(Acil-nosilac-protein) S-maloniltransferaza
(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
- ^ 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. & Vagelos, P.R. (1972). „Acyl carrier protein”. Adv. Enzymol. Relat. Areas Mol. Biol. 36: 269—311. PMID 4561013.
- ^ Williamson, I.P. & 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. & 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. & 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. & 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. & Hilbi, H. (1997). „Enzymic and genetic basis for bacterial growth on malonate”. Mol. Microbiol. 25: 3—10. PMID 11902724.
Literatura
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