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Literature summary extracted from

  • Hopkins, N.; Williams, C.H., Jr.
    Characterization of lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S (1995), Biochemistry, 34, 11757-11765.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.4 C44S 0.003% of the activity of wild-type enzyme with NAD+ and dihydrolipoamide. Enzyme is capable to catalyze reactions with NADH as electron donor and ferricyanide, thio-NAD+, 2,6-dichlorophenol indophenol and O2 as electron acceptor. The fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature Escherichia coli
1.8.1.4 C49S 0.012% of the activity of wild-type enzyme with NAD+ and dihydrolipoamide. Enzyme is capable to catalyze reactions with NADH as electron donor and ferricyanide, thio-NAD+, 2,6-dichlorophenol indophenol and O2 as electron acceptor. The fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature 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 2 ferricyanide + NADH activity with wild-type enzyme and mutant enzymes C44S and C49S Escherichia coli 2 ferrocyanide + NAD+ + H+
-
 ?
1.8.1.4 dihydrolipoamide + NAD+ mutant enzymes C44S and C49S show minute activity Escherichia coli lipoamide + NADH
-
 ?
1.8.1.4 O2 + NADH activity with wild-type enzyme and mutant enzymes C44S and C49S Escherichia coli ?
-
 ?
1.8.1.4 oxidized 2,6-dichlorophenolindophenol + NADH activity with wild-type enzyme and mutant enzymes C44S and C49S Escherichia coli ? + NAD+
-
 ?
1.8.1.4 thio-NAD+ + NADH activity with wild-type enzyme and mutant enzymes C44S and C49S Escherichia coli thio-NADH + NAD+
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 FAD the fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature Escherichia coli
1.8.1.4 NAD+
-
 Escherichia coli
1.8.1.4 NADH
-
 Escherichia coli