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Literature summary for 1.8.1.4 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
Search for more literature for 1.8.1.4

Protein Variants

Protein Variants Comment Organism
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens P09622
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + NAD+
-
 Homo sapiens lipoamide + NADH + H+
-
 r

Subunits

Subunits Comment Organism
homodimer
-
 Homo sapiens

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Homo sapiens
NAD+
-
 Homo sapiens
NADH
-
 Homo sapiens

General Information

General Information Comment Organism
evolution E3 belongs to the pyridine nucleotide-disulfide oxidoreductase family along with glutathione reductase (GR), thioredoxin reductase, mercuric reductase and trypanothione reductase Homo sapiens
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
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