title: Amino acid sequence around the active serine in the acyl transferase domain of rabbit mammary fatty acid synthase.
abstract: 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.
mesh_terms: 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
chemical_list: D010446:Peptide Fragments; D000217:Acyltransferases; D064429:Fatty Acid Synthases; D010196:Pancreatic Elastase