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

• Published in: FEBS letters Vol. 297; no. 3; pp. 247 - 249
• Main Authors: Khoroshilova, Natalia A., Muronetz, Vladimir I., Nagradova, Natalia K.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 10.02.1992; Elsevier
• Subjects: 3-Phosphoglycerate kinase; Analytical, structural and metabolic biochemistry; Animals; Bienzyme complex; Biological and medical sciences; D-glyceraldehyde-3-phosphate dehydrogenase; Enzymes and enzyme inhibitors; Enzymes, Immobilized; Escherichia coli; Fundamental and applied biological sciences. Psychology; Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism; Kinetics; Oxidoreductases; Phosphoglycerate Kinase - metabolism; Rabbits; Bienzyme complex; d-Glyceraldehyde-3-phosphate dehydrogenase; 3-Phosphoglycerate kinase; Stoichiometry; Multienzyme complex; Enzyme; Escherichia coli; Rabbit; Dissociation constant; Species specificity; Lagomorpha; Phosphoglycerate kinase; Vertebrata; Mammalia; Affinity chromatography; Glyceraldehyde-phosphate dehydrogenase; Bacteria; Kinetics; Immobilized enzyme; Enterobacteriaceae
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(92)80548-U

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.