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Literature summary for 1.8.1.4 extracted from

  • Argyrou, A.; Blanchard, J.S.; Palfey, B.A.
    The lipoamide dehydrogenase from Mycobacterium tuberculosis permits the direct observation of flavin intermediates in catalysis (2002), Biochemistry, 41, 14580-14590.
    View publication on PubMed
Search for more literature for 1.8.1.4

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information transient-state kinetics of reductive and oxidative half-reactions 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+ formation of a FADH2-NAD+ intermediate in catalysis, reaction mechanism of reductive and oxidative half-reactions involving enzyme, FAD/FADH2, and NAD+/NADH Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
reduced lipoamide + NAD+
-
 Mycobacterium tuberculosis oxidized 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
lipoamide dehydrogenase
-
 Mycobacterium tuberculosis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
 assays are performed at 4°C and at 25°C Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 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 disulfide, the cofactor cycles between reduced and oxidized state during catalysis Mycobacterium tuberculosis
NAD+ dependent on Mycobacterium tuberculosis
NADH
-
 Mycobacterium tuberculosis