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 | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- D-5-monosubstituted hydantoin L-5-monosubstituted hydantoin
This enzyme is a part of the reaction cascade known as the "hydantoinase process".
References
edit- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
External links
edit- Hydantoin+racemase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
