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Literature summary extracted from

  • Voegeli, B.; Rosenthal, R.G.; Stoffel, G.M.M.; Wagner, T.; Kiefer, P.; Cortina, N.S.; Shima, S.; Erb, T.J.
    InhA, the enoyl-thioester reductase from Mycobacterium tuberculosis forms a covalent adduct during catalysis (2018), J. Biol. Chem., 293, 17200-17207 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.3.1.9 T196A mutant retains 1.0% of wild-type kcat Mycobacterium tuberculosis
1.3.1.9 T196V mutant retains 0.15% of wild-type kcat Mycobacterium tuberculosis
1.3.1.9 Y158F mutant retains only 1.8% of the wild-type kcat with a 2fold increase of the Km for octenoyl-CoA. Residue Y158 is essential for stereospecificity of protonation, the mutant accumulates a covalent adduct between crotonyl-CoA and NADH Mycobacterium tuberculosis
1.3.1.9 Y158S strong decrease in kcat to only 0.16% of wild-type activity Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.9 0.01
-
 NADH mutant Y158F, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.056
-
 NADH mutant Y158S, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.059
-
 NADH mutant T196A, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.09
-
 NADH wild-type, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.11
-
 NADH mutant T196V, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.8
-
 octenoyl-CoA wild-type, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.9
-
 octenoyl-CoA mutant Y158S, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 2
-
 octenoyl-CoA mutant Y158F, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 4.3
-
 octenoyl-CoA mutant T196V, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 7.6
-
 octenoyl-CoA mutant T196A, pH 6.8, 30°C Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.9 Mycobacterium tuberculosis P9WGR1
-
-
1.3.1.9 Mycobacterium tuberculosis H37Rv P9WGR1
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.9 octenoyl-CoA + NADH + H+
-
 Mycobacterium tuberculosis octanoyl-CoA + NAD+
-
 ?
1.3.1.9 octenoyl-CoA + NADH + H+
-
 Mycobacterium tuberculosis H37Rv octanoyl-CoA + NAD+
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.1.9 0.0051
-
 NADH mutant T196V, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.0055
-
 octenoyl-CoA mutant Y158S, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.0059
-
 NADH mutant Y158S, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.0073
-
 octenoyl-CoA mutant T196V, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.012
-
 NADH mutant T196A, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.05
-
 octenoyl-CoA mutant T196A, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.079
-
 NADH mutant Y158F, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 0.088
-
 octenoyl-CoA mutant Y158F, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 3.5
-
 NADH wild-type, pH 6.8, 30°C Mycobacterium tuberculosis
1.3.1.9 3.6
-
 octenoyl-CoA wild-type, pH 6.8, 30°C Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
1.3.1.9 metabolism the NADH cofactor and the CoA thioester substrate form a covalent adduct during the InhA catalytic cycle. Residue Tyr158 is required for the stereospecificity of protonation and Thr196 is partially involved in hydride transfer and protonation Mycobacterium tuberculosis