Continued from EC 3.5.2 and EC 3.5.3
EC 3.5.4 In Cyclic Amidines
EC 3.5.5 In Nitriles
EC 3.5.99 In Other Compounds
Accepted name: cytosine deaminase
Reaction: cytosine + H2O = uracil + NH3
Other name(s): isocytosine deaminase
Systematic name: cytosine aminohydrolase
Comments: Also acts on 5-methylcytosine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-05-2
References:
1. Cohen, S.S. and Barner, H.D. The conversion of 5-methyldeoxycytidine to thymidine in vitro and in vivo. J. Biol. Chem. 226 (1957) 631-642.
2. Kream, J. and Chargaff, E. On the cytosine deaminase of yeast. J. Am. Chem. Soc. 74 (1952) 5157-5160.
Accepted name: adenine deaminase
Reaction: adenine + H2O = hypoxanthine + NH3
Other name(s): adenase; adenine aminase; ADase
Systematic name: adenine aminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-68-3
References:
1. Blauch, M., Koch, F.C. and Hane, M.E. A study of xanthine oxidase of rat blood. J. Biol. Chem. 130 (1939) 471-486.
2. Heppel, L.A., Hurwitz, J. and Horecker, B.L. Adenine deaminase of Azotobacter vinelandii. J. Am. Chem. Soc. 79 (1957) 630-633.
Accepted name: guanine deaminase
Reaction: guanine + H2O = xanthine + NH3
Other name(s): guanase; guanine aminase; GAH
Systematic name: guanine aminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9033-16-3
References:
1. Hitchings, G.H. and Falco, E.A. The identification of guanine in extracts of Girella nigricans. The specificity of guanase. Proc. Natl. Acad. Sci. USA 30 (1944) 294-297.
2. Kalckar, H.M. Differential spectrophotometry of purine compounds by means of specific enzymes. III. Studies of the enzymes of purine metabolism. J. Biol. Chem. 167 (1947) 461-475.
3. Rabinowitz, J.C. and Barker, H.A. Purine fermentation by Clostridium cylindrosporum. II. Purine transformations. J. Biol. Chem. 218 (1956) 161-173.
Accepted name: adenosine deaminase
Reaction: adenosine + H2O = inosine + NH3
(2) 2′-deoxyadenosine + H2O = 2′-deoxyinosine + NH3
Other name(s): deoxyadenosine deaminase
Systematic name: adenosine aminohydrolase
Comments: The enzyme, found in a wide variety of microorganisms, plants, invertebrates, and animals, plays a role in purine metabolism.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-93-1
References:
1. Kaplan, N.O., Colowick, S.P. and Ciotti, M.M. Enzymatic deamination of cytosine nucleosides. J. Biol. Chem. 194 (1952) 579-591.
2. Powell, J.F. and Hunter, J.R. Adenosine deaminase and ribosidase in spores of Bacillus cereus. Biochem. J. 62 (1956) 381-387.
3. Singh, L.S. and Sharma, R. Purification and characterization of intestinal adenosine deaminase from mice. Mol. Cell. Biochem. 204 (2000) 127–134. [PMID: 10718633]
4. Cristalli, G., Costanzi, S., Lambertucci, C., Lupidi, G., Vittori, S., Volpini, R. and Camaioni, E. Adenosine deaminase: functional implications and different classes of inhibitors. Med. Res. Rev. 21 (2001) 105–128. [PMID: 11223861]
Accepted name: cytidine deaminase
Reaction: (1) cytidine + H2O = uridine + NH3
(2) 2'-deoxycytidine + H2O = 2'-deoxyuridine + NH3
Other name(s): cytosine nucleoside deaminase; (deoxy)cytidine deaminase; cdd (gene name); CDA (gene name)
Systematic name: cytidine/2'-deoxycytidine aminohydrolase
Comments: Contains zinc. Catalyses the deamination of cytidine and 2'-deoxycytidine with similar efficiencies. The enzyme, which is widely distributed among organisms, is involved in salvage of both exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9025-06-3
References:
1. Roberts, D.W.A. The wheat leaf phosphatases. II. Pathway of hydrolysis of some nucleotides at pH 5.5. J. Biol. Chem. 222 (1956) 259-270. [PMID: 13366999]
2. Wang, T.P., Sable, H.Z. and Lampen, J.O. Enzymatic deamination of cytosine nucleosides. J. Biol. Chem. 184 (1950) 17-28. [PMID: 15421968]
3. Song, B.H. and Neuhard, J. Chromosomal location, cloning and nucleotide sequence of the Bacillus subtilis cdd gene encoding cytidine/deoxycytidine deaminase. Mol. Gen. Genet. 216 (1989) 462-468. [PMID: 2526291]
4. Laliberte, J. and Momparler, R.L. Human cytidine deaminase: purification of enzyme, cloning, and expression of its complementary DNA. Cancer Res. 54 (1994) 5401-5407. [PMID: 7923172]
5. Vincenzetti, S., Cambi, A., Neuhard, J., Schnorr, K., Grelloni, M. and Vita, A. Cloning, expression, and purification of cytidine deaminase from Arabidopsis thaliana. Protein Expr. Purif. 15 (1999) 8-15. [PMID: 10024464]
Accepted name: AMP deaminase
Reaction: AMP + H2O = IMP + NH3
For diagram click here.
Other name(s): adenylic acid deaminase; AMP aminase; adenylic deaminase; adenylate deaminase; 5-AMP deaminase; adenosine 5-monophosphate deaminase; 5-adenylate deaminase; adenyl deaminase; 5-adenylic acid deaminase; adenosine monophosphate deaminase; adenylate aminohydrolase; adenylate desaminase; adenosine 5-phosphate aminohydrolase; 5-adenylate deaminase
Systematic name: AMP aminohydrolase
Comments: cf. EC 3.5.4.17 adenosine-phosphate deaminase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9025-10-9
References:
1. Kalckar, H.M. Differential spectrophotometry of purine compounds by means of specific enzymes. III. Studies of the enzymes of purine metabolism. J. Biol. Chem. 167 (1947) 461-475.
2. Lee, Y.-P. 5'-Adenylic acid deaminase. I. Isolation of the crystalline enzyme from rabbit skeletal muscle. J. Biol. Chem. 227 (1957) 987-992.
3. Lee, Y.-P. 5'-Adenylic acid deaminase. II. Homogeneity and physicochemical properties. J. Biol. Chem. 227 (1957) 993-998.
4. Lee, Y.-P. 5'-Adenylic acid deaminase. III. Properties and kinetic studies. J. Biol. Chem. 227 (1957) 999-1007.
5. Mendicino, J. and Muntz, J.A. The activating effect of adenosine triphosphate on brain adenylic deaminase. J. Biol. Chem. 233 (1958) 178-183.
6. Turner, D.H. and Turner, J.F. Adenylic deaminase of pea seeds. Biochem. J. 79 (1961) 143-147.
7. Weil-Malherbe, W. and Green, R.H. Ammonia formation in brain. 2. Brain adenylic deaminase. Biochem. J. 61 (1955) 218-224.
Accepted name: ADP deaminase
Reaction: ADP + H2O = IDP + NH3
Other name(s): adenosine diphosphate deaminase; adenosinepyrophosphate deaminase
Systematic name: ADP aminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-79-6
References:
1. Deutsch, A. and Nilsson, R. On the dephosphorylation and deamination of adenosine triphosphate by actomyosin gel. Acta Chem. Scand. 8 (1954) 1898-1906.
Accepted name: aminoimidazolase
Reaction: 4-aminoimidazole + H2O = imidazol-4-one + NH3
Other name(s): 4-aminoimidazole hydrolase
Systematic name: 4-aminoimidazole aminohydrolase
Comments: Requires Fe2+. This enzyme forms part of the xanthine-degradation pathway in some bacteria. The product of the reaction, imidazol-4-one, can be converted non-enzymically into formiminoglycine. An enzyme has been identified in Clostridium cylindrosporum that can perform this hydrolysis reaction [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9025-17-6
References:
1. Rabinowitz, J.C. and Pricer, W.E. Purine fermentation by Clostridium cylindrosporum. V. Formiminoglycine. J. Biol. Chem. 222 (1956) 537-554. [PMID: 13367024]
2. Freter, K., Rabinowitz, J.C. and Witkop, B. Labile Stoffwechselprodukte. V. Zur Biogenese des Formiminoglycins aus 4(5H)-imidazolon. Ann. Chem. 607 (1957) 174-187.
3. Vogels, G.D. and Van der Drift, C. Degradation of purines and pyrimidines by microorganisms. Bacteriol. Rev. 40 (1976) 403-468. [PMID: 786256]
4. DeMoll, E. and Auffenberg, T. Purine metabolism in Methanococcus vannielii. J. Bacteriol. 175 (1993) 5754-5761. [PMID: 8376322]
Accepted name: methenyltetrahydrofolate cyclohydrolase
Reaction: 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate
For diagram of reaction click here (another example).
