Reversible effects of cross‐linking on the regulatory cooperativity of Acinetobacter citrate synthase

FEBS Letters

Mitchell, Colin G.¹  Weitzman, P.D.J.¹ 

[1] Department of Biochemistry, University of Bath, Bath BA2 7AY, England

关键词: Citrate synthase;    Acinetobacter calcoaceticus;    Cross-linking;    Cooperativity;    Allosteric regulation;    Dithiobis(succinimidyl propionate);   

DOI  :  10.1016/0014-5793(83)80082-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Citrate synthase was purified from Acinetobacter calcoaceticus and treated with the cleavable cross-linking reagent dithiobis(succinimidyl propionate). Cross-linking of the enzyme resulted in the abolition of the sigmoidal responses to inhibition by NADH and re-activation by AMP displayed by the native enzyme. Inhibition and re-activation were still observed but without any cooperativity. Cleavage of the disulphide bonds in the cross-links by treatment with dithiothreitol restored the sigmoidal characteristics of both inhibition and re-activation.

【 授权许可】

Unknown