EC 1.14.11.21, clavaminate synthase, and the second and third reactions of that enzyme. Requires Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Salowe, S.P., Krol, W.J., Iwatareuyl, D. and Townsend, C.A. Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction. Biochemistry 30 (1991) 2281-2292. [PMID: 1998687]
2. Zhou, J., Kelly, W.L., Bachmann, B.O., Gunsior, M., Townsend, C.A. and Solomon, E.I. Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional α-KG-dependent non-heme iron enzyme: Correlation with mechanisms and reactivities. J. Am. Chem. Soc. 123 (2001) 7388-7389.
3. Townsend, C.A. New reactions in clavulanic acid biosynthesis. Curr. Opin. Chem. Biol. 6 (2002) 583-589. [PMID: 12413541]
4. Wu, T.K., Busby, R.W., Houston, T.A., McIlwaine, D.B., Egan, L.A. and Townsend, C.A. Identification, cloning, sequencing, and overexpression of the gene encoding proclavaminate amidino hydrolase and characterization of protein function in clavulanic acid biosynthesis. J. Bacteriol. 177 (1995) 3714-3720. [PMID: 7601835]
Accepted name: N-succinylarginine dihydrolase
Reaction: N2-succinyl-L-arginine + 2 H2O = N2-succinyl-L-ornithine + 2 NH3 + CO2
For diagram, click here
Other name(s): N2-succinylarginine dihydrolase; arginine succinylhydrolase; SADH; AruB; AstB
Systematic name: N2-succinyl-L-arginine iminohydrolase (decarboxylating)
Comments: Arginine, N2-acetylarginine and N2-glutamylarginine do not act as substrates [3]. This is the second 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 2.6.1.81 (succinylornithine 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:
References:
1. 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]
2. Tocilj, A., Schrag, J.D., Li, Y., Schneider, B.L., Reitzer, L., Matte, A. and Cygler, M. Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli. J. Biol. Chem. 280 (2005) 15800-15808. [PMID: 15703173]
3. 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]
4. Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 50 (1986) 314-352. [PMID: 3534538]
5. 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]
Accepted name: N1-aminopropylagmatine ureohydrolase
Reaction: N1-aminopropylagmatine + H2O = spermidine + urea
For diagram of reaction click here.
Systematic name: N1-aminopropylagmatine amidinohydrolase
Comments: The enzyme, which has been characterized from the hyperthermophilic archaeon Pyrococcus kodakarensis and the thermophilic Gram-negative bacterium Thermus thermophilus, is involved in the biosynthesis of spermidine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ohnuma, M., Terui, Y., Tamakoshi, M., Mitome, H., Niitsu, M., Samejima, K., Kawashima, E. and Oshima, T. N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus. J. Biol. Chem. 280 (2005) 30073-30082. [PMID: 15983049]
2. Morimoto, N., Fukuda, W., Nakajima, N., Masuda, T., Terui, Y., Kanai, T., Oshima, T., Imanaka, T. and Fujiwara, S. Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis. J. Bacteriol. 192 (2010) 4991-5001. [PMID: 20675472]
Accepted name: Nω-hydroxy-L-arginine amidinohydrolase
Reaction: Nω-hydroxy-L-arginine + H2O = L-ornithine + hydroxyurea
Other name(s): dcsB (gene name)
Systematic name: Nω-hydroxy-L-arginine amidinohydrolase
Comments: The enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kumagai, T., Koyama, Y., Oda, K., Noda, M., Matoba, Y. and Sugiyama, M. Molecular cloning and heterologous expression of a biosynthetic gene cluster for the antitubercular agent D-cycloserine produced by Streptomyces lavendulae. Antimicrob. Agents Chemother. 54 (2010) 1132-1139. [PMID: 20086163]
2. Kumagai, T., Takagi, K., Koyama, Y., Matoba, Y., Oda, K., Noda, M. and Sugiyama, M. Heme protein and hydroxyarginase necessary for biosynthesis of D-cycloserine. Antimicrob. Agents Chemother. 56 (2012) 3682-3689. [PMID: 22547619]
Accepted name: (S)-ureidoglycine aminohydrolase
Reaction: (S)-2-ureidoglycine + H2O = (S)-ureidoglycolate + NH3
For diagram click here.
Other name(s): UGlyAH; UGHY; ylbA (gene name)
Systematic name: (S)-ureidoglycine aminohydrolase
Comments: Binds Mn2+. This enzyme, found in plants and bacteria, is part of the ureide pathway, which enables the recycling of the nitrogen in purine compounds. In plants it is localized in the endoplasmic reticulum.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Serventi, F., Ramazzina, I., Lamberto, I., Puggioni, V., Gatti, R. and Percudani, R. Chemical basis of nitrogen recovery through the ureide pathway: formation and hydrolysis of S-ureidoglycine in plants and bacteria. ACS Chem. Biol. 5 (2010) 203-214. [PMID: 20038185]
2. 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]
3. Shin, I., Percudani, R. and Rhee, S. Structural and functional insights into (S)-ureidoglycine aminohydrolase, key enzyme of purine catabolism in Arabidopsis thaliana. J. Biol. Chem. 287 (2012) 18796-18805. [PMID: 22493446]
Accepted name: arginine dihydrolase
Reaction: L-arginine + 2 H2O = L-ornithine + CO2 + 2 ammonia
Other name(s): argZ (gene name)
Systematic name: L-arginine aminodihydrolase (L-ornithine-forming)
Comments: The enzyme, characterized from different cyanobacterial species, is highly specific to arginine and does not require a metal cofactor. The enzyme from Nostoc is bifunctional, and also catalyses the activity of EC 4.3.1.12, ornithine cyclodeaminase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Zhang, H., Liu, Y., Nie, X., Liu, L., Hua, Q., Zhao, G.P. and Yang, C. The cyanobacterial ornithine-ammonia cycle involves an arginine dihydrolase. Nat. Chem. Biol. 14 (2018) 575-581. [PMID: 29632414]
2. Burnat, M., Picossi, S., Valladares, A., Herrero, A. and Flores, E. Catabolic pathway of arginine in Anabaena involves a novel bifunctional enzyme that produces proline from arginine. Mol. Microbiol. 111 (2019) 883-897. [PMID: 30636068]
3. Zhuang, N., Zhang, H., Li, L., Wu, X., Yang, C. and Zhang, Y. Crystal structures and biochemical analyses of the bacterial arginine dihydrolase ArgZ suggests a "bond rotation" catalytic mechanism. J. Biol. Chem. 295 (2020) 2113-2124. [PMID: 31914412]