Active site modification of the β-ketoacyl-ACP synthase FabF3 of Streptomyces coelicolor affects the fatty acid chain length of the CDA lipopeptides.
Using site directed mutagenesis we altered an active site residue (Phe107) of the enzyme encoded by fabF3 (SCO3248) in the Streptomyces coelicolor gene cluster required for biosynthesis of the calcium dependent antibiotics (CDAs), successfully generating two novel CDA derivatives comprising truncated (C4) lipid side chains and confirming that fabF3 encodes a KAS-II homologue that is involved in determining CDA fatty acid chain length.
FHMS, University of Surrey, Guildford, Surrey, GU2 7XH, UK.
Richard A
RA
Lewis
Laura
L
Nunns
Jenny
J
Thirlway
Kathleen
K
Carroll
Colin P
CP
Smith
Jason
J
Micklefield
D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D005227:Fatty Acids / Q000096:biosynthesis* / Q000737:chemistry; D007930:Leucine / Q000737:chemistry / Q000378:metabolism; D055666:Lipopeptides / Q000096:biosynthesis* / Q000737:chemistry / Q000378:metabolism; D016296:Mutagenesis; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D010649:Phenylalanine / Q000737:chemistry / Q000378:metabolism; D048372:Streptomyces coelicolor / Q000201:enzymology* / Q000235:genetics
C040487:CDA antibiotic; D005227:Fatty Acids; D055666:Lipopeptides; D010455:Peptides; D010649:Phenylalanine; D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase; D007930:Leucine