Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Kim, H.
    Characterization of site-specific human dihydrolipoamide dehydrogenase mutant with a switched kinetic mechanism (2014), Bull. Korean Chem. Soc., 35, 1603-1604 .
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.4 A328V site-directed mutagenesis of the conserved residue, the site-specific dihydrolipoamide dehydrogenase mutant shows a switched kinetic mechanism, it shows a random sequential kinetic mechanism with an interaction factor (alpha) of 8.5. The mutation deteriorates substantially the catalytic power of human E3 enzyme increasing the binding affinity for NAD+ and dihydrolipoamide . The mutation triggers this potential intrinsic property of the enzyme causing the kinetic mechanism of the mutant to switch from a ping-pong mechanism to a random sequential mechanism Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.4 additional information
-
 additional information kinetic analysis and mechanisms of wild-type and mutant enzymes, overview Homo sapiens
1.8.1.4 0.024
-
 NAD+ enzyme mutant, pH 8.0, 37°C Homo sapiens
1.8.1.4 0.027
-
 dihydrolipoamide enzyme mutant, pH 8.0, 37°C Homo sapiens
1.8.1.4 0.19
-
 NAD+ wild-type enzyme, pH 8.0, 37°C Homo sapiens
1.8.1.4 0.63
-
 dihydrolipoamide wild-type enzyme, pH 8.0, 37°C Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+ Homo sapiens
-
 lipoamide + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Homo sapiens P09622
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.1.4 protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+ kinetic mechanism of human E3 enzyme is a ping-pong mechanism. In human E3, dihydrolipoamide binds to the si-face of FAD, whereas NAD+ binds to the re-face. These two spatially separate substrate binding sites can allow the enzyme to form a ternary complex with two substrates, which is an essential feature of the sequential mechanism Homo sapiens
a

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+
-
 r

Subunits

EC Number Subunits Comment Organism
1.8.1.4 homodimer
-
 Homo sapiens

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.1.4 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.4 8
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 FAD
-
 Homo sapiens
1.8.1.4 NAD+
-
 Homo sapiens
1.8.1.4 NADH
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.8.1.4 evolution E3 belongs to the pyridine nucleotide-disulfide oxidoreductase family along with glutathione reductase (GR), thioredoxin reductase, mercuric reductase and trypanothione reductase Homo sapiens
1.8.1.4 additional information residue Ala328 is absolutely conserved, suggesting that it might be important for the structure and function of human E3. Ala328 is a component of alpha-helix 8 and is located near the presumed dihydrolipoamide binding channel. Ala328 is also located close to the active disulfide center between Cys45 and Cys50 Homo sapiens
1.8.1.4 physiological function E3 catalyzes the reoxidation of the dihydrolipoyl prosthetic group attached to the lysyl residue(s) of the acyltransferase components of these dehydrogenase complexes Homo sapiens