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(acyl-carrier-protein) S-malonyltransférase

L'[acyl-carrier-protein] S-malonyltransférase, ou ACP S-malonyltransférase, est une acyltransférase qui catalyse la réaction : Acétyl-CoA + ACP CoA + malonyl-ACP.

C'est l'une des enzymes du complexe acide gras synthase de la biosynthèse des acides gras.

Notes et références

    • (en) Alberts AW, Majerus PW and Vagelos PR, « Acetyl-CoA acyl carrier protein transacylase », Methods Enzymol., methods in Enzymology, vol. 14,‎ , p. 50-53 (ISBN 978-0-12-181871-5). DOI 10.1016/S0076-6879(69)14009-4
    • (en) Prescott DJ, Vagelos PR, « Acyl carrier protein », Adv. Enzymol. Relat. Areas. Mol. Biol., vol. 36,‎ , p. 269-311. PMID 4561013
    • (en) Williamson IP, Wakil SJ, « 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., vol. 241, no 10,‎ , p. 2326-2332. PMID 5330116
    • (en) Joshi VC, Wakil SJ, « 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., vol. 143, no 2,‎ , p. 493-505. DOI 10.1016/0003-9861(71)90234-7 PMID 4934182
    • (en) Brennan PJ, Minnikin DE, Locht C, Besra GS, « 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., vol. 276, no 30,‎ , p. 27967-27974. DOI 10.1074/jbc.M103687200 PMID 11373295
    • (en) O'Connell JD 3rd Khosla C, Stroud RM, « Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase », Structure., vol. 11, no 2,‎ , p. 147-154. DOI 10.1016/S0969-2126(03)00004-2 PMID 12575934
    • (en) Szafranska AE, Hitchman TS, Cox RJ, Crosby J, Simpson TJ, « 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., vol. 41, no 5,‎ , p. 1421-1427. DOI 10.1021/bi012001p PMID 11814333
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