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Literature summary for 1.3.1.118 extracted from

  • Chollet, A.; Maveyraud, L.; Lherbet, C.; Bernardes-Genisson, V.
    An overview on crystal structures of InhA protein Apo-form, in complex with its natural ligands and inhibitors (2018), Eur. J. Med. Chem., 146, 318-343 .
    View publication on PubMed

Application

Application Comment Organism
pharmacology the enzyme is a target for the development of new anti-tubercular drugs Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
overview of 80 available crystal structures of wild-type and mutant InhA, in its apo form, in complex with its cofactor, with an analogue of its natural ligands (C16 fatty acid and/or NADH) or with inhibitor Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
K165A mutation prevents NADH from binding Mycobacterium tuberculosis
K165M mutation prevents NADH from binding Mycobacterium tuberculosis
K165Q mutation has no effect on NADH binding Mycobacterium tuberculosis
K165R mutation has no effect on NADH binding Mycobacterium tuberculosis
Y158A mutation improves the KM for the cofactor by a factor of 13 Mycobacterium tuberculosis
Y158F mutation improves the KM for the cofactor by a factor of 33 Mycobacterium tuberculosis
Y158S mutation has no effect on NADH binding Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
Ethionamide the indirect inhibitor forms a covalent adduct with the cofactor Mycobacterium tuberculosis
Genz10850
-
Mycobacterium tuberculosis
GENZ8575
-
Mycobacterium tuberculosis
isoniazid the indirect inhibitor forms a covalent adduct with the cofactor, leading compound for antitubercular drug therapy Mycobacterium tuberculosis
additional information overview of 80 available crystal structures of wild-type and mutant InhA, in its apo form, in complex with its cofactor, with an analogue of its natural ligands (C16 fatty acid and/or NADH) or with inhibitors Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WGR1
-
-
Mycobacterium tuberculosis ATCC 25618 P9WGR1
-
-

Synonyms

Synonyms Comment Organism
enoyl-ACP reductase InhA
-
Mycobacterium tuberculosis

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.00016
-
pH and temperature not specified in the publication Mycobacterium tuberculosis Genz10850
0.0024
-
pH and temperature not specified in the publication Mycobacterium tuberculosis GENZ8575

General Information

General Information Comment Organism
metabolism the enzyme is involved in the mycobacterial fatty acid biosynthesis pathway. It is essential for the survival of Mycobacterium tuberculosis Mycobacterium tuberculosis
physiological function the enzyme is the causative agent of tuberculosis Mycobacterium tuberculosis