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
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1.3.1.118
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tuberculosis
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mycobacterium
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isoniazid
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ethionamide
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antituberculous
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isonicotinic
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drug-targeted
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pharmacology
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fas-ii
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antitubercular
- 1.3.1.118
- tuberculosis
- mycobacterium
- isoniazid
- ethionamide
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antituberculous
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isonicotinic
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drug-targeted
- pharmacology
- fas-ii
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antitubercular
Reaction
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
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Substrates Products
Substrates Products on EC 1.3.1.118 - meromycolic acid enoyl-[acyl-carrier-protein] reductase
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REACTION DIAGRAM
trans-2-octenoyl-[acyl-carrier protein] + NADH + H+
octanoyl-[acyl-carrier protein] + NAD+
decanoyl-CoA + NAD+
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trans-2-decenoyl-CoA + NADH + H+
decanoyl-CoA + NAD+
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trans-2-decenoyl-CoA + NADH + H+
decanoyl-CoA + NAD+
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dodecanoyl-CoA + NAD+
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trans-2-dodecenoyl-CoA + NADH + H+
dodecanoyl-CoA + NAD+
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trans-2-dodecenoyl-CoA + NADH + H+
dodecanoyl-CoA + NAD+
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pre-steady state kinetics and equilibrium data of 2-trans-dodecenoyl-CoA substrate binding to InhA. The results indicate both positive homotropic cooperativity upon substrate binding to InhA, and a bimolecular association process followed by a slow isomerization of the enzyme-substrate binary complex
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trans-2-dodecenoyl-CoA + NADH + H+
dodecanoyl-CoA + NAD+
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trans-2-dodecenoyl-CoA + NADH + H+
dodecanoyl-CoA + NAD+
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trans-2-dodecenoyl-CoA + NADH + H+
dodecanoyl-CoA + NAD+
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hexadecanoyl-CoA + NAD+
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trans-2-hexadecenoyl-CoA + NADH + H+
hexadecanoyl-CoA + NAD+
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octanoyl-CoA + NAD+
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trans-2-octenoyl-CoA + NADH + H+
octanoyl-CoA + NAD+
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octanoyl-[acyl-carrier protein] + NAD+
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trans-2-octenoyl-[acyl-carrier protein] + NADH + H+
octanoyl-[acyl-carrier protein] + NAD+
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no activity with crotonoyl-CoA. The enzyme preferentially reduces long-chain 2-trans-enoyl-ACP substrates (12-24 carbons). The two substrates bind to InhA via a sequential kinetic mechanism, with the preferred ordered addition of NADH and the enoyl substrate. The chemical mechanism involves stereospecific hydride transfer of the 4S hydrogen of NADH to the C3 position of the 2-trans-enoyl substrate, followed by protonation at C2 of an enzymestabilized enolate intermediate
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additional information
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no activity with crotonoyl-CoA. The enzyme preferentially reduces long-chain 2-trans-enoyl-ACP substrates (12-24 carbons). The two substrates bind to InhA via a sequential kinetic mechanism, with the preferred ordered addition of NADH and the enoyl substrate. The chemical mechanism involves stereospecific hydride transfer of the 4S hydrogen of NADH to the C3 position of the 2-trans-enoyl substrate, followed by protonation at C2 of an enzymestabilized enolate intermediate
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additional information
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no activity with crotonoyl-CoA. The enzyme preferentially reduces long-chain 2-trans-enoyl-ACP substrates (12-24 carbons). The two substrates bind to InhA via a sequential kinetic mechanism, with the preferred ordered addition of NADH and the enoyl substrate. The chemical mechanism involves stereospecific hydride transfer of the 4S hydrogen of NADH to the C3 position of the 2-trans-enoyl substrate, followed by protonation at C2 of an enzymestabilized enolate intermediate
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