PMID:2687245
| Citation |
Richarme, G (1989) Purification of a new dihydrolipoamide dehydrogenase from Escherichia coli. J. Bacteriol. 171:6580-5 |
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| Abstract |
I purified a new dihydrolipoamide dehydrogenase from a lpd mutant of Escherichia coli deficient in the lipoamide dehydrogenase (EC 1.6.4.3) common to the pyruvate dehydrogenase (EC 1.2.4.1) and 2-oxoglutarate dehydrogenase complexes. The occurrence of the new lipoamide dehydrogenase in lpd mutants, including a lpd deletion mutant and the immunological properties of the enzyme, showed that it is different from the lpd gene product. The new dihydrolipoamide dehydrogenase had a molecular weight of 46,000, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It was expressed in low amounts. It catalyzed the NAD+-dependent reduction of dihydrolipoamide with a maximal activity of 20 mumol/min per mg of protein and exhibited a hyperbolic dependence of catalytic activity on the concentration of both dihydrolipoamide and NAD+. The possible implication of the new dihydrolipoamide in the function of 2-oxo acid dehydrogenase complexes is discussed, as is its relation to binding protein-dependent transport. |
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| Keywords |
Centrifugation, Zonal; Chromatography, Affinity; Chromatography, DEAE-Cellulose; Chromatography, Gel; Dihydrolipoamide Dehydrogenase/genetics; Dihydrolipoamide Dehydrogenase/isolation & purification; Dihydrolipoamide Dehydrogenase/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Escherichia coli/genetics; Immunoblotting; Kinetics; Molecular Weight; Mutation |
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