3-Oksoacil-(acil-nosilac-protein) sintaza
3-Oksoacil-(acil-nosilac-protein) sintaza (EC 2.3.1.41, beta-ketoacil-ACP sintaza I, beta-ketoacilna sintetaza, beta-ketoacil-ACP sintetaza, beta-ketoacil-acil nosilac protein sintetaza, beta-ketoacil-(acil nosilac protein) sintaza, beta-ketoacilsintaza, 3-ketoacil-acil nosilac protein sintaza, beta-ketoacil acil nosilac protein sintaza, 3-oksoacil:ACP sintaza I, KASI, KAS I, FabF1, FabB, acil-(acil-nosilac-protein):malonil-(acil-nosilac-protein) C-aciltransferaza (dekarboksilacija)) je enzim sa sistematskim imenom acil-(acil-nosilac protein):malonil-(acil-nosilac protein) C-aciltransferaza (dekarboksilacija).[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
| 3-Oksoacil-(acil-nosilac-protein) sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.3.1.41 | ||||||||
| CAS broj | 2621625 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- acil-[acil-nosilac protein] + malonil-[acil-nosilac protein] 3-oksoacil-[acil-nosilac protein] + CO2 + [acil-nosilac protein]
Ovaj enzim je odgovoran za produžavanje lanca pri biosintezi disociranih (tip II) masnih kiselina, i.e. adicija dva C atoma na masno kiselinski lanac. Escherichia coli mutanti kojima nedostaje ovaj enzim su deficitarni u nezasićenim masnim kiselinama.
Reference
uredi- ↑ Alberts, A.W., Majerus, P.W. and Vagelos, P.R. (1969). „Acetyl-CoA acyl carrier protein transacylase”. Methods Enzymol. 14: 50-53.
- ↑ Prescott, D.J. and Vagelos, P.R. (1972). „Acyl carrier protein”. Adv. Enzymol. Relat. Areas Mol. Biol. 36: 269-311. PMID 4561013.
- ↑ Toomey, R.E. and Wakil, S.J. (1966). „Studies on the mechanism of fatty acid synthesis. XVI. Preparation and general properties of acyl-malonyl acyl carrier protein-condensing enzyme from Escherichia coli”. J. Biol. Chem. 241: 1159-1165. PMID 5327099.
- ↑ D'Agnolo, G., Rosenfeld, I.S. and Vagelos, P.R. (1975). „Multiple forms of β-ketoacyl-acyl carrier protein synthetase in Escherichia coli”. J. Biol. Chem. 250: 5289-5294. PMID 237914.
- ↑ Garwin, J.L., Klages, A.L. and Cronan, J.E., Jr.. (1980). „Structural, enzymatic, and genetic studies of β-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli”. J. Biol. Chem. 255: 11949-11956. PMID 7002930.
- ↑ 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.
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.
- 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.