(Acil-nosilac-protein) S-maloniltransferaza
(Preusmjereno sa stranice EC 2.3.1.39)
| (Acil-nosilac-protein) S-maloniltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.3.1.39 | ||||||||
| CAS broj | 37257-17-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
(Acil-nosilac-protein) S-maloniltransferaza (EC 2.3.1.39, (acil nosilac protein)maloniltransferaza, FabD, malonil koenzim A-acil nosilac protein transacilaza, malonilna transacilaza, malonil transferaza, malonil-KoA-acil nosilac protein transacilaza, malonil-KoA:(acil-nosilac-protein) S-maloniltransferaza, malonil-KoA:ACP transacilaza, malonil-KoA:ACP-SH transacilaza, malonil-KoA:AcpM transacilaza, malonil-KoA:acil nosilac protein transacilaza, malonil-KoA:acil-nosilac-protein transacilaza, malonil-KoA/defosfo-KoA aciltransferaza, MAT, MCAT, MdcH) je enzim sa sistematskim imenom malonil-KoA:(acil-nosilac protein) S-maloniltransferaza.[1][2][3][4][5][6][7][8][9][10][11][12] Ovaj enzim katalizuje sledeću hemijsku reakciju
- malonil-KoA + [acil-nosilac protein] KoA + malonil-[acil-nosilac protein]
Ovaj enzim, zajedno sa EC 2.3.1.38, [acil-nosilac-protein] S-acetiltransferazom, je esencijalan za inicijaciju biosinteze masnih kiselina kod bakterija.
Reference[uredi | uredi kod]
- ↑ 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.
- ↑ Williamson, I.P. and Wakil, S.J. (1966). „Studies on the mechanism of fatty acid synthesis. XVII. Preparation and general properties of acetyl coenzyme A and malonyl coenzyme A-acyl carrier protein transacylases”. J. Biol. Chem. 241: 2326-2332. PMID 5330116.
- ↑ Joshi, V.C. and Wakil, S.J. (1971). „Studies on the mechanism of fatty acid synthesis. XXVI. Purification and properties of malonyl-coenzyme A--acyl carrier protein transacylase of Escherichia coli”. Arch. Biochem. Biophys. 143: 493-505. PMID 4934182.
- ↑ Kremer, L., Nampoothiri, K.M., Lesjean, S., Dover, L.G., Graham, S., Betts, J., Brennan, P.J., Minnikin, D.E., Locht, C. and Besra, G.S. (2001). „Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II”. J. Biol. Chem. 276: 27967-27974. PMID 11373295.
- ↑ Keatinge-Clay, A.T., Shelat, A.A., Savage, D.F., Tsai, S.C., Miercke, L.J., O'Connell, J.D., 3rd, Khosla, C. and Stroud, R.M. (2003). „Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase”. Structure 11: 147-154. PMID 12575934.
- ↑ Szafranska, A.E., Hitchman, T.S., Cox, R.J., Crosby, J. and Simpson, T.J. (2002). „Kinetic and mechanistic analysis of the malonyl CoA:ACP transacylase from Streptomyces coelicolor indicates a single catalytically competent serine nucleophile at the active site”. Biochemistry 41: 1421-1427. PMID 11814333.
- ↑ Hoenke, S., Schmid, M. and Dimroth, P. (1997). „Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli”. Eur. J. Biochem. 246: 530-538. PMID 9208947.
- ↑ Koo, J.H. and Kim, Y.S. (1999). „Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus”. Eur. J. Biochem. 266: 683-690. PMID 10561613.
- ↑ Hoenke, S. and Dimroth, P. (1999). „Formation of catalytically active acetyl-S-malonate decarboxylase requires malonyl-coenzyme A:acyl carrier protein transacylase as auxiliary enzyme”. Eur. J. Biochem. 259: 181-187. PMID 9914491.
- ↑ Chohnan, S., Fujio, T., Takaki, T., Yonekura, M., Nishihara, H. and Takamura, Y. (1998). „Malonate decarboxylase of Pseudomonas putida is composed of five subunits”. FEMS Microbiol. Lett. 169: 37-43. PMID 9851033.
- ↑ Dimroth, P. and Hilbi, H. (1997). „Enzymic and genetic basis for bacterial growth on malonate”. Mol. Microbiol. 25: 3-10. PMID 11902724.
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.