Issue 5, 2009

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

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

Supplementary files

Article information

Article type
Paper
Submitted
05 Dec 2008
Accepted
29 Jan 2009
First published
20 Mar 2009

Mol. BioSyst., 2009,5, 511-518

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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