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

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Abstract
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.