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1.3.1.118: meromycolic acid enoyl-[acyl-carrier-protein] reductase

This is an abbreviated version!
For detailed information about meromycolic acid enoyl-[acyl-carrier-protein] reductase, go to the full flat file.

Word Map on EC 1.3.1.118

Reaction

a meromycolyl-[acyl-carrier protein]
+
NAD+
=
a trans-DELTA2-meromycolyl-[acyl-carrier protein]
+
NADH
+
H+

Synonyms

2-trans-enoyl-ACP reductase, 2-trans-enoyl-ACP(CoA) reductase, 2-trans-enoyl-acyl carrier protein reductase, enoyl acyl carrier protein reductase, enoyl acyl carrier protein reductase InhA, enoyl-ACP reductase, enoyl-ACP reductase InhA, enoyl-acyl carrier protein reductase, FAS-II enoyl reductase, FASII enoyl-ACP reductase, InhA, InhA Protein, MtInhA

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.1 With NAD+ or NADP+ as acceptor
                1.3.1.118 meromycolic acid enoyl-[acyl-carrier-protein] reductase

Crystallization

Crystallization on EC 1.3.1.118 - meromycolic acid enoyl-[acyl-carrier-protein] reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization and structure determination of InhA ternary complexes with PT501, PT504, PT506, PT511, PT512 and PT514
crystallization of InhA with isoniazid-NADP bound and the structure of the complex is solved
hanging drop vapor diffusion technique, formation of the ternary enzyme/NAD+x012-(o-tolyloxy)-5-hexylphenol complex
molecular docking studies are performed on the crystal structure of Mycobacterium tuberculosis enoyl reductase (InhA) complexed with 1-cyclohexyl-N-(3,5-dichlorophenyl)-5-oxopyrrolidine-3-carboxamide
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
the crystal structure of the enzyme in complex with NAD+ and trans-2-hexadecenoyl-(N-acetylcysteamine)-thioester reveals that the substrate binds in a general U-shaped conformation, with the trans double bond positioned directly adjacent to the nicotinamide ring of NAD+. The side chain of Tyr158 directly interacts with the thioester carbonyl oxygen of the C16 fatty acyl substrate and therefore can help stabilize the enolate intermediate, proposed to form during substrate catalysis. Hydrophobic residues, primarily from the substrate binding loop (residues 196-219), engulf the fatty acyl chain portion of the substrate. The substrate binding loop of InhA is longer than that of other enoyl-ACP reductases and creates a deeper substrate binding crevice, consistent with the ability of InhA to recognize longer chain fatty acyl substrates
the crystal structure of the enzyme in complex with the inhibitor N-(4-methylbenzoyl)-4-benzylpiperidine reveals the binding mode of the inhibitor within the active site