Hydantoin racemase
| 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 | ||||||||
| |||||||||
Hydantoin racemase (EC 5.1.99.5, 5'-monosubstituted-hydantoin racemase, HyuA, HyuE) is an enzyme with system 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
- ^ Watabe, K., Ishikawa, T., Mukohara, Y. and Nakamura, H. (1992). "Purification and characterization of the hydantoin racemase of Pseudomonas sp. strain NS671 expressed in Escherichia coli". J. Bacteriol. 174: 7989–7995. PMID 1459947.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Wiese, A., Pietzsch, M., Syldatk, C., Mattes, R. and Altenbuchner, J. (2000). "Hydantoin racemase from Arthrobacter aurescens DSM 3747: heterologous expression, purification and characterization". J. Biotechnol. 80: 217–230. doi:10.1016/s0168-1656(00)00262-5. PMID 10949312.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Martínez-Rodríguez, S., Las Heras-Vázquez, F.J., Mingorance-Cazorla, L., Clemente-Jiménez, J.M. and 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. doi:10.1128/aem.70.1.625-630.2004. PMID 14711700.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Martínez-Rodríguez, S., Las Heras-Vázquez, F.J., Clemente-Jiménez, J.M. and Rodríguez-Vico, F. (2004). "Biochemical characterization of a novel hydantoin racemase from Agrobacterium tumefaciens C58". Biochimie. 86: 77–81. doi:10.1016/j.biochi.2004.01.004. PMID 15016445.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Suzuki, S., Onishi, N. and Yokozeki, K. (2005). "Purification and characterization of hydantoin racemase from Microbacterium liquefaciens AJ 3912". Biosci. Biotechnol. Biochem. 69: 530–536. doi:10.1271/bbb.69.530. PMID 15784981.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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. (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. doi:10.1110/ps.062452106. PMID 17132860.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. (2001). "Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids". Curr. Opin. Biotechnol. 12: 559–563. doi:10.1016/s0958-1669(01)00263-4. PMID 11849938.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- Hydantoin+racemase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)