Klavaminat sintaza
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Klavaminat sintaza | |||||||||
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Identifikatori | |||||||||
EC broj | 1.14.11.21 | ||||||||
CAS broj | 122799-56-8 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Klavaminat sintaza (EC 1.14.11.21, klavaminatna sintaza 2, sintaza klavaminske kiseline) je enzim sa sistematskim imenom dezoksiamidinoproklavaminat,2-oksoglutarat:kiseonik oksidoreduktaza (3-hidroksilacija).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) dezoksiamidinoproklavaminat + 2-oksoglutarat + O2 amidinoproklavaminat + sukcinat + CO2
- (2) proklavaminat + 2-oksoglutarat + O2 dihidroklavaminat + sukcinat + CO2 +H2O
- (3) dihidroklavaminat + 2-oksoglutarat + O2 klavaminat + sukcinat + CO2 +H2O
Ovaj enzim sadrži gvožđe nevezano za hem. On katalizuje tri zasebne oksidativne reakcije u biositezi beta-laktamaznog inhibitora klavulanata kod Streptomyces clavuligerus.
Reference[uredi | uredi kod]
- ↑ Salowe, S.P., Krol, W.J., Iwatareuyl, D. and Townsend, C.A. (1991). „Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction”. Biochemistry 30: 2281-2292. PMID 1998687.
- ↑ Zhou, J., Gunsior, M., Bachmann, B.O., Townsend, C.A. and Solomon, E.I. (1998). „Substrate binding to the α-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: Coupling mechanism of oxidative decarboxylation and hydroxylation”. J. Am. Chem. Soc. 120: 13539-13540.
- ↑ Zhang, Z.H., Ren, J.S., Stammers, D.K., Baldwin, J.E., Harlos, K. and Schofield, C.J. (2000). „Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase”. Nat. Struct. Biol. 7: 127-133. PMID 10655615.
- ↑ Zhou, J., Kelly, W.L., Bachmann, B.O., Gunsior, M., Townsend, C.A. and Solomon, E.I. (2001). „Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional α-KG-dependent non-heme iron enzyme: Correlation with mechanisms and reactivities”. J. Am. Chem. Soc. 123: 7388-7398. PMID 11472170.
- ↑ Townsend, C.A. (2002). „New reactions in clavulanic acid biosynthesis”. Curr. Opin. Chem. Biol. 6: 583-589. PMID 12413541.
Literatura[uredi | uredi kod]
- 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.