The effect of substrates on the inter‐domain interactions of the hinge‐bending enzyme 3‐phosphoglycerate kinase

FEBS Letters

Pain, Roger H.¹  Adams, Benjamin¹ 

[1] Department of Biochemistry, University of Newcastle upon Tyne, Newcastle upon Tyne NE1 7RU, England

关键词: Phosphoglycerate kinase Enzyme mechanism yConformational stability Hinge-bending Denaturation;   

DOI  :  10.1016/0014-5793(86)80280-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A hinge-bending mechanism has been proposed for phosphoglycerate kinase, in which the two domains bend about the connecting “swaist& rsquo; region. In partially denaturing concentrations of guanidinium chloride the substrate 3-phosphoglycerate stabilises one domain against denaturation and destabilises the other. The reduction of mutual stabilisation of the two domains on binding substrate indicates a freeing of the hinge to allow the protein to take up other states rather than a directive mechanism. The stabilisation of both domains at higher concentrations of ATP at which the enzyme is inhibited supports this mechanism.

【 授权许可】

Unknown