Interaction between d‐glyceraldehyde‐3‐phosphate dehydrogenase and 3‐phosphoglycerate kinase and its functional consequences

FEBS Letters

Muronetz, Vladimir I.¹  Nagradova, Natalia K.¹  Khoroshilova, Natalia A.¹ 

[1] A. N. Belozersky Institute of Physico-Chemical Biology, Moscow, State University, Moscow 119899, USSR

关键词: d-Glyceraldehyde-3-phosphate dehydrogenase;    3-Phosphoglycerate kinase;    Bienzyme complex;   

DOI  :  10.1016/0014-5793(92)80548-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

E. Coli d-glyceraldehyde-3-phosphate dehydrogenase covalently bound to Sepharose was shown to form a complex with soluble E. coli 3-phosphoglycerate kinase with a stoichiometry of 1.77±0.61 kinase molecules per tetramer of the dehydrogenase and an apparent K _d of 1.03±0.68μM (10 mM sodium phosphate, 0.15 M NaCl). No interaction was detected between E. coli d-glyceraldehyde-3-phosphate dehydrogenase and rabbit muscle 3-phosphoglycerate kinase. The species-specificity of the bienzyme association made it possible to develop a kinetic approach to demonstrate the functionally significant interaction between E. coli d-glyceraldehyde-3-phosphate dehydrogenase and E. coli 3-phosphoglycerate kinase, which consists of an increase in steady-state rate of the coupled reaction.

【 授权许可】

Unknown