Preliminary kinetic analysis of acyl carrier protein-ketoacylsynthase interactions in the actinorhodin minimal polyketide synthase.
Interactions between the acyl carrier protein (ACP) and ketoacylsynthase (KS) components of the actinorhodin polyketide 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 KS(beta) and ACP helix II, but self-malonylation acceleration and extension by KS(alpha) appear not to be affected strongly by the same mutations.
Beltran-Alvarez
Pedro
P
University of Bristol, School of Chemistry, Cantocks Close, Bristol, UKBS8 1TS.
Arthur
Christopher J
CJ
Cox
Russell J
RJ
Crosby
John
J
Crump
Matthew P
MP
Simpson
Thomas J
TJ
D000213:Acyl Carrier Protein / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D048630:Polyketide Synthases / Q000737:chemistry / Q000378:metabolism*; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D013379:Substrate Specificity
D000213:Acyl Carrier Protein; D029968:Escherichia coli Proteins; D048630:Polyketide Synthases; C087193:polyketide beta-ketoacylsynthase