Other name(s): Citrovorum factor cyclodehydrase; cyclohydrolase; formyl-methenyl-methylenetetrahydrofolate synthetase (combined); 5,10-methenyltetrahydrofolate 5-hydrolase (decyclizing)
Systematic name: 5,10-methenyltetrahydrofolate 5-hydrolase (ring-opening)
Comments: In eukaryotes, the enzyme occurs as a trifunctional enzyme that also has methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and formate—tetrahydrofolate ligase (EC 6.3.4.3) activity. In some prokaryotes, it occurs as a bifunctional enzyme that also has dehydrogenase (EC 1.5.1.5) activity or formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-97-8
References:
1. Rabinowitz, J.C. and Pricer, W.E. The enzymatic synthesis of N10-formyltetrahydrofolic acid and its role in ATP formation during formiminoglycine degradation. J. Am. Chem. Soc. 78 (1956) 4176-4178.
2. Tabor, H. and Wyngaarden, L. The enzymatic formation of formiminotetrahydrofolic acid, 5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid in the metabolism of formiminoglutamic acid. J. Biol. Chem. 234 (1959) 1830-1846.
Accepted name: IMP cyclohydrolase
Reaction: IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
For reaction pathway click here.
Other name(s): inosinicase; inosinate cyclohydrolase; IMP 1,2-hydrolase (decyclizing)
Systematic name: IMP 1,2-hydrolase (ring-opening)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9013-81-4
References:
1. Flaks, J.G., Erwin, M.J. and Buchanan, J.M. Biosynthesis of the purines. XVIII. 5-Amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase and inosinicase. J. Biol. Chem. 229 (1957) 603-612.
Accepted name: pterin deaminase
Reaction: a 2-amino-4-hydroxypteridine + H2O = a 2,4-dihydroxypteridine + NH3
Other name(s): acrasinase
Systematic name: 2-amino-4-hydroxypteridine aminohydrolase
Comments: The animal enzyme is specific for pterin, isoxanthopterin and tetrahydropterin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9025-04-1
References:
1. Levenberg, B. and Hayaishi, O. A bacterial pterin deaminase. J. Biol. Chem. 234 (1959) 955-961.
2. Rembold, H. and Simmersbach, F. Catabolism of pteridine cofactors. II. A specific pterin deaminase in rat liver. Biochim. Biophys. Acta 184 (1969) 589-596. [PMID: 5821022]
Accepted name: dCMP deaminase
Reaction: dCMP + H2O = dUMP + NH3
Other name(s): deoxycytidylate deaminase; deoxy-CMP-deaminase; deoxycytidylate aminohydrolase; deoxycytidine monophosphate deaminase; deoxycytidine-5'-phosphate deaminase; deoxycytidine-5'-monophosphate aminohydrolase
Systematic name: dCMP aminohydrolase
Comments: Also acts on some 5-substituted dCMPs.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-92-0
References:
1. Scarano, E. The enzymatic deamination of 6-aminopyrimidine deoxyribonucleotides. I. The enzymatic deamination of deoxycytidine 5'-phosphate and of 5-methyldeoxycytidine 5-methyldeoxycytidine 5'-phosphate.J. Biol. Chem. 235 (1960) 706-713.
2. Scarano, E., Bonaduce, L. and de Petrocellis, B. The enzymatic deamination of 6-aminopyrimidine deoxyribonucleotides. II. Purification and properties of a 6-aminopyrimidine deoxyribonucleoside 5'-phosphate deaminase from unfertilized eggs of sea urchin. J. Biol. Chem. 235 (1960) 3556-3561.
3. Sergott, R.C., Debeer, L.J. and Bessman, M.J. On the regulation of a bacterial deoxycytidylate deaminase. J. Biol. Chem. 246 (1971) 7755-7758. [PMID: 5002683]
Accepted name: dCTP deaminase
Reaction: dCTP + H2O = dUTP + NH3
Other name(s): deoxycytidine triphosphate deaminase; 5-methyl-dCTP deaminase
Systematic name: dCTP aminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37289-18-2
References:
1. Tomita, F. and Takahashi, I. A novel enzyme, dCTP deaminase, found in Bacillus subtilis infected with phage PBS I. Biochim. Biophys. Acta 179 (1969) 18-27. [PMID: 4976547]
[EC 3.5.4.14 Transferred entry: deoxycytidine deaminase. Now included in EC 3.5.4.5, (deoxy)cytidine deaminase (EC 3.5.4.14 created 1972, deleted 2013)]
Accepted name: guanosine deaminase
Reaction: guanosine + H2O = xanthosine + NH3
Other name(s): guanosine aminase
Systematic name: guanosine aminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9067-85-0
References:
1. Isihida, Y., Shirafiji, H., Kida, M. and Yoneda, M. Studies on the guanosine degrading system in bacterial cell. III. Preparation and properties of guanosine deaminase. Agric. Biol. Chem. 33 (1969) 384-390.
Accepted name: GTP cyclohydrolase I
Reaction: GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
For diagram of reaction click here.
Glossary: 7,8-dihydroneopterin 3'-triphosphate = 6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin
Other name(s): GTP cyclohydrolase; guanosine triphosphate cyclohydrolase; guanosine triphosphate 8-deformylase; dihydroneopterin triphosphate synthase; GTP 8-formylhydrolase
Systematic name: GTP 7,8-8,9-dihydrolase
Comments: The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic. This enzyme is involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 (sepiapterin reductase) and EC 4.2.3.12 (6-pyruvoyltetrahydropterin synthase) [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37289-19-3
References:
1. Burg, A.W. and Brown, G.M. The biosynthesis of folic acid. 8. Purification and properties of the enzyme that catalyzes the production of formate from carbon atom 8 of guanosine triphosphate. J. Biol. Chem. 243 (1968) 2349-2358. [PMID: 4296838]
2. Wolf, W.A. and Brown, G.M. The biosynthesis of folic acid. X. Evidence for an Amadori rearrangement in the enzymatic formation of dihydroneopterin triphosphate from GTP. Biochim. Biophys. Acta 192 (1969) 468-478. [PMID: 4904679]
3. Supangat, S., Choi, Y.K., Park, Y.S., Son, D., Han, C.D. and Lee, K.H. Expression, purification, crystallization and preliminary X-ray analysis of sepiapterin reductase from Chlorobium tepidum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 202-204. [PMID: 16510994]
Accepted name: adenosine-phosphate deaminase
Reaction: (1) AMP + H2O = IMP + NH3
(2) ADP + H2O = IDP + NH3
(3) ATP + H2O = ITP + NH3
Glossary: IMP = inosine 5'-phosphate
AMP = adenosine 5'-phosphate
Other name(s): adenylate deaminase; adenine nucleotide deaminase; adenosine (phosphate) deaminase
Systematic name: adenosine-phosphate aminohydrolase
Comments: Acts on AMP, ADP, ATP, NAD+ and adenosine, in decreasing order of activity. The bacterial enzyme can also accept the deoxy derivatives. cf. EC 3.5.4.6, AMP deaminase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-20-6
References:
1. Su, J.-C., Li, C.-C. and Ting, C.C. A new adenylate deaminase from red marine alga Porphyra crispata. Biochemistry 5 (1966) 536-543. [PMID: 5940938]
2. Yates, M.G. A non-specific adenine nucleotide deaminase from Desulfovibrio desulfuricans. Biochim. Biophys. Acta 171 (1969) 299-310. [PMID: 5773435]
Accepted name: ATP deaminase
Reaction: ATP + H2O = ITP + NH3
Other name(s): adenosine triphosphate deaminase
Systematic name: ATP aminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37289-21-7
References:
1. Chung, S.-T. and Aida, K. Purification and properties of ATP deaminase from Microsporum audouini. J. Biochem. (Tokyo) 61 (1967) 1-9. [PMID: 6048966]
Accepted name: phosphoribosyl-AMP cyclohydrolase
Reaction: 1-(5-phospho-β-D-ribosyl)-AMP + H2O = 1-(5-phospho-β-D-ribosyl)-5-[(5-phospho-β-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
For diagram click here.
Other name(s): PRAMP-cyclohydrolase; phosphoribosyladenosine monophosphate cyclohydrolase; 1-(5-phospho-D-ribosyl)-AMP 1,6-hydrolase
Systematic name: 1-(5-phospho-β-D-ribosyl)-AMP 1,6-hydrolase
Comments: The Neurospora crassa enzyme also catalyses the reactions of EC 1.1.1.23 (histidinol dehydrogenase) and EC 3.6.1.31 (phosphoribosyl-ATP diphosphatase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37289-22-8
References:
1. Minson, A.C. and Creaser, E.H. Purification of a trifunctional enzyme, catalysing three steps of the histidine pathway, from Neurospora crassa. Biochem. J. 114 (1969) 49-56. [PMID: 4309307]
Accepted name: pyrithiamine deaminase
Reaction: 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(2-hydroxyethyl)-2-methylpyridinium + H2O = 1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(2-hydroxyethyl)-2-methylpyridinium + NH3
Glossary: pyrithiamine = 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(2-hydroxyethyl)-2-methylpyridinium bromide hydrobromide
Other name(s): 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(2-hydroxyethyl)-2-methylpyridinium-bromide aminohydrolase
Systematic name: 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(β-hydroxyethyl)-2-methylpyridinium aminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-23-9
References:
1. Sinha, A.K. and Chatterjee, G.C. Metabolism of pyrithiamine by the pyrithiamine-requiring mutant of Staphylococcus aureus. Biochem. J. 107 (1968) 165-169. [PMID: 5641872]
Accepted name: creatinine deaminase
Reaction: creatinine + H2O = N-methylhydantoin + NH3
For diagram of reaction click here.
