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Literature summary extracted from

  • Maeda-Yorita, K.; Russell, G.C.; Guest, J.R.; Massey, V.; Williams, C.H., Jr.
    Modulation of the Oxidation-Reduction Potential of the Flavin in Lipoamide Dehydrogenase from Escherichia coli by Alteration of a Nearby Charged Residue, K53R (1994), Biochemistry, 33, 6213-6220.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.4 K53R spectral and redox properties of FAD in the mutant enzyme as well as the interaction of the flavin with bound NAD+ are profoundly affected by the mutation, K53R does not catalyze either the dihydrolipoamide-NAD+ or the NADH-lipoamide reactions except at very low concentrations of reducing substrate. The absorbance spectrum in the visible and near-ultraviolet is little changed from that of wild-type enzyme, in contrast to wild-type enzyme the spectrum of K53R is sensitive to pH. Unlike the wild-type enzyme, the binding of beta-NAD+ to K53R alters the spectrum Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+
-
 Escherichia coli lipoamide + NADH
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 NAD+
-
 Escherichia coli