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Literature summary extracted from

  • Kim, H.
    Site-specific modifications of the Cys-45 residue in human dihydrolipoamide dehydrogenase to Ser and Tyr (2007), Bull. Korean Chem. Soc., 28, 907-908.
No PubMed abstract available

Application

EC Number Application Comment Organism
1.8.1.4 degradation conservation of the Cys-45 residue in human E3 is essential to the efficient catalytic function of the enzyme Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.4 expressed in Escherichia coli XL1-Blue Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.4 C45S Ser-45 mutant is highly purified, shows 5270fold lower activity than wild-type enzyme. Destroyed disulfide bond between Cys-45 and Cys-50 of the active disulfide center in human E3. UV-visible spectrum of the Ser-45 mutant is similar to that of the reduced form of the enzyme and the second fluorescence emission of the mutant disappears Homo sapiens
1.8.1.4 C45Y purification of the Tyr-45 mutant is not successful. Recombinant human E3 becomes too unstable to be easily obtained from Escherichia coli Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.4
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+
-
 Homo sapiens lipoamide + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.1.4 dihydrolipoamide dehydrogenase
-
 Homo sapiens
1.8.1.4 dihydrolipoamide:NAD+ oxidoreductase
-
 Homo sapiens
1.8.1.4 E3
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 FAD contains one FAD as a prosthetic group in each subunit Homo sapiens
1.8.1.4 NAD+
-
 Homo sapiens