Glossary: N-methylhydantoin = N-methylimidazolidine-2,4-dione
Other name(s): creatinine hydrolase; creatinine desiminase
Systematic name: creatinine iminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37289-15-9
References:
1. Szulmajster, J. Bacterial degradation of creatinine. II. Creatinine desimidase. Biochim. Biophys. Acta 30 (1958) 154-163.
Accepted name: 1-pyrroline-4-hydroxy-2-carboxylate deaminase
Reaction: 1-pyrroline-4-hydroxy-2-carboxylate + H2O = 2,5-dioxopentanoate + NH3
Other name(s): HPC deaminase; 1-pyrroline-4-hydroxy-2-carboxylate aminohydrolase (decyclizing)
Systematic name: 1-pyrroline-4-hydroxy-2-carboxylate aminohydrolase (ring-opening)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9054-77-7
References:
1. Singh, R.M.M. and Adams, E. Enzymatic deamination of δ1-pyrroline-4-hydroxy-2-carboxylate to 2,5-dioxovalerate (α-ketoglutaric semialdehyde). J. Biol. Chem. 240 (1965) 4344-4351.
2. Singh, R.M.M. and Adams, E. Isolation and identification of 2,5-dioxovalerate, an intermediate in the bacterial oxidation of hydroxyproline. J. Biol. Chem. 240 (1965) 4352-4356.
Accepted name: blasticidin-S deaminase
Reaction: blasticidin S + H2O = deaminohydroxyblasticidin S + NH3
Systematic name: blasticidin-S aminohydrolase
Comments: Catalyses the deamination of the cytosine moiety of the antibiotics blasticidin S, cytomycin and acetylblasticidin S.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 54576-55-5
References:
1. Yamaguchi, I., Shibata, H., Seto, H. and Misato, T. Isolation and purification of blasticidin S deaminase from Aspergillus terreus. J. Antibiot. 28 (1975) 7-14. [PMID: 236272]
Accepted name: sepiapterin deaminase
Reaction: sepiapterin + H2O = xanthopterin-B2 + NH3
Systematic name: sepiapterin aminohydrolase
Comments: Also acts on isosepiapterin, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-22-3
References:
1. Tsusué, M. Studies on sepiapterin deaminase from the silkworm, Bombyx mori. Purification and some properties of the enzyme. J. Biochem. (Tokyo) 69 (1971) 781-788. [PMID: 5572808]
Accepted name: GTP cyclohydrolase II
Reaction: GTP + 4 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + 2 phosphate
For diagram of reaction click here
Other name(s): guanosine triphosphate cyclohydrolase II; GTP-8-formylhydrolase; ribA (gene name); GTP 7,8-8,9-dihydrolase (diphosphate-forming)
Systematic name: GTP 7,8-8,9-dihydrolase (formate-releasing, phosphate-releasing)
Comments: The enzyme, found in prokaryotes and some eukaryotes, hydrolytically cleaves the C-N bond at positions 8 and 9 of GTP guanine, followed by a subsequent hydrolytic attack at the base, which liberates formate, and cleavage of the α-β phosphodiester bond of the triphosphate to form diphosphate. The enzyme continues with a slow cleavage of the diphosphate to form two phosphate ions. The enzyme requires zinc and magnesium ions for the cleavage reactions at the GTP guanine and triphosphate sites, respectively. It is one of the enzymes required for flavin biosynthesis in many bacterial species, lower eukaryotes, and plants. cf. EC 3.5.4.16, GTP cyclohydrolase I, EC 3.5.4.29, GTP cyclohydrolase IIa, and EC 3.5.4.39, GTP cyclohydrolase IV.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56214-35-8
References:
1. Foor, F. and Brown, G.M. Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli. J. Biol. Chem. 250 (1975) 3545-3551. [PMID: 235552]
2. Ritz, H., Schramek, N., Bracher, A., Herz, S., Eisenreich, W., Richter, G. and Bacher, A. Biosynthesis of riboflavin: studies on the mechanism of GTP cyclohydrolase II. J. Biol. Chem. 276 (2001) 22273-22277. [PMID: 11301327]
3. Schramek, N., Bracher, A. and Bacher, A. Biosynthesis of riboflavin. Single turnover kinetic analysis of GTP cyclohydrolase II. J. Biol. Chem. 276 (2001) 44157-44162. [PMID: 11553632]
4. Ren, J., Kotaka, M., Lockyer, M., Lamb, H.K., Hawkins, A.R. and Stammers, D.K. GTP cyclohydrolase II structure and mechanism. J. Biol. Chem. 280 (2005) 36912-36919. [PMID: 16115872]
5. Smith, M.M., Beaupre, B.A., Fourozesh, D.C., Meneely, K.M., Lamb, A.L. and Moran, G.R. Finding ways to relax: a revisionistic analysis of the chemistry of E. coli GTP cyclohydrolase II. Biochemistry 60 (2021) 3027-3039. [PMID: 34569786]
Accepted name: diaminohydroxyphosphoribosylaminopyrimidine deaminase
Reaction: 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH3
Systematic name: 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine 2-aminohydrolase
Comments: The substrate is the product of EC 3.5.4.25 GTP cyclohydrolase II.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 68994-19-4
References:
1. Burrows, R.B. and Brown, G.M. Presence of Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin. J. Bacteriol. 136 (1978) 657-667. [PMID: 30756]
Accepted name: methenyltetrahydromethanopterin cyclohydrolase
Reaction: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = 5-formyl-5,6,7,8-tetrahydromethanopterin
For diagram of reaction click here
Glossary: tetrahydromethanopterin
Other name(s): 5,10-methenyltetrahydromethanopterin cyclohydrolase; N5,N10-methenyltetrahydromethanopterin cyclohydrolase; methenyl-H4MPT cyclohydrolase; 5,10-methenyltetrahydromethanopterin 10-hydrolase (decyclizing)
Systematic name: 5,10-methenyltetrahydromethanopterin 10-hydrolase (ring-opening)
Comments: Methanopterin is a pterin analogue. The enzyme is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 99533-50-3
References:
1. Donnelly, M.I., Escalante-Semerena, J.C., Rinehart, K.L., Jr. and Wolfe, R.S. Methenyl-tetrahydromethanopterin cyclohydrolase in cell extracts of Methanobacterium. Arch. Biochem. Biophys. 242 (1985) 430-439. [PMID: 4062290]
Accepted name: S-adenosylhomocysteine deaminase
Reaction: S-adenosyl-L-homocysteine + H2O = S-inosyl-L-homocysteine + NH3
Other name(s): adenosylhomocysteine deaminase
Systematic name: S-adenosyl-L-homocysteine aminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 125149-24-8
References:
1. Zulty, J.J. and Speedie, M.K. Purification and characterization of S-adenosylhomocysteine deaminase from streptonigrin-producing Streptomyces flocculus. J. Bacteriol. 171 (1989) 6840-6844. [PMID: 2592350]
Accepted name: GTP cyclohydrolase IIa
Reaction: GTP + 3 H2O = 2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + 2 phosphate
For diagram of reaction, click here
Systematic name: GTP 8,9-hydrolase (phosphate-forming)
Comments: Requires Mg2+. This enzyme catalyses the hydrolysis of the imidazole ring of guanosine 5'-triphosphate, N7-methylguanosine 5'-triphosphate or inosine 5'-triphosphate. Xanthosine 5'-triphosphate and ATP are not substrates. It also catalyses the hydrolysis of diphosphate to form two equivalents of phosphate. Unlike GTP cyclohydrolase II (EC 3.5.4.25), this enzyme does not release formate, but does hydrolyse the diphosphate from GTP to phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Graham, D.E., Xu, H. and White, R.H. A member of a new class of GTP cyclohydrolases produces formylaminopyrimidine nucleotide monophosphates. Biochemistry 41 (2002) 15074-15084. [PMID: 12475257]
Accepted name: dCTP deaminase (dUMP-forming)
Reaction: dCTP + 2 H2O = dUMP + diphosphate + NH3
Systematic name: dCTP aminohydrolase (dUMP-forming)
Comments: Requires Mg2+. Is highly specific for dCTP as substrate as dCMP, CTP, CDP, CMP, cytosine or deoxycytosine are not deaminated. While most bacteria require two enzymes to form dUMP from dCTP (EC 3.5.4.13, dCTP deaminase and EC 3.6.1.23, dUTP diphosphatase), the archaeon Methanocaldococcus jannaschii uses a single enzyme to carry out both functions. This enzyme can also act as a dUTP diphosphatase, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Li, H., Xu, H., Graham, D.E. and White, R.H. The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase. J. Biol. Chem. 278 (2003) 11100-11106. [PMID: 12538648]
Accepted name: S-methyl-5'-thioadenosine deaminase
Reaction: S-methyl-5'-thioadenosine + H2O = S-methyl-5'-thioinosine + NH3
Other name(s): MTA deaminase; 5-methylthioadenosine deaminase
Systematic name: S-methyl-5'-thioadenosine amidohydrolase
Comments: The enzyme from Thermotoga maritima also functions as S-adenosylhomocysteine deaminase (EC 3.5.4.28) and has some activity against adenosine. Adenosine 5'-monophosphate and S-adenosyl-L-methionine (SAM) are not substrates.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Hermann, J.C., Marti-Arbona, R., Fedorov, A.A., Fedorov, E., Almo, S.C., Shoichet, B.K. and Raushel, F.M. Structure-based activity prediction for an enzyme of unknown function. Nature 448 (2007) 775-779. [PMID: 17603473]
Accepted name: 8-oxoguanine deaminase
Reaction: 8-oxoguanine + H2O = urate + NH3
Glossary: 8-oxoguanine = 2-amino-7,9-dihydro-1H-purine-6,8-dione
Other name(s): 8-OGD
Systematic name: 8-oxoguanine aminohydrolase
Comments: Zn2+ is bound in the active site. 8-Oxoguanine is formed via the oxidation of guanine within DNA by reactive oxygen species. If uncorrected, this modification leads to the incorporation of 8-oxoG:A mismatches and eventually to G:C to T:A transversions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Hall, R.S., Fedorov, A.A., Marti-Arbona, R., Fedorov, E.V., Kolb, P., Sauder, J.M., Burley, S.K., Shoichet, B.K., Almo, S.C. and Raushel, F.M. The hunt for 8-oxoguanine deaminase. J. Am. Chem. Soc. 132 (2010) 1762-1763. [PMID: 20088583]
