Amino acid sequence around the active serine in the acyl transferase domain of rabbit mammary fatty acid synthase

FEBS Letters

Grahame Hardie, D.²  McCarthy, Alun D.²  Williams, Dudley H.¹  Santikarn, Sitthivet¹  Aitken, Alastair² 

[1] Chemistry Laboratories, University of Cambridge, Lensfield Road, Cambridge, England;Biochemistry Department, Dundee University, Dundee DD1 4HN, Scotland, England

关键词: Amino acid sequence;    Active serine;    Acyl transferase;    Fatty acid synthase;   

DOI  :  10.1016/0014-5793(83)80986-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown