The Enzyme Database

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EC 3.5.1.77     
Accepted name: N-carbamoyl-D-amino-acid hydrolase
Reaction: an N-carbamoyl-D-amino acid + H2O = a D-amino acid + NH3 + CO2
Other name(s): D-N-carbamoylase; N-carbamoylase (ambiguous); N-carbamoyl-D-amino acid hydrolase
Systematic name: N-carbamoyl-D-amino-acid amidohydrolase
Comments: This enzyme, along with EC 3.5.1.87 (N-carbamoyl-L-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [2]. It has strict stereospecificity for N-carbamoyl-D-amino acids and does not act upon the corresponding L-amino acids or on the N-formyl amino acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and -ureidopropanoate, which are substrates for other amidohydrolases.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 71768-08-6
References:
1.  Ogawa, J., Shimizu, S., Yamada, H. N-Carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c; purification and characterization. Eur. J. Biochem. 212 (1993) 685–691. [DOI] [PMID: 8462543]
2.  Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559–563. [DOI] [PMID: 11849938]
[EC 3.5.1.77 created 1999, modified 2008]
 
 
EC 3.5.1.87     
Accepted name: N-carbamoyl-L-amino-acid hydrolase
Reaction: an N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O = an L-2-amino acid + NH3 + CO2
Other name(s): N-carbamyl L-amino acid amidohydrolase; N-carbamoyl-L-amino acid amidohydrolase; L-N-carbamoylase; N-carbamoylase (ambiguous)
Systematic name: N-carbamoyl-L-amino-acid amidohydrolase
Comments: This enzyme, along with EC 3.5.1.77 (N-carbamoyl-D-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [3]. The enzyme from Alcaligenes xylosoxidans has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan. The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyse N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents [2]. The enzyme is inactive on derivatives of D-amino acids. In addition to N-carbamoyl L-amino acids, the enzyme can also hydrolyse formyl and acetyl derivatives to varying degrees [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ogawa, J., Miyake, H. and Shimizu, S. Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans. Appl. Microbiol. Biotechnol. 43 (1995) 1039–1043. [PMID: 8590654]
2.  Martínez-Rodríguez, S., Clemente-Jiménez, J.M., Rodríguez-Vico, F. and Las Heras-Vázquez, F.J. Molecular cloning and biochemical characterization of L-N-carbamoylase from Sinorhizobium meliloti CECT4114. J. Mol. Microbiol. Biotechnol. 9 (2005) 16–25. [DOI] [PMID: 16254442]
3.  Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559–563. [DOI] [PMID: 11849938]
[EC 3.5.1.87 created 2001, modified 2008]
 
 
EC 3.5.2.2     
Accepted name: dihydropyrimidinase
Reaction: 5,6-dihydrouracil + H2O = 3-ureidopropanoate
For diagram of pyrimidine catabolism, 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. [DOI] [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]
[EC 3.5.2.2 created 1961]
 
 
EC 3.5.2.3     
Accepted name: dihydroorotase
Reaction: (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate
For diagram of pyrimidine biosynthesis, 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.
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. [PMID: 13163076]
[EC 3.5.2.3 created 1961]
 
 
EC 3.5.2.4     
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. [PMID: 13163076]
[EC 3.5.2.4 created 1961]
 
 
EC 3.5.2.14     
Accepted name: N-methylhydantoinase (ATP-hydrolysing)
Reaction: ATP + N-methylhydantoin + 2 H2O = ADP + phosphate + N-carbamoylsarcosine
For diagram of creatine biosynthesis, 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. [DOI] [PMID: 3827889]
[EC 3.5.2.14 created 1989]
 
 
EC 3.5.4.21     
Accepted name: creatinine deaminase
Reaction: creatinine + H2O = N-methylhydantoin + NH3
For diagram of creatine biosynthesis, 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. [DOI] [PMID: 13584408]
[EC 3.5.4.21 created 1972]
 
 
EC 5.1.99.5     
Accepted name: hydantoin racemase
Reaction: D-5-monosubstituted hydantoin = L-5-monosubstituted hydantoin
Glossary: hydantoin = imidazolidine-2,4-dione
Other name(s): 5′-monosubstituted-hydantoin racemase; HyuA; HyuE
Systematic name: D-5-monosubstituted-hydantoin racemase
Comments: This enzyme, along with N-carbamoylase (EC 3.5.1.77 and EC 3.5.1.87) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [7]. The enzyme from Pseudomonas sp. (HyuE) has a preference for hydantoins with aliphatic substituents, e.g. D- and L-5-[2-(methylsulfanyl)ethyl]hydantoin, whereas that from Arthrobacter aurescens shows highest activity with arylalkyl substituents, especially 5-benzylhydantoin, at the 5-position [2]. In the enzyme from Sinorhizobium meliloti, Cys76 is responsible for recognition and proton retrieval of D-isomers, while Cys181 is responsible for L-isomer recognition and racemization [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Watabe, K., Ishikawa, T., Mukohara, Y. and Nakamura, H. Purification and characterization of the hydantoin racemase of Pseudomonas sp. strain NS671 expressed in Escherichia coli. J. Bacteriol. 174 (1992) 7989–7995. [DOI] [PMID: 1459947]
2.  Wiese, A., Pietzsch, M., Syldatk, C., Mattes, R. and Altenbuchner, J. Hydantoin racemase from Arthrobacter aurescens DSM 3747: heterologous expression, purification and characterization. J. Biotechnol. 80 (2000) 217–230. [DOI] [PMID: 10949312]
3.  Martínez-Rodríguez, S., Las Heras-Vázquez, F.J., Mingorance-Cazorla, L., Clemente-Jiménez, J.M. and Rodríguez-Vico, F. Molecular cloning, purification, and biochemical characterization of hydantoin racemase from the legume symbiont Sinorhizobium meliloti CECT 4114. Appl. Environ. Microbiol. 70 (2004) 625–630. [DOI] [PMID: 14711700]
4.  Martínez-Rodríguez, S., Las Heras-Vázquez, F.J., Clemente-Jiménez, J.M. and Rodríguez-Vico, F. Biochemical characterization of a novel hydantoin racemase from Agrobacterium tumefaciens C58. Biochimie 86 (2004) 77–81. [DOI] [PMID: 15016445]
5.  Suzuki, S., Onishi, N. and Yokozeki, K. Purification and characterization of hydantoin racemase from Microbacterium liquefaciens AJ 3912. Biosci. Biotechnol. Biochem. 69 (2005) 530–536. [DOI] [PMID: 15784981]
6.  Martínez-Rodríguez, S., Andújar-Sánchez, M., Neira, J.L., Clemente-Jiménez, J.M., Jara-Pérez, V., Rodríguez-Vico, F. and Las Heras-Vázquez, F.J. Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from Sinorhizobium meliloti. Protein Sci. 15 (2006) 2729–2738. [DOI] [PMID: 17132860]
7.  Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559–563. [DOI] [PMID: 11849938]
[EC 5.1.99.5 created 2008]
 
 


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