Accepted name: tRNA(adenine34) deaminase
Reaction: adenine34 in tRNA + H2O = hypoxanthine34 in tRNA + NH3
Other name(s): tRNA:A34 deaminase; tadA protein; ADAT2-ADAT3 complex; TADA; tRNA adenosine deaminase arginine; AtTadA; tadA/ecADAT2; tRNA A:34 deaminase
Systematic name: tRNA(adenine34) aminohydrolase
Comments: The enzyme is involved in editing of tRNA. The active site contains Zn2+ [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Spears, J.L., Rubio, M.A., Gaston, K.W., Wywial, E., Strikoudis, A., Bujnicki, J.M., Papavasiliou, F.N. and Alfonzo, J.D. A single zinc ion is sufficient for an active Trypanosoma brucei tRNA editing deaminase. J. Biol. Chem. 286 (2011) 20366-20374. [PMID: 21507956]
2. Delannoy, E., Le Ret, M., Faivre-Nitschke, E., Estavillo, G.M., Bergdoll, M., Taylor, N.L., Pogson, B.J., Small, I., Imbault, P. and Gualberto, J.M. Arabidopsis tRNA adenosine deaminase arginine edits the wobble nucleotide of chloroplast tRNAArg(ACG) and is essential for efficient chloroplast translation. Plant Cell 21 (2009) 2058-2071. [PMID: 19602623]
3. Kuratani, M., Ishii, R., Bessho, Y., Fukunaga, R., Sengoku, T., Shirouzu, M., Sekine, S. and Yokoyama, S. Crystal structure of tRNA adenosine deaminase (TadA) from Aquifex aeolicus. J. Biol. Chem. 280 (2005) 16002-16008. [PMID: 15677468]
4. Wolf, J., Gerber, A.P. and Keller, W. tadA, an essential tRNA-specific adenosine deaminase from Escherichia coli. EMBO J. 21 (2002) 3841-3851. [PMID: 12110595]
5. Lee, W.H., Kim, Y.K., Nam, K.H., Priyadarshi, A., Lee, E.H., Kim, E.E., Jeon, Y.H., Cheong, C. and Hwang, K.Y. Crystal structure of the tRNA-specific adenosine deaminase from Streptococcus pyogenes. Proteins 68 (2007) 1016-1019. [PMID: 17554781]
6. Ragone, F.L., Spears, J.L., Wohlgamuth-Benedum, J.M., Kreel, N., Papavasiliou, F.N. and Alfonzo, J.D. The C-terminal end of the Trypanosoma brucei editing deaminase plays a critical role in tRNA binding. RNA 17 (2011) 1296-1306. [PMID: 21602302]
Accepted name: tRNAAla(adenine37) deaminase
Reaction: adenine37 in tRNAAla + H2O = hypoxanthine37 in tRNAAla + NH3
Other name(s): ADAT1; Tad1p
Systematic name: tRNAAla(adenine37) aminohydrolase
Comments: The enzyme deaminates adenosine37 to inosine in eukaryotic tRNAAla [1]. tRNA editing is strictly dependent on Mg2+ [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Maas, S., Gerber, A.P. and Rich, A. Identification and characterization of a human tRNA-specific adenosine deaminase related to the ADAR family of pre-mRNA editing enzymes. Proc. Natl. Acad. Sci. USA 96 (1999) 8895-8900. [PMID: 10430867]
2. Gerber, A., Grosjean, H., Melcher, T. and Keller, W. Tad1p, a yeast tRNA-specific adenosine deaminase, is related to the mammalian pre-mRNA editing enzymes ADAR1 and ADAR2. EMBO J. 17 (1998) 4780-4789. [PMID: 9707437]
3. Keegan, L.P., Gerber, A.P., Brindle, J., Leemans, R., Gallo, A., Keller, W. and O'Connell, M.A. The properties of a tRNA-specific adenosine deaminase from Drosophila melanogaster support an evolutionary link between pre-mRNA editing and tRNA modification. Mol. Cell Biol. 20 (2000) 825-833. [PMID: 10629039]
Accepted name: tRNA(cytosine8) deaminase
Reaction: cytosine8 in tRNA + H2O = uracil8 in tRNA + NH3
Other name(s): CDAT8
Systematic name: tRNA(cytosine8) aminohydrolase
Comments: The enzyme from Methanopyrus kandleri specifically catalyses the deamimation of cytosine at position 8 of tRNA in 30 different tRNAs. This cytosine-to-uracil editing guarantees the proper folding and functionality of the tRNAs.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Randau, L., Stanley, B.J., Kohlway, A., Mechta, S., Xiong, Y. and Söll, D. A cytidine deaminase edits C to U in transfer RNAs in Archaea. Science 324 (2009) 657-659. [PMID: 19407206]
Accepted name: mRNA(cytosine6666) deaminase
Reaction: cytosine6666 in apolipoprotein B mRNA + H2O = uracil6666 in apolipoprotein B mRNA + NH3
Other name(s): APOBEC-1 (catalytic component of an RNA-editing complex); APOBEC1 (catalytic subunit); apolipoprotein B mRNA-editing enzyme 1 (catalytic component of an RNA-editing complex); apoB mRNA-editing enzyme catalytic polypeptide 1 (catalytic component of an RNA-editing complex); apoB mRNA editing complex; apolipoprotein B mRNA editing enzyme; REPR
Systematic name: mRNA(cytosine6666) aminohydrolase
Comments: The apolipoprotein B mRNA editing enzyme complex catalyses the editing of apolipoprotein B mRNA at cytidine6666 to uridine, thereby transforming the codon for glutamine-2153 to a termination codon. Editing results in translation of a truncated apolipoprotein B isoform (apoB-48) with distinct functions in lipid transport. The catalytic component (APOBEC-1) contains zinc at the active site [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Chester, A., Weinreb, V., Carter, C.W., Jr. and Navaratnam, N. Optimization of apolipoprotein B mRNA editing by APOBEC1 apoenzyme and the role of its auxiliary factor, ACF. RNA 10 (2004) 1399-1411. [PMID: 15273326]
2. Fujino, T., Navaratnam, N., Jarmuz, A., von Haeseler, A. and Scott, J. C-→U editing of apolipoprotein B mRNA in marsupials: identification and characterisation of APOBEC-1 from the American opossum Monodelphus domestica. Nucleic Acids Res. 27 (1999) 2662-2671. [PMID: 10373583]
3. Barnes, C. and Smith, H.C. Apolipoprotein B mRNA editing in vitro is a zinc-dependent process. Biochem. Biophys. Res. Commun. 197 (1993) 1410-1414. [PMID: 8280158]
4. Chester, A., Somasekaram, A., Tzimina, M., Jarmuz, A., Gisbourne, J., O'Keefe, R., Scott, J. and Navaratnam, N. The apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decay. EMBO J. 22 (2003) 3971-3982. [PMID: 12881431]
Accepted name: double-stranded RNA adenine deaminase
Reaction: adenine in double-stranded RNA + H2O = hypoxanthine in double-stranded RNA + NH3
Other name(s): ADAR; double-stranded RNA adenosine deaminase; dsRAD; dsRNA adenosine deaminase; DRADA1; double-stranded RNA-specific adenosine deaminase
Systematic name: double-stranded RNA adenine aminohydrolase
Comments: This eukaryotic enzyme is involved in RNA editing. It destabilizes double-stranded RNA through conversion of adenosine to inosine. Inositol hexakisphosphate is required for activity [4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Hough, R.F. and Bass, B.L. Purification of the Xenopus laevis double-stranded RNA adenosine deaminase. J. Biol. Chem. 269 (1994) 9933-9939. [PMID: 8144588]
2. O'Connell, M.A., Gerber, A. and Keegan, L.P. Purification of native and recombinant double-stranded RNA-specific adenosine deaminases. Methods 15 (1998) 51-62. [PMID: 9614652]
3. Wong, S.K., Sato, S. and Lazinski, D.W. Substrate recognition by ADAR1 and ADAR2. RNA 7 (2001) 846-858. [PMID: 11421361]
4. Macbeth, M.R., Schubert, H.L., Vandemark, A.P., Lingam, A.T., Hill, C.P. and Bass, B.L. Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing. Science 309 (2005) 1534-1539. [PMID: 16141067]
Accepted name: single-stranded DNA cytosine deaminase
Reaction: cytosine in single-stranded DNA + H2O = uracil in single-stranded DNA + NH3
Other name(s): AID; activation-induced deaminase; AICDA (gene name); activation-induced cytidine deaminase
Systematic name: single-stranded DNA cytosine aminohydrolase
Comments: The enzyme exclusively catalyses deamination of cytosine in single-stranded DNA. It preferentially deaminates five-nucleotide bubbles. The optimal target consists of a single-stranded NWRCN motif (W = A or T, R = A or G) [2]. The enzyme initiates antibody diversification processes by deaminating immunoglobulin sequences.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Sohail, A., Klapacz, J., Samaranayake, M., Ullah, A. and Bhagwat, A.S. Human activation-induced cytidine deaminase causes transcription-dependent, strand-biased C to U deaminations. Nucleic Acids Res. 31 (2003) 2990-2994. [PMID: 12799424]
2. Larijani, M., Petrov, A.P., Kolenchenko, O., Berru, M., Krylov, S.N. and Martin, A. AID associates with single-stranded DNA with high affinity and a long complex half-life in a sequence-independent manner. Mol. Cell Biol. 27 (2007) 20-30. [PMID: 17060445]
3. Brar, S.S., Sacho, E.J., Tessmer, I., Croteau, D.L., Erie, D.A. and Diaz, M. Activation-induced deaminase, AID, is catalytically active as a monomer on single-stranded DNA. DNA Repair (Amst.) 7 (2008) 77-87. [PMID: 17889624]
4. Larijani, M. and Martin, A. Single-stranded DNA structure and positional context of the target cytidine determine the enzymatic efficiency of AID. Mol. Cell Biol. 27 (2007) 8038-8048. [PMID: 17893327]
5. Verma, S., Goldammer, T. and Aitken, R. Cloning and expression of activation induced cytidine deaminase from Bos taurus. Vet. Immunol. Immunopathol. 134 (2010) 151-159. [PMID: 19766322]
Accepted name: GTP cyclohydrolase IV
Reaction: GTP + H2O = 7,8-dihydroneopterin 2',3'-cyclic phosphate + formate + diphosphate
For diagram of reaction click here.
