The Enzyme Database

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EC 2.5.1.47     
Accepted name: cysteine synthase
Reaction: O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
For diagram of O3-Acetyl-L-serine metabolism, click here
Glossary: O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid
Other name(s): O-acetyl-L-serine sulfhydrylase; O-acetyl-L-serine sulfohydrolase; O-acetylserine (thiol)-lyase; O-acetylserine (thiol)-lyase A; O-acetylserine sulfhydrylase; O3-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide); acetylserine sulfhydrylase; cysteine synthetase; S-sulfocysteine synthase; 3-O-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase; O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
Systematic name: O-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
Comments: A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (β-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37290-89-4
References:
1.  Becker, M.A., Kredich, N.M. and Tomkins, G.M. The purification and characterization of O-acetylserine sulfhydrylase-A from Salmonella typhimurium. J. Biol. Chem. 244 (1969) 2418–2427. [PMID: 4891157]
2.  Hara, S., Payne, M.A., Schnackerz, K.D. and Cook, P.F. A rapid purification procedure and computer-assisted sulfide ion selective electrode assay for O-acetylserine sulfhydrylase from Salmonella typhimurium. Protein Expr. Purif. 1 (1990) 70–76. [PMID: 2152186]
3.  Ikegami, F., Kaneko, M., Lambein, F., Kuo, Y.-H. and Murakoshi, I. Difference between uracilylalanine synthases and cysteine synthases in Pisum sativum. Phytochemistry 26 (1987) 2699–2704.
4.  Murakoshi, I., Kaneko, M., Koide, C. and Ikegami, F. Enzymatic-synthesis of the neuroexcitatory amino-acid quisqualic by cysteine synthase. Phytochemistry 25 (1986) 2759–2763.
5.  Tai, C.H., Burkhard, P., Gani, D., Jenn, T., Johnson, C. and Cook, P.F. Characterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase. Biochemistry 40 (2001) 7446–7452. [DOI] [PMID: 11412097]
6.  Bettati, S., Benci, S., Campanini, B., Raboni, S., Chirico, G., Beretta, S., Schnackerz, K.D., Hazlett, T.L., Gratton, E. and Mozzarelli, A. Role of pyridoxal 5′-phosphate in the structural stabilization of O-acetylserine sulfhydrylase. J. Biol. Chem. 275 (2000) 40244–40251. [DOI] [PMID: 10995767]
[EC 2.5.1.47 created 1972 as EC 4.2.99.8, modified 1976, modified 1990, transferred 2002 to EC 2.5.1.47]
 
 
EC 2.5.1.51     
Accepted name: β-pyrazolylalanine synthase
Reaction: O-acetyl-L-serine + pyrazole = 3-(pyrazol-1-yl)-L-alanine + acetate
For diagram of O3-Acetyl-L-serine metabolism, click here
Glossary: O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid
Other name(s): β-(1-pyrazolyl)alanine synthase; β-pyrazolealanine synthase; β-pyrazolylalanine synthase (acetylserine); O3-acetyl-L-serine acetate-lyase (adding pyrazole); BPA-synthase; pyrazolealanine synthase; pyrazolylalaninase; 3-O-acetyl-L-serine:pyrazole 1-(2-amino-2-carboxyethyl)transferase; O3-acetyl-L-serine:pyrazole 1-(2-amino-2-carboxyethyl)transferase
Systematic name: O-acetyl-L-serine:pyrazole 1-(2-amino-2-carboxyethyl)transferase
Comments: The enzyme is highly specific for acetylserine and pyrazole. Not identical with EC 2.5.1.52 L-mimosine synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37290-81-6
References:
1.  Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y. Purification and characterization of β-(pyrazol-1-yl)-L-alanine synthase from Citrullus vulgaris. Phytochemistry 23 (1984) 973–977.
2.  Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y. Purification and characterization of L-mimosine synthase from Leucaena leucocephala. Phytochemistry 23 (1984) 1905–1908.
3.  Murakoshi, I., Kuramoto, H. and Haginiwa, J. The enzymic synthesis of β-substituted alanines. Phytochemistry 11 (1972) 177–182.
4.  Noji, M., Murakoshi, I. and Saito, K. Evidence for identity of β-pyrazolealanine synthase with cysteine synthase in watermelon: formation of β-pyrazole-alanine by cloned cysteine synthase in vitro and in vivo. Biochem. Biophys. Res. Commun. 197 (1993) 1111–1117. [DOI] [PMID: 8280125]
[EC 2.5.1.51 created 1989 as EC 4.2.99.14 (EC 4.2.99.17 incorporated 1992), transferred 2002 to EC 2.5.1.51]
 
