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Literature summary for 1.3.1.118 extracted from

  • Schroeder, E.; Basso, L.; Santos, D.; De Souza, O.
    Molecular dynamics simulation studies of the wild-type, I21V, and I16T mutants of isoniazid-resistant Mycobacterium tuberculosis enoyl reductase (InhA) in complex with NADH Toward the understanding of NADH-InhA different affinities (2005), Biophys. J., 89, 876-884 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
I16T mutation in the glycine-rich loop. Although very flexible, in the wild-type enzyme/NADH complex, the NADH molecule keeps its extended conformation firmly bound to the binding site of the enzyme. In the mutant complex, the NADH pyrophosphate moiety undergoes considerable conformational changes, reducing its interactions with its binding site and probably indicating the initial phase of ligand expulsion from the cavity Mycobacterium tuberculosis
I21V mutation in the glycine-rich loop. Although very flexible, in the wild-type enzyme/NADH complex, the NADH molecule keeps its extended conformation firmly bound to the binding site of the enzyme. In the mutant complex, the NADH pyrophosphate moiety undergoes considerable conformational changes, reducing its interactions with its binding site and probably indicating the initial phase of ligand expulsion from the cavity Mycobacterium tuberculosis

Organism

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

Synonyms Comment Organism
InhA
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 Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NADH although very flexible, in the wild-type enzyme/NADH complex, the NADH molecule keeps its extended conformation firmly bound to the binding site of the enzyme Mycobacterium tuberculosis

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the NADH-dependent reduction of long-chain trans-2-enoyl-ACP fatty acids, an intermediate in mycolic acid biosynthesis Mycobacterium tuberculosis