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

BRENDA support

Literature summary for 1.3.1.9 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
Search for more literature for 1.3.1.9

Protein Variants

Protein Variants Comment Organism
T196A mutant retains 1.0% of wild-type kcat Mycobacterium tuberculosis
T196V mutant retains 0.15% of wild-type kcat Mycobacterium tuberculosis
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
Y158S strong decrease in kcat to only 0.16% of wild-type activity Mycobacterium tuberculosis

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WGR1
-
-
Mycobacterium tuberculosis H37Rv P9WGR1
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

General Information

General Information Comment Organism
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