 
EC 2.5.1.52     
Accepted name: L-mimosine synthase
Reaction: O-acetyl-L-serine + 3,4-dihydroxypyridine = 3-(3,4-dihydroxypyridin-1-yl)-L-alanine + acetate
For diagram of O3-Acetyl-L-serine metabolism, click here
Glossary: O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid
L-mimosine = (2S)-2-amino-3-(3-hydroxy-4-oxopyridin-1(4H)-yl)propanoic acid
Other name(s): O3-acetyl-L-serine acetate-lyase (adding 3,4-dihydroxypyridin-1-yl); 3-O-acetyl-L-serine:3,4-dihydroxypyridine 1-(2-amino-2-carboxyethyl)transferase; O3-acetyl-L-serine:3,4-dihydroxypyridine 1-(2-amino-2-carboxyethyl)transferase
Systematic name: O-acetyl-L-serine:3,4-dihydroxypyridine 1-(2-amino-2-carboxyethyl)transferase
Comments: Brings about the biosynthesis of L-mimosine in plants of the Mimosa and Leucaena genera. Not identical with EC 2.5.1.51, β-pyrazolylalanine synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 93229-75-5
References:
1.  Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y. Purification and characterization of β-(pyrazol-1-yl)-L-alanine synthase from Citrullus vulgaris. Phytochemistry 23 (1984) 973–977.
2.  Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y. Purification and characterization of L-mimosine synthase from Leucaena leucocephala. Phytochemistry 23 (1984) 1905–1908.
3.  Murakoshi, I., Kuramoto, H. and Haginiwa, J. The enzymic synthesis of β-substituted alanines. Phytochemistry 11 (1972) 177–182.
4.  Noji, M., Murakoshi, I. and Saito, K. Evidence for identity of β-pyrazolealanine synthase with cysteine synthase in watermelon: formation of β-pyrazole-alanine by cloned cysteine synthase in vitro and in vivo. Biochem. Biophys. Res. Commun. 197 (1993) 1111–1117. [DOI] [PMID: 8280125]
[EC 2.5.1.52 created 1989 as EC 4.2.99.15, transferred 2002 to EC 2.5.1.52]
 
 
EC 4.3.3.8     
Accepted name: mimosinase
Reaction: L-mimosine + H2O = 3-hydroxy-4H-pyrid-4-one + pyruvate + NH3 (overall reaction)
(1a) L-mimosine = 3-hydroxy-4H-pyrid-4-one + 2-aminoprop-2-enoate
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
Glossary: L-mimosine = (2S)-2-amino-3-[3-hydroxy-4-oxopyridin-1(4H)-yl]propanoate
Other name(s): mimosine amidohydrolase (incorrect)
Systematic name: (2S)-2-amino-3-[3-hydroxy-4-oxopyridin-1(4H)-yl]propanoate 3-hydroxy-4H-pyrid-4-one-lyase (2-aminoprop-2-enoate-forming)
Comments: A pyridoxal 5′-phosphate protein. The enzyme degrades the toxic amino acid L-mimosine. It cleaves a carbon-nitrogen bond, releasing 3-hydroxy-4H-pyrid-4-one and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. It is thought to have evolved from EC 4.4.1.13, cysteine-S-conjugate β-lyase. It has been described in both mimosine-producing plants and some bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 104118-49-2
References:
1.  Tangendjaja, B., Lowry, J.B. and Wills, R.H. Isolation of a mimosine degrading enzyme from Leucaena leaf. J. Sci. Food Agric. 37 (1986) 523–526. [DOI]
2.  Negi, V.S., Bingham, J.P., Li, Q.X. and Borthakur, D. A carbon-nitrogen lyase from Leucaena leucocephala catalyzes the first step of mimosine degradation. Plant Physiol. 164 (2014) 922–934. [DOI] [PMID: 24351687]
3.  Oogai, S., Fukuta, M., Watanabe, K., Inafuku, M. and Oku, H. Molecular characterization of mimosinase and cystathionine β-lyase in the Mimosoideae subfamily member Mimosa pudica. J. Plant Res. 132 (2019) 667–680. [DOI] [PMID: 31368041]
4.  Oogai, S., Fukuta, M., Inafuku, M. and Oku, H. Isolation and characterization of mimosine degrading enzyme from Arthrobacter sp. Ryudai-S1. World J. Microbiol. Biotechnol. 38:172 (2022). [DOI] [PMID: 35908235]
[EC 4.3.3.8 created 1989 as EC 3.5.1.61, transferred 2022 to EC 4.3.3.8]
 
 


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