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Issue 5, 2009
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Preliminary kinetic analysis of acyl carrier proteinketoacylsynthase interactions in the actinorhodin minimal polyketide synthase

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Abstract

Interactions between the acyl carrier protein (ACP) and ketoacylsynthase (KS) components of the actinorhodinpolyketide synthase have been investigated using kinetic assays. These indicate that for three different quantifiable interactions (acceleration of self-malonylation, initiation and extension) mutations of E47 and E53 residues located on ACP helix II have different effects. Initiation clearly involves interaction between KSβ and ACP helix II, but self-malonylation acceleration and extension by KSα appear not to be affected strongly by the same mutations.

Graphical abstract: Preliminary kinetic analysis of acyl carrier protein–ketoacylsynthase interactions in the actinorhodin minimal polyketide synthase

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Publication details

The article was received on 05 Dec 2008, accepted on 29 Jan 2009 and first published on 20 Mar 2009


Article type: Paper
DOI: 10.1039/B821844G
Citation: Mol. BioSyst., 2009,5, 511-518
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    Preliminary kinetic analysis of acyl carrier proteinketoacylsynthase interactions in the actinorhodin minimal polyketide synthase

    P. Beltran-Alvarez, C. J. Arthur, R. J. Cox, J. Crosby, M. P. Crump and T. J. Simpson, Mol. BioSyst., 2009, 5, 511
    DOI: 10.1039/B821844G

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