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] |
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[EC 3.5.1.77 created 1999, modified 2008] |
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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, PDB |
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] |
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[EC 3.5.1.87 created 2001, modified 2008] |
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EC |
3.5.2.2 |
Accepted name: |
dihydropyrimidinase |
Reaction: |
5,6-dihydrouracil + H2O = 3-ureidopropanoate |
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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] |
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[EC 3.5.2.2 created 1961] |
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EC |
3.5.2.3 |
Accepted name: |
dihydroorotase |
Reaction: |
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate |
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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] |
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[EC 3.5.2.3 created 1961] |
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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] |
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[EC 3.5.2.4 created 1961] |
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EC |
3.5.2.14 |
Accepted name: |
N-methylhydantoinase (ATP-hydrolysing) |
Reaction: |
ATP + N-methylhydantoin + 2 H2O = ADP + phosphate + N-carbamoylsarcosine |
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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] |
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[EC 3.5.2.14 created 1989] |
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EC |
3.5.4.21 |
Accepted name: |
creatinine deaminase |
Reaction: |
creatinine + H2O = N-methylhydantoin + NH3 |
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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] |
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[EC 3.5.4.21 created 1972] |
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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] |
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[EC 5.1.99.5 created 2008] |
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