Hidantoinska racemaza
(Preusmjereno sa stranice D-5-monosubstituted-hydantoin racemase)
Hidantoinska racemaza (EC 5.1.99.5, 5'-monosupstituisana hidantoinska racemaza, HyuA, HyuE) je enzim sa sistematskim imenom D-5-monosubstituted-hidantoin racemaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Hidantoinska racemaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 5.1.99.5 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- D-5-monosupstituisani hidantoin L-5-monosupstituisani hidantoin
Ovaj enzim učestvuje u reakcionoj kaskadi poznatoj kao "hidantoinazni proces".
Reference
uredi- ↑ 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.
- ↑ 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. PMID 10949312.
- ↑ 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. PMID 14711700.
- ↑ 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. PMID 15016445.
- ↑ 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. PMID 15784981.
- ↑ 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. PMID 17132860.
- ↑ 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. PMID 11849938.
Literatura
uredi- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.