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

Hydantoin racemase
Identifiers
EC no.5.1.99.5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
D-5-monosubstituted hydantoin L-5-monosubstituted hydantoin

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

References

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  1. ^ Watabe K, Ishikawa T, Mukohara Y, Nakamura H (December 1992). "Purification and characterization of the hydantoin racemase of Pseudomonas sp. strain NS671 expressed in Escherichia coli". Journal of Bacteriology. 174 (24): 7989–95. PMC 207535. PMID 1459947.
  2. ^ Wiese A, Pietzsch M, Syldatk C, Mattes R, Altenbuchner J (July 2000). "Hydantoin racemase from Arthrobacter aurescens DSM 3747: heterologous expression, purification and characterization". Journal of Biotechnology. 80 (3): 217–30. doi:10.1016/s0168-1656(00)00262-5. PMID 10949312.
  3. ^ Martínez-Rodríguez S, Las Heras-Vázquez FJ, Mingorance-Cazorla L, Clemente-Jiménez JM, Rodríguez-Vico F (January 2004). "Molecular cloning, purification, and biochemical characterization of hydantoin racemase from the legume symbiont Sinorhizobium meliloti CECT 4114". Applied and Environmental Microbiology. 70 (1): 625–30. doi:10.1128/aem.70.1.625-630.2004. PMC 321266. PMID 14711700.
  4. ^ Martínez-Rodríguez S, Las Heras-Vázquez FJ, Clemente-Jiménez JM, Rodríguez-Vico F (February 2004). "Biochemical characterization of a novel hydantoin racemase from Agrobacterium tumefaciens C58" (PDF). Biochimie. 86 (2): 77–81. doi:10.1016/j.biochi.2004.01.004. PMID 15016445.
  5. ^ Suzuki S, Onishi N, Yokozeki K (March 2005). "Purification and characterization of hydantoin racemase from Microbacterium liquefaciens AJ 3912". Bioscience, Biotechnology, and Biochemistry. 69 (3): 530–6. doi:10.1271/bbb.69.530. PMID 15784981.
  6. ^ Martínez-Rodríguez S, Andújar-Sánchez M, Neira JL, Clemente-Jiménez JM, Jara-Pérez V, Rodríguez-Vico F, Las Heras-Vázquez FJ (December 2006). "Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from Sinorhizobium meliloti". Protein Science. 15 (12): 2729–38. doi:10.1110/ps.062452106. PMC 2242435. PMID 17132860.
  7. ^ Altenbuchner J, Siemann-Herzberg M, Syldatk C (December 2001). "Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids". Current Opinion in Biotechnology. 12 (6): 559–63. doi:10.1016/s0958-1669(01)00263-4. PMID 11849938.
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