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3. Improving fatty acid production in Escherichia coli through the overexpression of malonyl coA-acyl carrier protein transacylase. Zhang X, Agrawal A, San KY. Biotechnol Prog; 2012; 28(1):60-5. PubMed ID: 22038854 [Abstract] [Full Text] [Related]
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6. The crystal structure of MCAT from Mycobacterium tuberculosis reveals three new catalytic models. Li Z, Huang Y, Ge J, Fan H, Zhou X, Li S, Bartlam M, Wang H, Rao Z. J Mol Biol; 2007 Aug 24; 371(4):1075-83. PubMed ID: 17604051 [Abstract] [Full Text] [Related]
7. Crystallization of the malonyl coenzyme A-acyl carrier protein transacylase from Escherichia coli. Serre L, Swenson L, Green R, Wei Y, Verwoert II, Verbree EC, Stuitje AR, Derewenda ZS. J Mol Biol; 1994 Sep 09; 242(1):99-102. PubMed ID: 8078074 [Abstract] [Full Text] [Related]
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13. Kinetic and mechanistic analysis of the malonyl CoA:ACP transacylase from Streptomyces coelicolor indicates a single catalytically competent serine nucleophile at the active site. Szafranska AE, Hitchman TS, Cox RJ, Crosby J, Simpson TJ. Biochemistry; 2002 Feb 05; 41(5):1421-7. PubMed ID: 11814333 [Abstract] [Full Text] [Related]
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20. The malonyl/acetyltransferase and beta-ketoacyl synthase domains of the animal fatty acid synthase can cooperate with the acyl carrier protein domain of either subunit. Joshi AK, Witkowski A, Smith S. Biochemistry; 1998 Feb 24; 37(8):2515-23. PubMed ID: 9485400 [Abstract] [Full Text] [Related] Page: [Next] [New Search]