3-Hidroksidekanoil-(acil-nosilac-protein) dehidrataza
(Preusmjereno sa stranice D-3-hydroxydecanoyl-(acyl-carrier protein) dehydratase)
| 3-Hidroksidekanoil-(acil-nosilac-protein) dehidrataza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 4.2.1.60 | ||||||||
| CAS broj | 9030-79-9 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
3-Hidroksidekanoil-(acil-nosilac-protein) dehidrataza (EC 4.2.1.60, D-3-hidroksidekanoil-(acil-nosilac protein) dehidrataza, 3-hidroksidekanoil-acil nosilac protein dehidraza, 3-hidroksidekanoil-acil nosilac protein dehidrataza, beta-hidroksidekanoil tioestar dehidraza, beta-hidroksidekanoatna dehidraza, beta-hidroksidekanoil tiol estarska dehidraza, FabA, beta-hidroksiacil-acil nosilac protein dehidrataza, HDDaza, beta-hidroksiacil-ACP dehidraza, (3R)-3-hidroksidekanoil-(acil-nosilac-protein) hidrolijaza) je enzim sa sistematskim imenom (3R)-3-hidroksidekanoil-(acil-nosilac protein) hidrolijaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) (3R)-3-hidroksidekanoil-[acil-nosilac protein] trans-dec-2-enoil-[acil-nosilac protein] + H2O
- (2) (3R)-3-hidroksidekanoil-[acil-nosilac protein] cis-dec-3-enoil-[acil-nosilac protein] + H2O
Ovaj enzim je specifičan za C10 lance.
- ↑ Kass, L.R., Brock, D.J.H. and Bloch, K. (1967). „β-Hydroxydecanoyl thioester dehydrase. I. Purification and properties”. J. Biol. Chem. 242: 4418-4431. PMID 4863739.
- ↑ Brock, D.J.H., Kass, L.R. and Bloch, K. (1967). „β-Hydroxydecanoyl thioester dehydrase. II. Mode of action”. J. Biol. Chem. 242: 4432-4440. PMID 4863740.
- ↑ Sharma, A., Henderson, B.S., Schwab, J.M. and Smith, J.L. (1990). „Crystallization and preliminary X-ray analysis of β-hydroxydecanoyl thiol ester dehydrase from Escherichia coli”. J. Biol. Chem. 265: 5110-5112. PMID 2180957.
- ↑ Magnuson, K., Jackowski, S., Rock, C.O. and Cronan, J.E., Jr. (1993). „Regulation of fatty acid biosynthesis in Escherichia coli”. Microbiol. Rev. 57: 522-542. PMID 8246839.
- ↑ Bloch, K. (1969). „Enzymatic synthesis of monounsaturated fatty acids”. Acc. Chem. Res. 2: 193-202.
- ↑ Wang, H. and Cronan, J.E. (2004). „Functional replacement of the FabA and FabB proteins of Escherichia coli fatty acid synthesis by Enterococcus faecalis FabZ and FabF homologues”. J. Biol. Chem. 279: 34489-34495. PMID 15194690.
- ↑ Cronan, J.E., Jr. and Rock, C.O. (1996). „Biosynthesis of membrane lipids”. u: Neidhardt, F.C.. Escherichia coli and Salmonella: Cellular and Molecular Biology. 1 (2nd izd.). Washington, DC: ASM Press. str. 612-636.
- 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.
- Cronan, J.E., Jr. and Rock, C.O. (1996). „Biosynthesis of membrane lipids”. u: Neidhardt, F.C.. Escherichia coli and Salmonella: Cellular and Molecular Biology. 1 (2nd izd.). Washington, DC: ASM Press. str. 612-636.