Antibodies against an inter‐domain segment of polypeptide chain inhibit active‐site coupling in the pyruvate dehydrogenase multienzyme complex

FEBS Letters

Appella, Ettore¹  Ullrich, Stephen J.¹  Perham, Richard N.²  Radford, Sheena E.² 

[1] Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA;Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, England

关键词: Pyruvate dehydrogenase;    Multienzyme complex;    Synthetic peptide;    Antibody;    Domain;    Active-site coupling;   

DOI  :  10.1016/0014-5793(89)80750-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A synthetic peptide, AAPAAAPAKQEAAAPAPAAKAEAPAAAPAAKA, proved to be an efficient and specific immunogen in rabbits. The amino acid sequence of the peptide is identical to that of the inter-domain region (PEP3) linking the innermost of the three lipoyl domains to the dihydrolipoamide dehydrogenase-binding domain in the dihydrolipoamide acetyltransferase chain of the pyruvate dehydrogenase complex of Escherichia coli. Fab fragments from anti-PEP3 antibodies selectively inhibited active-site coupling in the complex without affecting the individual activities of the three component enzymes, highlighting the role of the inter-domain regions as flexible linkers in catalysis.

【 授权许可】

Unknown