Hydantoin racemase

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Hydantoin racemase
Identifiers
EC number 5.1.99.5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Hydantoin racemase (EC 5.1.99.5, 5'-monosubstituted-hydantoin racemase, HyuA, HyuE) is an enzyme with systematic name D-5-monosubstituted-hydantoin racemase.[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction

D-5-monosubstituted hydantoin L-5-monosubstituted hydantoin

This enzyme is a part of the reaction cascade known as the "hydantoinase process".

References[edit]

  1. ^ Watabe, K.; Ishikawa, T.; Mukohara, Y.; Nakamura, H. (1992). "Purification and characterization of the hydantoin racemase of Pseudomonas sp. strain NS671 expressed in Escherichia coli". J. Bacteriol. 174: 7989–7995. PMC 207535Freely accessible. PMID 1459947. 
  2. ^ Wiese, A.; Pietzsch, M.; Syldatk, C.; Mattes, R.; Altenbuchner, J. (2000). "Hydantoin racemase from Arthrobacter aurescens DSM 3747: heterologous expression, purification and characterization". J. Biotechnol. 80: 217–230. PMID 10949312. doi:10.1016/s0168-1656(00)00262-5. 
  3. ^ Martínez-Rodríguez, S.; Las Heras-Vázquez, F.J.; Mingorance-Cazorla, L.; Clemente-Jiménez, J.M.; Rodríguez-Vico, F. (2004). "Molecular cloning, purification, and biochemical characterization of hydantoin racemase from the legume symbiont Sinorhizobium meliloti CECT 4114". Appl. Environ. Microbiol. 70: 625–630. PMC 321266Freely accessible. PMID 14711700. doi:10.1128/aem.70.1.625-630.2004. 
  4. ^ Martínez-Rodríguez, S.; Las Heras-Vázquez, F.J.; Clemente-Jiménez, J.M.; Rodríguez-Vico, F. (2004). "Biochemical characterization of a novel hydantoin racemase from Agrobacterium tumefaciens C58". Biochimie. 86: 77–81. PMID 15016445. doi:10.1016/j.biochi.2004.01.004. 
  5. ^ Suzuki, S.; Onishi, N.; Yokozeki, K. (2005). "Purification and characterization of hydantoin racemase from Microbacterium liquefaciens AJ 3912". Biosci. Biotechnol. Biochem. 69: 530–536. PMID 15784981. doi:10.1271/bbb.69.530. 
  6. ^ Martínez-Rodríguez, S.; Andújar-Sánchez, M.; Neira, J.L.; Clemente-Jiménez, J.M.; Jara-Pérez, V.; Rodríguez-Vico, F.; Las Heras-Vázquez, F.J. (2006). "Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from Sinorhizobium meliloti". Protein Sci. 15: 2729–2738. PMC 2242435Freely accessible. PMID 17132860. doi:10.1110/ps.062452106. 
  7. ^ Altenbuchner, J.; Siemann-Herzberg, M.; Syldatk, C. (2001). "Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids". Curr. Opin. Biotechnol. 12: 559–563. PMID 11849938. doi:10.1016/s0958-1669(01)00263-4. 

External links[edit]