Amino acid sequence around the active-site serine residue in the acyltransferase domain of goat mammary fatty acid synthetase.
Goat mammary fatty acid synthetase was labelled in the acyltransferase domain by formation of O-ester intermediates by incubation with [1-14C]acetyl-CoA and [2-14C]malonyl-CoA. Tryptic-digest and CNBr-cleavage peptides were isolated and purified by high-performance reverse-phase and ion-exchange liquid chromatography. The sequences of the malonyl- and acetyl-labelled peptides were shown to be identical. The results confirm the hypothesis that both acetyl and malonyl groups are transferred to the mammalian fatty acid synthetase complex by the same transferase. The sequence is compared with those of other fatty acid synthetase transferases.
D000105:Acetyl Coenzyme A / Q000494:pharmacology; D000217:Acyltransferases / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D064429:Fatty Acid Synthases / Q000378:metabolism*; D005260:Female; D006041:Goats; D008316:Malonyl Coenzyme A / Q000494:pharmacology; D008321:Mammary Glands, Animal / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D012694:Serine / Q000032:analysis
D010446:Peptide Fragments; D012694:Serine; D008316:Malonyl Coenzyme A; D000105:Acetyl Coenzyme A; D000217:Acyltransferases; D064429:Fatty Acid Synthases