Amino acid sequence around the active serine in the acyl transferase domain of rabbit mammary fatty acid synthase.
Rabbit mammary fatty acid synthase was labelled in the acyl transferase domain(s) by the formation of the O-ester intermediates after incubation with [14C]acetyl- or malonyl-CoA. Elastase peptides containing the labelled acyl groups were isolated using high performance liquid chromatography and sequenced by fast atom bombardment mass spectrometry. An identical peptide (acyl-Ser-Leu-Gly-Glu-Val-Ala) was obtained after labelling with acetyl- or malonyl-CoA. This confirms the hypothesis that, unlike Escherichia coli or yeast, a single transferase catalyses the transfer of both acetyl- and malonyl-groups in the mammalian complex. The sequence at this site is compared with that around the active serine in other acyl transferases and hydrolases.
D000217:Acyltransferases / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D064429:Fatty Acid Synthases / Q000378:metabolism*; D005260:Female; D007774:Lactation; D008321:Mammary Glands, Animal / Q000201:enzymology*; D010196:Pancreatic Elastase; D010446:Peptide Fragments / Q000032:analysis; D011247:Pregnancy; D011817:Rabbits; D013045:Species Specificity
D010446:Peptide Fragments; D000217:Acyltransferases; D064429:Fatty Acid Synthases; D010196:Pancreatic Elastase