Glossary: 7,8-dihydroneopterin 2',3'-cyclic phosphate = 2-amino-6-{(S)-hydroxy[(4R)-2-hydroxy-2-oxido-1,3,2-dioxaphospholan-4-yl]methyl}-7,8-dihydropteridin-4(1H)-one = 2-amino-6-[(1S,2R)-1,2,3-trihydroxypropyl]-7,8-dihydro-4(1H)-pteridinone 1,2-cyclic phosphate
Other name(s): MptA; GTP cyclohydrolase MptA
Systematic name: GTP 7,8-8,9-dihydrolase (cyclizing, formate-releasing, diphosphate-releasing)
Comments: Requires Fe2+. A zinc protein. The enzyme is involved in methanopterin biosynthesis in methanogenic archaea. cf. GTP cyclohydrolase I (EC 3.5.4.16), GTP cyclohydrolase II (EC 3.5.4.25) and GTP cyclohydrolase IIa (EC 3.5.4.29).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Grochowski, L.L., Xu, H., Leung, K. and White, R.H. Characterization of an Fe2+-dependent archaeal-specific GTP cyclohydrolase, MptA, from Methanocaldococcus jannaschii. Biochemistry 46 (2007) 6658-6667. [PMID: 17497938]
Accepted name: aminodeoxyfutalosine deaminase
Reaction: 6-amino-6-deoxyfutalosine + H2O = futalosine + NH3
For diagram of reaction click here.
Glossary: 6-amino-6-deoxyfutalosine = 3-{3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]propanoyl}benzoate
futalosine = 3-{3-[(3S,4R)-3,4-dihydroxy-5-(6-oxo-1,6-dihydro-9H-purin-9-yl)tetrahydrofuran-2-yl]propanoyl}benzoate
Other name(s): AFL deaminase; aminofutalosine deaminase; mqnX (gene name)
Systematic name: 6-amino-6-deoxyfutalosine deaminase
Comments: The enzyme, found in several bacterial species, is part of the futalosine pathway for menaquinone biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Arakawa, C., Kuratsu, M., Furihata, K., Hiratsuka, T., Itoh, N., Seto, H. and Dairi, T. Diversity of the early step of the futalosine pathway. Antimicrob. Agents Chemother. 55 (2011) 913-916. [PMID: 21098241]
2. Goble, A.M., Toro, R., Li, X., Ornelas, A., Fan, H., Eswaramoorthy, S., Patskovsky, Y., Hillerich, B., Seidel, R., Sali, A., Shoichet, B.K., Almo, S.C., Swaminathan, S., Tanner, M.E. and Raushel, F.M. Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by distantly related enzymes. Biochemistry 52 (2013) 6525-6536. [PMID: 23972005]
Accepted name: 5'-deoxyadenosine deaminase
Reaction: 5'-deoxyadenosine + H2O = 5'-deoxyinosine + NH3
Other name(s): MJ1541 (gene name); DadD
Systematic name: 5'-deoxyadenosine aminohydrolase
Comments: The enzyme from the archaeon Methanocaldococcus jannaschii is involved in the recycling of 5'-deoxyadenosine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Miller, D., O'Brien, K., Xu, H. and White, R.H. Identification of a 5'-deoxyadenosine deaminase in Methanocaldococcus jannaschii and its possible role in recycling the radical S-adenosylmethionine enzyme reaction product 5'-deoxyadenosine. J. Bacteriol. 196 (2014) 1064-1072. [PMID: 24375099]
Accepted name: N-isopropylammelide isopropylaminohydrolase
Reaction: N-isopropylammelide + H2O = cyanuric acid + isopropylamine
For diagram of reaction click here.
Glossary: N-isopropylammelide = 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine
cyanuric acid = 1,3,5-triazine-2,4,6(1H,3H,5H)-trione = 2,4,6-trihydroxy-s-triazine
Other name(s): atzC (gene name)
Systematic name: N-isopropylammelide isopropylaminohydrolase
Comments: Requires Zn2+. This bacterial enzyme is involved indegradation of the herbicide atrazine. It can hydrolyse other N-substituted amino dihydroxy-s-triazine molecules, and prefers substrates with linear N-alkyl groups to those with branched alkyl groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sadowsky, M.J., Tong, Z., de Souza, M. and Wackett, L.P. AtzC is a new member of the amidohydrolase protein superfamily and is homologous to other atrazine-metabolizing enzymes. J. Bacteriol. 180 (1998) 152-158. [PMID: 9422605]
2. Shapir, N., Osborne, J.P., Johnson, G., Sadowsky, M.J. and Wackett, L.P. Purification, substrate range, and metal center of AtzC: the N-isopropylammelide aminohydrolase involved in bacterial atrazine metabolism. J. Bacteriol. 184 (2002) 5376-5384. [PMID: 12218024]
3. Balotra, S., Warden, A.C., Newman, J., Briggs, L.J., Scott, C. and Peat, T.S. X-ray structure and mutagenesis studies of the N-isopropylammelide isopropylaminohydrolase, AtzC. PLoS One 10 (2015) e0137700. [PMID: 26390431]
Accepted name: hydroxydechloroatrazine ethylaminohydrolase
Reaction: hydroxyatrazine + H2O = N-isopropylammelide + ethylamine
For diagram of reaction click here.
Glossary: hydroxyatrazine = 4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine
N-isopropylammelide = 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine
Other name(s): atzB (gene name); 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine ethylaminohydrolase
Systematic name: hydroxyatrazine ethylaminohydrolase
Comments: Contains Zn2+. This bacterial enzyme is involved indegradation of the herbicide atrazine. The enzyme has a broad substrate range, and requires a monohydroxylated s-triazine ring with a minimum of one primary or secondary amine substituent and either a chloride or amine leaving group. It catalyses both deamination and dechlorination reactions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Boundy-Mills, K.L., de Souza, M.L., Mandelbaum, R.T., Wackett, L.P. and Sadowsky, M.J. The atzB gene of Pseudomonas sp. strain ADP encodes the second enzyme of a novel atrazine degradation pathway. Appl. Environ. Microbiol. 63 (1997) 916-923. [PMID: 9055410]
2. Seffernick, J.L., Aleem, A., Osborne, J.P., Johnson, G., Sadowsky, M.J. and Wackett, L.P. Hydroxyatrazine N-ethylaminohydrolase (AtzB): an amidohydrolase superfamily enzyme catalyzing deamination and dechlorination. J. Bacteriol. 189 (2007) 6989-6997. [PMID: 17660279]
Accepted name: ectoine hydrolase
Reaction: ectoine + H2O = (2S)-2-acetamido-4-aminobutanoate
Glossary: ectoine = (4S)-2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylate
Other name(s): doeA (gene name)
Systematic name: ectoine aminohydrolase
Comments: The enzyme, found in some halophilic bacteria, is involved in the degradation of the compatible solute ectoine. The enzyme, which belongs to peptidase family M24, only acts in the direction of ectoine hydrolysis. It also produces smaller amounts of N4-acetyl-L-2,4-diaminobutanoate, which is recycled back to ectoine by EC 4.2.1.108, ectoine synthase.
BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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: melamine deaminase
Reaction: (1) melamine + H2O = ammeline + NH3
(2) ammeline + H2O = ammelide + NH3
Glossary: melamine = 2,4,6-triamino-1,3,5-triazine
ammeline = 4,6-diamino-1,3,5-triazin-2-ol
ammelide = 6-amino-1,3,5-triazine-2,4-diol
Other name(s): triA (gene name)
Systematic name: melamine aminohydrolase
Comments: The enzyme, isolated from the bacterium Acidovorax citrulli, performs the deamination of melamine 15-fold faster than the deamination of ammeline. It also has activity with 2-chloro-4,6-diamino-s-triazine, but has no activity toward halo-substituted triazine ring compounds such as atrazine (cf. EC 3.8.1.8, atrazine chlorohydrolase).
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Seffernick, J.L., Souza, M.L., Sadowsky, M.J. and Wackett, L.P. Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but functionally different. J. Bacteriol. 183 (2001) 2405-2410. [PMID: 11274097]
Accepted name: cAMP deaminase
Reaction: 3',5'-cyclic AMP + H2O = 3',5'-cyclic IMP + NH3
Other name(s): cyclic adenylate deaminase; CadD
Systematic name: 3',5'-cyclic AMP aminohydrolase
Comments: Requires Zn2+. The enzyme, isolated from the bacterium Leptospira interrogans, is specific for cAMP.
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Goble, A.M., Feng, Y., Raushel, F.M. and Cronan, J.E. Discovery of a cAMP deaminase that quenches cyclic AMP-dependent regulation. ACS Chem. Biol. 8 (2013) 2622-2629. [PMID: 24074367]
Accepted name: nitrilase
Reaction: A nitrile + 2 H2O = a carboxylate + NH3
Other name(s): acetonitrilase; benzonitrilase
Systematic name: nitrile aminohydrolase
Comments: Acts on a wide range of aromatic nitriles including (indole-3-yl)acetonitrile, and also on some aliphatic nitriles, and on the corresponding acid amides. cf. EC 4.2.1.84 nitrile hydratase.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9024-90-2
References:
1. Harper, D.B. Microbial metabolism of aromatic nitriles. Enzymology of C-N cleavage by Nocardia sp. (rhodochrous group) N.C.I.B. 11216. Biochem. J. 165 (1977) 309-319. [PMID: 21655]
2. Thimann, K.V. and Mahadevan, S. Nitrilase. I. Occurrence, preparation, and general properties of the enzyme. Arch. Biochem. Biophys. 105 (1964) 133-141.
3. Pace, H.C. and Brenner, C. The nitrilase superfamily: classification, structure and function. Genome Biol. 2 (2001) 0001.1-0001.9. [PMID: 11380987]
Accepted name: ricinine nitrilase
Reaction: ricinine + 2 H2O = 3-carboxy-4-methoxy-N-methyl-2-pyridone + NH3
For reaction pathway click here.
Systematic name: ricinine aminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9075-40-5
References:
1. Robinson, W.G. and Hook, R.H. Ricinine nitrilase. I. Reaction product and substrate specificity.J. Biol. Chem. 239 (1964) 4257-4262. [PMID: 14247679]
2. Hook, R.H. and Robinson, W.G. Ricinine nitrilase. II. Purification and properties.J. Biol. Chem. 239 (1964) 4263-4267. [PMID: 14247680]
3. Pace, H.C. and Brenner, C. The nitrilase superfamily: classification, structure and function. Genome Biol. 2 (2001) 0001.1-0001.9. [PMID: 11380987]
[EC 3.5.5.3 Transferred entry: now EC 4.2.1.104 cyanate hydratase (EC 3.5.5.3 created 1972, deleted 1990)]
Accepted name: cyanoalanine nitrilase
Reaction: 3-cyano-L-alanine + 2 H2O = L-aspartate + NH3 (overall reaction)
(1a) 3-cyano-L-alanine + H2O = L-asparagine
(1b) L-asparagine + H2O = L-aspartate + NH3
Other name(s): β-cyanoalanine nitrilase
Systematic name: 3-cyano-L-alanine aminohydrolase
Comments: L-Asparagine is formed as an intermediate. cf. EC 4.2.1.65, 3-cyanoalanine hydratase and EC 3.5.1.1, asparaginase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 85638-44-4
References:
1. Yanase, H., Sakai, T. and Tonomuro, K. Purification, crystallization and some properties of β-cyano-L-alanine-degrading enzyme in Pseudomonas sp. 13. Agric. Biol. Chem. 47 (1983) 473-482.
Accepted name: arylacetonitrilase
Reaction: 4-chlorophenylacetonitrile + 2 H2O = 4-chlorophenylacetate + NH3
Systematic name: arylacetonitrile aminohydrolase
Comments: Requires thiol compounds. Also hydrolyses other 4-substituted phenylacetonitriles, thien-2-ylacetonitrile, tolylacetonitriles, and, more slowly, benzyl cyanide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 132053-06-6
References:
1. Mauger, J., Nagasawa, T. and Yamada, H. Occurrence of a novel nitrilase, arylacetonitrilase, in Alcaligenes faecalis JM3. Arch. Microbiol. 155 (1990) 1-6.
2. Nagasawa, T., Mauger, J. and Yamada, H. A novel nitrilase, arylacetonitrilase, of Alcaligenes faecalis JM3. Purification and characterization. Eur. J. Biochem. 194 (1990) 765-772. [PMID: 2269298]
Accepted name: bromoxynil nitrilase
Reaction: 3,5-dibromo-4-hydroxybenzonitrile + 2 H2O = 3,5-dibromo-4-hydroxy-benzoate + NH3
Systematic name: 3,5-dibromo-4-hydroxybenzonitrile aminohydrolase
Comments: Involved in the bacterial degradation of the herbicide bromoxynil. Highly specific.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 157857-12-0
References:
1. Stalker, D.M., Malyj, L.D. and McBride, K.E. Purification and properties of a nitrilase specific for the herbicide bromoxynil and corresponding nucleotide sequence analysis of the bxn gene. J. Biol. Chem. 263 (1988) 6310-6314. [PMID: 2834373]
Accepted name: aliphatic nitrilase
Reaction: R-CN + 2 H2O = R-COOH + NH3
Systematic name: aliphatic nitrile aminohydrolase
Comments: preferentially hydrolyses aliphatic nitriles, some of which are apparently not substrates for other known nitrilases (EC 3.5.5.1). Substrates include crotononitrile, acrylonitrile and glutaronitrile.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 395644-15-2
References:
1. Kobayashi, M., Yanaka, N., Nagasawa, T., Yamada, H. Primary structure of an aliphatic nitrile-degrading enzyme, aliphatic nitrilase from Rhodococcus rhodochrous K22 and expression of its gene and identification of its active site residue. Biochemistry 31 (1992) 9000-9007. [PMID: 1390687]
2. Pace, H.C. and Brenner, C. The nitrilase superfamily: classification, structure and function. Genome Biol. 2 (2001) 0001.1-0001.9. [PMID: 11380987]
Accepted name: thiocyanate hydrolase
Reaction: thiocyanate + 2 H2O = carbonyl sulfide + NH3 + HO-
Systematic name: thiocyanate aminohydrolase
Comments: The enzyme from Thiobacillus thioparus catalyses the first step in the degradation of thiocyanate.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 142539-65-9
References:
1. Katayama, Y., Matsushita, Y., Kaneko, M., Kondo, M., Mizuno, T. and Nyunoya, H. Cloning of genes coding for the three subunits of thiocyanate hydrolase of Thiobacillus thioparus THI 115 and their evolutionary relationships to nitrile hydratase. J. Bacteriol. 180 (1998) 2583-2589. [PMID: 9573140]
2. Katayama, Y., Narahara, Y., Inoue, Y., Amano, F., Kanagawa, T. and Kuraishi, H. A thiocyanate hydrolase of Thiobacillus thioparus. J. Biol. Chem. 267 (1992) 9170-9175. [PMID: 1577754]
Accepted name: riboflavinase
Reaction: riboflavin + H2O = ribitol + lumichrome
Systematic name: riboflavin hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9024-79-7
References:
