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Interaction between d ‐glyceraldehyde‐3‐phosphate dehydrogenase and 3‐phosphoglycerate kinase and its functional consequences
Author(s) -
Khoroshilova Natalia A.,
Muronetz Vladimir I.,
Nagradova Natalia K.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80548-u
Subject(s) - phosphoglycerate kinase , glyceraldehyde 3 phosphate dehydrogenase , dehydrogenase , biochemistry , tetramer , glyceraldehyde , chemistry , kinase , escherichia coli , microbiology and biotechnology , lactate dehydrogenase , enzyme , biology , gene
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.