Evidence that the medium-chain acyltransferase of lactating-goat mammary-gland fatty acid synthetase is identical with the acetyl/malonyltransferase.
Competitive binding experiments with malonyl-CoA and [1-14C]acetyl-CoA, [1-14C]butyryl-CoA or [1-14C]decanoyl-CoA indicate that all these substrates are transferred to lactating-goat mammary-gland fatty acid synthetase by the same transferase. Isolation and determination of the amino acid sequence of [1-14C]decanoyl-labelled CNBr-cleavage peptide from the decanoyltransferase site showed that this transferase is identical with the acetyl/malonyltransferase.
D000105:Acetyl Coenzyme A / Q000378:metabolism; D000214:Acyl Coenzyme A / Q000378:metabolism; D000217:Acyltransferases / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D064429:Fatty Acid Synthases / Q000378:metabolism*; D005260:Female; D005561:Formates / Q000378:metabolism; D006041:Goats; D007774:Lactation; D008316:Malonyl Coenzyme A / Q000378:metabolism; D008321:Mammary Glands, Animal / Q000201:enzymology*; D011247:Pregnancy
D000214:Acyl Coenzyme A; D005561:Formates; C008817:peroxyformic acid; C045561:decanoyl-coenzyme A; C024343:butyryl-coenzyme A; D008316:Malonyl Coenzyme A; D000105:Acetyl Coenzyme A; D000217:Acyltransferases; D064429:Fatty Acid Synthases