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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
1.3.1.9 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
1.3.1.9 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
1.3.1.118 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
1.3.1.118 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

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
-
-

Synonyms

EC Number Synonyms Comment Organism
1.3.1.9 InhA
-
 Mycobacterium tuberculosis
1.3.1.118 InhA
-
 Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.9 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
1.3.1.118 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

EC Number General Information Comment Organism
1.3.1.9 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
1.3.1.118 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