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Issue 6, 2009
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Catalysis and mechanism of malonyl transferase activity in type II fatty acid biosynthesisacyl carrier proteins

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Abstract

One of the unexplored, yet important aspects of the biology of acyl carrier proteins(ACPs) is the self-acylation and malonyl transferase activities dedicated to ACPs in polyketide synthesis. Our studies demonstrate the existence of malonyl transferase activityin ACPs involved in type II fatty acid biosynthesis from Plasmodium falciparum and Escherichia coli. We also show that the catalytic malonyl transferase activityis intrinsic to an individual ACP. Mutational analysis implicates an arginine/lysine in loop II and an arginine/glutamine in helix III as the catalytic residues for transferase function. The hydrogen bonding properties of these residues appears to be indispensable for the transferase reaction. Complementation of fabD(Ts) E. coli highlights the putative physiological role of this process. Our studies thus shed light on a key aspect of ACP biology and provide insights into the mechanism involved therein.

Graphical abstract: Catalysis and mechanism of malonyl transferase activity in type II fatty acid biosynthesisacyl carrier proteins

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Publication details

The article was received on 17 Nov 2008, accepted on 30 Mar 2009 and first published on 27 Apr 2009


Article type: Paper
DOI: 10.1039/B820420A
Citation: Mol. BioSyst., 2009,5, 651-659
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    Catalysis and mechanism of malonyl transferase activity in type II fatty acid biosynthesisacyl carrier proteins

    A. Misra, N. Surolia and A. Surolia, Mol. BioSyst., 2009, 5, 651
    DOI: 10.1039/B820420A

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