1. Yanagita, T. and Foster, J.W. A bacterial riboflavin hydrolase. J. Biol. Chem. 221 (1956) 593-607.
Accepted name: aminopyrimidine aminohydrolase
Reaction: (1) 4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
(2) thiamine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
Other name(s): thiaminase (ambiguous); thiaminase II, tenA (gene name)
Systematic name: 4-amino-5-aminomethyl-2-methylpyrimidine aminohydrolase
Comments: Previously known as thiaminase II, this enzyme is involved in the regeneration of the thiamine pyrimidine from degraded products, rather than in thiamine degradation, and participates in thiamine salvage pathways.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9024-80-0
References:
1. Fujita, A., Nose, Y. and Kuratani, K. Second type of bacterial thiaminase. J. Vitaminol. (Kyoto) 1 (1954) 1-7. [PMID: 13243520]
2. Ikehata, H. Purification of thiaminase II. J. Gen. Appl. Microbiol. 6 (1960) 30-39.
3. Toms, A.V., Haas, A.L., Park, J.H., Begley, T.P. and Ealick, S.E. Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II. Biochemistry 44 (2005) 2319-2329. [PMID: 15709744]
4. Benach, J., Edstrom, W.C., Lee, I., Das, K., Cooper, B., Xiao, R., Liu, J., Rost, B., Acton, T.B., Montelione, G.T. and Hunt, J.F. The 2.35 Å structure of the TenA homolog from Pyrococcus furiosus supports an enzymatic function in thiamine metabolism. Acta Crystallogr. D Biol. Crystallogr. 61 (2005) 589-598. [PMID: 15858269]
5. Jenkins, A.H., Schyns, G., Potot, S., Sun, G. and Begley, T.P. A new thiamin salvage pathway. Nat. Chem. Biol. 3 (2007) 492-497. [PMID: 17618314]
6. Jenkins, A.L., Zhang, Y., Ealick, S.E. and Begley, T.P. Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis. Bioorg. Chem. 36 (2008) 29-32. [PMID: 18054064]
7. French, J.B., Begley, T.P. and Ealick, S.E. Structure of trifunctional THI20 from yeast. Acta Crystallogr. D Biol. Crystallogr. 67 (2011) 784-791. [PMID: 21904031]
[EC 3.5.99.3 Transferred entry: hydroxydechloroatrazine ethylaminohydrolase, now classified as EC 3.5.4.43, hydroxydechloroatrazine ethylaminohydrolase (EC 3.5.99.3 created 2000, deleted 2016)]
EC 3.5.99.4 Transferred entry: N-isopropylammelide isopropylaminohydrolase, now classified as EC 3.5.4.42, N-isopropylammelide isopropylaminohydrolase (EC 3.5.99.4 created 2000, deleted 2016)]
Accepted name: 2-aminomuconate deaminase
Reaction: 2-aminomuconate + H2O = (3E)-2-oxohex-3-enedioate + NH3
Other name(s): amnD (gene name); nbaF (gene name)
Systematic name: 2-aminomuconate aminohydrolase
Comments: 2-Aminomuconate is an intermediate in the bacterial biodegradation of nitrobenzene. The enzyme has been isolated from several species, including Pseudomonas pseudocaligenes JS45, Pseudomonas fluorescens KU-7, Pseudomonas sp. AP3 and Burkholderia cenocepacia J2315. The reaction is spontaneous in acid conditions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 201098-29-5
References:
1. He, Z and Spain, J.C. Studies of the catabolic pathway of degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45: removal of the amino group from 2-aminomuconic semialdehyde. Appl. Environ. Microbiol. 63 (1997) 4839-4843. [PMID: 9471964]
2. He, Z. and Spain, J.C. A novel 2-aminomuconate deaminase in the nitrobenzene degradation pathway of Pseudomonas pseudoalcaligenes JS45. J. Bacteriol. 180 (1998) 2502-2506. [PMID: 9573204]
3. Takenaka, S., Murakami, S., Kim, Y.J. and Aoki, K. Complete nucleotide sequence and functional analysis of the genes for 2-aminophenol metabolism from Pseudomonas sp. AP-3. Arch. Microbiol. 174 (2000) 265-272. [PMID: 11081795]
4. Muraki, T., Taki, M., Hasegawa, Y., Iwaki, H. and Lau, P.C. Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7. Appl. Environ. Microbiol. 69 (2003) 1564-1572. [PMID: 12620844]
Accepted name: glucosamine-6-phosphate deaminase
Reaction: α-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3
For diagram click here.
Other name(s): glucosaminephosphate isomerase (ambiguous); glucosamine-6-phosphate isomerase (ambiguous); phosphoglucosaminisomerase (ambiguous); glucosamine phosphate deaminase; aminodeoxyglucosephosphate isomerase (ambiguous); phosphoglucosamine isomerase (ambiguous); 2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing)
Systematic name: 2-amino-2-deoxy-α-D-glucose-6-phosphate aminohydrolase (ketol isomerizing)
Comments: The enzyme uses ring opening and isomerization of the aldose-ketose type to convert the -CH(-NH2)-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH2-OH, forming 2-deoxy-2-imino-D-arabino-hexitol, which then hydrolyses to yield fructose 6-phosphate and ammonia. N-Acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9013-10-9
References:
1. Wolfe, J.B., Britton, B.B., Nakada, H.I. Glucosamine degradation by Escherichia coli. III. Isolation and studies of "phosphoglucosaminisomerase". Arch. Biochem. Biophys. 66 (1957) 333-339. [PMID: 13403679]
2. Comb, D.G., Roseman, S. Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase. J. Biol. Chem. 232 (1958) 807-827. [PMID: 13549465]
3. Pattabiraman, T.N., Bachhawat, B.K. Purification of glucosamine 6-phosphate deaminase from human brain. Biochim. Biophys. Acta 54 (1961) 273-283. [PMID: 14484386]
4. Liu, C., Li, D., Liang, Y.H., Li, L.F. and Su, X.D. Ring-opening mechanism revealed by crystal structures of NagB and its ES intermediate complex. J. Mol. Biol. 379 (2008) 73-81. [PMID: 18436239]
Accepted name: 1-aminocyclopropane-1-carboxylate deaminase
Reaction: 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3 (overall reaction)
(1a) 1-aminocyclopropane-1-carboxylate = 2-aminobut-2-enoate
(1b) 2-aminobut-2-enoate = 2-iminobutanoate (spontaneous)
(1c) 2-iminobutanoate + H2O = 2-oxobutanoate + NH3 (spontaneous)
Other name(s): 1-aminocyclopropane-1-carboxylate endolyase (deaminating); ACC deaminase; 1-aminocyclopropane carboxylic acid deaminase
Systematic name: 1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing)
Comments: A pyridoxal 5'-phosphate enzyme. The enzyme, found in certain soil bacteria and fungi, catalyses the ring opening of 1-aminocyclopropane-1-carboxylate, the immediate precursor to ethylene, an important plant hormone that regulates fruit ripening and other processes. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 69553-48-6
References:
1. Honma, M. and Shimomura, T. Metabolism of 1-aminocyclopropane-1-carboxylic acid. Agric. Biol. Chem. 42 (1978) 1825-1831.
