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Literature summary extracted from

  • Luckner, S.; Liu, N.; Am Ende, C.; Tonge, P.; Kisker, C.
    A slow, tight binding inhibitor of InhA, the enoyl-acyl carrier protein reductase from Mycobacterium tuberculosis (2010), J. Biol. Chem., 285, 14330-14337 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.9 expression in Escherichia coli BL21(DE3)pLysS Mycobacterium tuberculosis
1.3.1.118 expression in Escherichia coli BL21(DE3)pLysS Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.1.9 hanging drop vapor diffusion technique, formation of the ternary enzyme/NAD+x012-(o-tolyloxy)-5-hexylphenol complex Mycobacterium tuberculosis
1.3.1.118 hanging drop vapor diffusion technique, formation of the ternary enzyme/NAD+x012-(o-tolyloxy)-5-hexylphenol complex Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.9 2-(o-tolyloxy)-5-hexylphenol i.e. PT70, slow, tight binding inhibitor. It binds preferentially to the enzyme/NAD+x01complex and has a residence time of 24 min on the target, which is 14000 times longer than that of the rapid reversible inhibitor from which it is derived. The 1.8 A crystal structure of the ternary complex between InhA, NAD+, and PT70 reveals the molecular details of enzyme inhibitor recognition and supports the hypothesis that slow onset inhibition is coupled to ordering of an active site loop, which leads to the closure of the substrate-binding pocket Mycobacterium tuberculosis
1.3.1.118 2-(o-tolyloxy)-5-hexylphenol i.e. PT70, slow, tight binding inhibitor. It binds preferentially to the enzyme/NAD+x01complex and has a residence time of 24 min on the target, which is 14000 times longer than that of the rapid reversible inhibitor from which it is derived. The 1.8 A crystal structure of the ternary complex between InhA, NAD+, and PT70 reveals the molecular details of enzyme inhibitor recognition and supports the hypothesis that slow onset inhibition is coupled to ordering of an active site loop, which leads to the closure of the substrate-binding pocket Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.9 Mycobacterium tuberculosis P9WGR1
-
-
1.3.1.9 Mycobacterium tuberculosis ATCC 25618 P9WGR1
-
-
1.3.1.118 Mycobacterium tuberculosis P9WGR1
-
-
1.3.1.118 Mycobacterium tuberculosis ATCC 25618 P9WGR1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.9
-
Mycobacterium tuberculosis
1.3.1.118
-
Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
1.3.1.9 enoyl-ACP reductase
-
Mycobacterium tuberculosis
1.3.1.9 InhA
-
Mycobacterium tuberculosis
1.3.1.118 enoyl-ACP reductase
-
Mycobacterium tuberculosis
1.3.1.118 InhA
-
Mycobacterium tuberculosis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.3.1.9 0.000022
-
2-(o-tolyloxy)-5-hexylphenol pH 6.8, 23°C Mycobacterium tuberculosis
1.3.1.118 0.000022
-
2-(o-tolyloxy)-5-hexylphenol pH 6.8, 23°C Mycobacterium tuberculosis

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.3.1.9 0.0000053
-
pH 6.8, 23°C, at 10 nM enzyme concentration Mycobacterium tuberculosis 2-(o-tolyloxy)-5-hexylphenol
1.3.1.9 0.0000503
-
pH 6.8, 23°C, at 100 nM enzyme concentration Mycobacterium tuberculosis 2-(o-tolyloxy)-5-hexylphenol
1.3.1.118 0.0000053
-
pH 6.8, 23°C, at 10 nM enzyme concentration Mycobacterium tuberculosis 2-(o-tolyloxy)-5-hexylphenol
1.3.1.118 0.0000503
-
pH 6.8, 23°C, at 100 nM enzyme concentration Mycobacterium tuberculosis 2-(o-tolyloxy)-5-hexylphenol