Evidence that the multifunctional polypeptides of vertebrate and fungal fatty acid synthases have arisen by independent gene fusion events

FEBS Letters

Grahame Hardie, D.¹  McCarthy, Alun D.¹  Dean Goldring, J.P.¹ 

[1] MRC Protein Phosphorylation Group, Biochemistry Department, Dundee University, Medical Sciences Institute, Dundee, DD1 4HN, Scotland

关键词: Multifunctional protein;    Fatty acid synthase;    Active site labelling;    Enoyl reductase;   

DOI  :  10.1016/0014-5793(83)80776-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The enoyl reductase (NADPH binding site) of rabbit mammary fatty acid synthase has been radioactively labelled using pyridoxal phosphate and sodium [³H]borohydride. Using this method we have been able to add this site to the four sites whose location has already been mapped within the multifunctional polypeptide chain of the protein. The results show that the enoyl reductase lies between the 3-oxoacylsynthase and the acyl carrier. This confirms that the active sites occur in a different order on the single multifunctional polypeptide of vertebrate fatty acid synthase and the two multifunctional polypeptides of fungal fatty acid synthase, and suggests that these two systems have arisen by independent gene fusion events.

【 授权许可】

Unknown