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Literature summary for 1.8.1.4 extracted from

  • Argyrou, A.; Sun, G.; Palfey, B.A.; Blanchard, J.S.
    Catalysis of diaphorase reactions by Mycobacterium tuberculosis lipoamide dehydrogenase occurs at the EH4 level (2003), Biochemistry, 42, 2218-2228.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information transient-state and steady-state kinetics of the enzyme in two-electron-reduced and four-electron-reduced state at 4°C and 25°C, respectively Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced lipoamide + NAD+ Mycobacterium tuberculosis enzyme catalyzes the NAD+-dependent oxidation of dihydrolipoyl cofactors being covalently attached to the acyltransferase components of pyruvate dehydrogenase, 2-ketoglutarate dehydrogenase, and glycine reductase multienzyme complexes oxidized lipoamide + NADH
-
r

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+ in the two-electron-reduced enzyme, the disulfide is reduced while the FAD cofactor is oxidized, in the four-electron-reduced enzyme, both redox centers are reduced, mechanism of the diaphorase reaction which occurs when the enzyme is in the four-electron-reduced state Mycobacterium tuberculosis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricyanide + NADH
-
Mycobacterium tuberculosis 2 ferrocyanide + NAD+ + H+
-
?
2,6-dimethyl-1,4-benzoquinone + NADH 90fold reaction by the enzyme in four-electron-reduced state compared to the enzyme in two-electron-reduced state Mycobacterium tuberculosis 2,6-dimethyl-1,4-benzoquinol + NAD+
-
?
DL-lipoate + NADH
-
Mycobacterium tuberculosis ? + NAD+
-
?
DL-lipoylbutanoate + NADH
-
Mycobacterium tuberculosis ? + NAD+
-
?
DL-lipoylpentanoate + NADH 100fold reaction by the enzyme in two-electron-reduced state compared to the enzyme in four-electron-reduced state Mycobacterium tuberculosis ? + NAD+
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
-
Mycobacterium tuberculosis NAD+ + reduced 2,6-dichlorophenolindophenol
-
?
O2 + NADH 40fold reaction by the enzyme in four-electron-reduced state compared to the enzyme in two-electron-reduced state Mycobacterium tuberculosis H2O2 + NAD+
-
?
reduced DL-lipoamide + NAD+
-
Mycobacterium tuberculosis oxidized DL-lipoamide + NADH
-
r
reduced lipoamide + NAD+ enzyme catalyzes the NAD+-dependent oxidation of dihydrolipoyl cofactors being covalently attached to the acyltransferase components of pyruvate dehydrogenase, 2-ketoglutarate dehydrogenase, and glycine reductase multienzyme complexes Mycobacterium tuberculosis oxidized lipoamide + NADH
-
r

Synonyms

Synonyms Comment Organism
diaphorase
-
Mycobacterium tuberculosis
lipoamide dehydrogenase
-
Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.25
-
O2 pH 7.5, 25°C Mycobacterium tuberculosis
190
-
2,6-dimethyl-1,4-benzoquinone pH 7.5, 25°C Mycobacterium tuberculosis
220
-
DL-lipoylpentanoate pH 7.5, 25°C Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
FAD tightly but noncovalently bound to the enzyme, the cofactor cycles between reduced and oxidized state during catalysis Mycobacterium tuberculosis
additional information enzyme contains a redox-active disulfid, the cofactor cycles between reduced and oxidized state during catalysis, in the two-electron-reduced enzyme, the disulfide is reduced while the FAD cofactor is oxidized, in the four-electron.reduced enzyme, both redox centers are reduced Mycobacterium tuberculosis
NAD+
-
Mycobacterium tuberculosis
NADH
-
Mycobacterium tuberculosis