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Amino acid sequence around the active serine in the acyl transferase domain of rabbit mammary fatty acid synthase
Author(s) -
McCarthy Alun D.,
Aitken Alastair,
Grahame Hardie D.,
Santikarn Sitthivet,
Williams Dudley H.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80986-7
Subject(s) - transferase , biochemistry , rabbit (cipher) , fatty acid synthase , serine , acyl carrier protein , peptide sequence , chemistry , atp synthase , fatty acid , enzyme , biology , biosynthesis , gene , statistics , mathematics
Rabbit mammary fatty acid synthase was labelled in the acyl transferase domain(s) by the formation of the O ‐ester intermediates after incubation with [ 14 C]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.