2. Yao, M., Ose, T., Sugimoto, H., Horiuchi, A., Nakagawa, A., Wakatsuki, S., Yokoi, D., Murakami, T., Honma, M. and Tanaka, I. Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus. J. Biol. Chem. 275 (2000) 34557-34565. [PMID: 10938279]
3. Thibodeaux, C.J. and Liu, H.W. Mechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase: characterization of an unusual pyridoxal 5'-phosphate-dependent reaction. Biochemistry 50 (2011) 1950-1962. [PMID: 21244019]
Accepted name: 5-nitroanthranilic acid aminohydrolase
Reaction: 5-nitroanthranilate + H2O = 5-nitrosalicylate + NH3
Other name(s): naaA (gene name); 5NAA deaminase
Systematic name: 5-nitroanthranilate amidohydrolase
Comments: The enzyme catalyses the initial step in biodegradation of 5-nitroanthranilic acid by Bradyrhizobium sp. strain JS329.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Qu, Y. and Spain, J.C. Biodegradation of 5-nitroanthranilic acid by Bradyrhizobium sp. strain JS329. Appl. Environ. Microbiol. 76 (2010) 1417-1422. [PMID: 20081004]
EC 3.5.99.9
Accepted name: 2-nitroimidazole nitrohydrolase
Reaction: 2-nitroimidazole + H2O = imidazol-2-one + nitrite
Other name(s): NnhA; 2NI nitrohydrolase; 2NI denitrase
Systematic name: 2-nitroimidazole nitrohydrolase
Comments: The enzyme catalyses the initial step in the biodegradation of 2-nitroimidazole by the soil bacterium Mycobacterium sp. JS330
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Qu, Y. and Spain, J.C. Catabolic pathway for 2-nitroimidazole involves a novel nitrohydrolase that also confers drug resistance. Environ Microbiol 13 (2011) 1010-1017. [PMID: 21244596]
Accepted name: 2-iminobutanoate/2-iminopropanoate deaminase
Reaction: (1) 2-iminobutanoate + H2O = 2-oxobutanoate + NH3
Other name(s): yjgF (gene name); ridA (gene name); enamine/imine deaminase (ambiguous)
Systematic name: 2-iminobutanoate aminohydrolase
Comments: This enzyme, which has been found in all species and tissues examined, catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
PDB,
CAS registry number:
References:
1. Lambrecht, J.A., Flynn, J.M. and Downs, D.M. Conserved YjgF protein family deaminates reactive enamine/imine intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme reactions. J. Biol. Chem. 287 (2012) 3454-3461. [PMID: 22094463]
Accepted name: 2-aminomuconate deaminase (2-hydroxymuconate-forming)
Reaction: 2-aminomuconate + H2O = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NH3
Glossary: 2-aminomuconate = (2Z,4E)-2-aminohexa-2,4-dienedioate
Other name(s): cnbZ (gene name)
Systematic name: 2-aminomuconate aminohydrolase [(2Z,4E)-2-hydroxyhexa-2,4-dienedioate-forming]
Comments: The enzyme, characterized from the bacterium Comamonas testosteroni CNB-1, converts 2-aminomuconate to 2-hydroxyhexa-2,4-dienedioate, unlike the enzymes from Pseudomonas, which produce (3E)-2-oxohex-3-enedioate (see EC 3.5.99.5, 2-aminomuconate deaminase). The enzyme also acts on 2-amino-5-chloromuconate.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Liu, L., Wu, J.F., Ma, Y.F., Wang, S.Y., Zhao, G.P. and Liu, S.J. A novel deaminase involved in chloronitrobenzene and nitrobenzene degradation with Comamonas sp. strain CNB-1. J. Bacteriol. 189 (2007) 2677-2682. [PMID: 17259310]
Accepted name: salsolinol synthase
Reaction: (R)-salsolinol + H2O = dopamine + acetaldehyde
For diagram of reaction click here
Glossary: (R)-salsolinol = (+)-salsolinol = (1R)-1,2,3,4-tetrahydro-1-methylisoquinoline-6,7-diol
Other name(s): Sal synthase
Systematic name: (R)-salsolinol dopamine-hydrolase (acetaldehyde-forming)
Comments: The enzyme, present in mammalian brains, forms the catechol isoquinoline (R)-salsolinol. This compound can be metabolized to (R)-N-methylsalsolinol, a 1-methyl-4-phenylpyridinium-like neurotoxin that impairs the function of dopaminergic neurons, causing the clinical symptoms of Parkinson's disease.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Naoi, M., Maruyama, W., Dostert, P., Kohda, K. and Kaiya, T. A novel enzyme enantio-selectively synthesizes (R)-salsolinol, a precursor of a dopaminergic neurotoxin, N-methyl-(R)-salsolinol. Neurosci. Lett. 212 (1996) 183-186. [PMID: 8843103]
2. Naoi, M., Maruyama, W., Takahashi, T., Akao, Y. and Nakagawa, Y. Involvement of endogenous N-methyl-(R)-salsolinol in Parkinson's disease: induction of apoptosis and protection by (–)deprenyl. J Neural Transm Suppl (2000) 111-121. [PMID: 11128601]
3. Chen, X., Zheng, X., Ali, S., Guo, M., Zhong, R., Chen, Z., Zhang, Y., Qing, H. and Deng, Y. Isolation and sequencing of salsolinol synthase, an enzyme catalyzing salsolinol biosynthesis. ACS Chem Neurosci 9 (2018) 1388-1398. [PMID: 29602279]
4. Xiong, Q., Zheng, X., Wang, J., Chen, Z., Deng, Y., Zhong, R., Wang, J. and Chen, X. Sal synthase induced cytotoxicity of PC12 cells through production of the dopamine metabolites salsolinol and N-methyl-salsolinol. J Integr Neurosci 21 (2022) 71. [PMID: 35364659]
Accepted name: strictosidine synthase
Reaction: 3-α(S)-strictosidine + H2O = tryptamine + secologanin
For diagram of reaction click here
Other name(s): strictosidine synthetase; STR; 3-α(S)-strictosidine tryptamine-lyase; 3-α(S)-strictosidine tryptamine-lyase (secologanin-forming)
Systematic name: 3-α(S)-strictosidine tryptamine-hydrolase (secologanin-forming)
Comments: Catalyses a Pictet-Spengler reaction between the aldehyde group of secologanin and the amino group of tryptamine [4,5]. Involved in the biosynthesis of the monoterpenoid indole alkaloids.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Treimer, J.K. and Zenk, M.H. Purification and properties of strictosidine synthase, the key enzyme in indole alkaloid formation. Eur. J. Biochem. 101 (1979) 225-233. [PMID: 510306]
2. Kutchan, T.M. Strictosidine: from alkaloid to enzyme to gene. Phytochemistry 32 (1993) 493-506. [PMID: 7763429]
3. de Waal, A., Meijer, A.H. and Verpoorte, R. Strictosidine synthase from Catharanthus roseus: purification and characterization of multiple forms. Biochem. J. 306 (1995) 571-580. [PMID: 7887913]
4. Ruppert, M., Woll, J., Giritch, A., Genady, E., Ma, X. and Stöckigt, J. Functional expression of an ajmaline pathway-specific esterase from
Rauvolfia in a novel plant-virus expression system. Planta 222 (2005) 888-898. [PMID: 16133216]
5. McCoy, E., Galan, M.C. and O'Connor, S.E. Substrate specificity of strictosidine synthase. Bioorg. Med. Chem. Lett. 16 (2006) 2475-2478. [PMID: 16481164]
6. Ma, X., Panjikar, S., Koepke, J., Loris, E. and Stöckigt, J. The structure of Rauvolfia serpentina strictosidine synthase is a novel six-bladed β-propeller fold in plant proteins. Plant Cell 18 (2006) 907-920. [PMID: 16531499]
Accepted name: (S)-norcoclaurine synthase
Reaction: (S)-norcoclaurine + H2O = dopamine + 4-hydroxyphenylacetaldehyde
For diagram of reaction, click here
Glossary: dopamine = 4-(2-aminoethyl)benzene-1,2-diol
Other name(s): (S)-norlaudanosoline synthase; 4-hydroxyphenylacetaldehyde hydro-lyase (adding dopamine); 4-hydroxyphenylacetaldehyde hydro-lyase [adding dopamine; (S)-norcoclaurine-forming]
Systematic name: (S)-norcoclaurine dopamine hydrolase (4-hydroxyphenylacetaldehyde-forming)
Comments: The reaction makes a six-membered ring by forming a bond between C-6 of the 3,4-dihydroxyphenyl group of the dopamine and C-1 of the aldehyde in the imine formed between the substrates. The product is the precursor of the benzylisoquinoline alkaloids in plants. The enzyme, formerly known as (S)-norlaudanosoline synthase, will also catalyse the reaction of 4-(2-aminoethyl)benzene-1,2-diol + (3,4-dihydroxyphenyl)acetaldehyde to form (S)-norlaudanosoline, but this alkaloid has not been found to occur in plants.
Links to other databases:
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References:
1. Stadler, R., Zenk, M.H. A revision of the generally accepted pathway for the biosynthesis of the benzyltetrahydroisoquinoline reticuline. Liebigs Ann. Chem. (1990) 555-562.
2. Stadler, R., Kutchan, T.M., Zenk, M.H. (S)-Norcoclaurine is the central intermediate in benzylisoquinoline alkaloid biosynthesis. Phytochemistry 28 (1989) 1083-1086.
3. Samanani, N. and Facchini, P.J. Purification and characterization of norcoclaurine synthase. The first committed enzyme in benzylisoquinoline alkaloid biosynthesis in plants. J. Biol. Chem. 277 (2002) 33878-33883. [PMID: 12107162]
Accepted name: deacetylisoipecoside synthase
Reaction: deacetylisoipecoside + H2O = dopamine + secologanin
For diagram of reaction, click here
Glossary: dopamine = 4-(2-aminoethyl)benzene-1,2-diol
Other name(s): deacetylisoipecoside dopamine-lyase; deacetylisoipecoside dopamine-lyase (secologanin-forming)
Systematic name: deacetylisoipecoside dopamine-hydolase (secologanin-forming)
Comments: The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 3.5.99.16, deacetylipecoside synthase. The product is rapidly converted to demethylisoalangiside.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. DeEknamkul, W., Ounaroon, A., Tanahashi, T., Kutchan, T. and Zenk, M.H. Enzymatic condensation of dopamine and secologanin by cell-free extracts of Alangium lamarckii. Phytochemistry 45 (1997) 477-484.
Accepted name: deacetylipecoside synthase
Reaction: deacetylipecoside + H2O = dopamine + secologanin
For diagram of reaction click here
Glossary: dopamine = 4-(2-aminoethyl)benzene-1,2-diol
Other name(s): deacetylipecoside dopamine-lyase; deacetylipecoside dopamine-lyase (secologanin-forming)
Systematic name: deacetylipecoside dopamine-hydroyase (secologanin-forming)
Comments: The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 3.5.99.15, deacetylisoipecoside synthase. The product is rapidly converted to demethylalangiside.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. DeEknamkul, W., Ounaroon, A., Tanahashi, T., Kutchan, T. and Zenk, M.H. Enzymatic condensation of dopamine and secologanin by cell-free extracts of Alangium lamarckii. Phytochemistry 45 (1997) 477-484.
2. De-Eknamkul, W., Suttipanta, N. and Kutchan, T.M. Purification and characterization of deacetylipecoside synthase from Alangium lamarckii Thw. Phytochemistry 55 (2000) 177-181. [PMID: 11065292]
(2) 2-iminopropanoate + H2O = pyruvate + NH3
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (2Z,4E)-2-hydroxymuconate
Continued with EC 3.6.1 and EC 3.6.2
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