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
ECTree
1.3.1.118 meromycolic acid enoyl-[acyl-carrier-protein] reductaseAdvanced search results
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results (Engineering
Engineering on EC 1.3.1.118 - meromycolic acid enoyl-[acyl-carrier-protein] reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
I16T
I21V
I47T
similar to wild-type InhA, cross-linking of the isoniazid resistant mutant gives three bands on SDS-PAGE assigned to monomer, dimer, and tetrameric forms of the protein. The inhibition of the enzyme with the isoniazid-NAD adduct results in loss of the band assigned to tetramer. In contrast, cross-linking in the presence of saturating concentrations of NADH yields a lower amount of the tetramer upon SDS-PAGE
S94A
T266A
phosphoablative mutant with activity similar to wild-type enzyme
T266D
phosphomimetic mutant with strongly reduced activity (31.4% compared to wild-type enzyme), introduction of inhA_T266D fails to complement growth and mycolic acid defects of an inhA-thermosensitive Mycobacterium smegmatis strain, in a similar manner to what is observed following isoniazid treatment
T266E
phosphomimetic mutant with strongly reduced activity (29.5% compared to wild-type enzyme), introduction of inhA_T266E fails to complement growth and mycolic acid defects of an inhA-thermosensitive Mycobacterium smegmatis strain, in a similar manner to what is observed following isoniazid treatment
Y158A
mutation improves the KM for the cofactor by a factor of 13
Y158F
mutation improves the KM for the cofactor by a factor of 33
I16T
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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
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I21V
I47T
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similar to wild-type InhA, cross-linking of the isoniazid resistant mutant gives three bands on SDS-PAGE assigned to monomer, dimer, and tetrameric forms of the protein. The inhibition of the enzyme with the isoniazid-NAD adduct results in loss of the band assigned to tetramer. In contrast, cross-linking in the presence of saturating concentrations of NADH yields a lower amount of the tetramer upon SDS-PAGE
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S94A
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mutation confers resistance to both isoniazid and ethionamide. Binding of NADH to the mutant is altered
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T266A
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phosphoablative mutant with activity similar to wild-type enzyme
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T266D
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phosphomimetic mutant with strongly reduced activity (31.4% compared to wild-type enzyme), introduction of inhA_T266D fails to complement growth and mycolic acid defects of an inhA-thermosensitive Mycobacterium smegmatis strain, in a similar manner to what is observed following isoniazid treatment
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Y158A
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mutation improves the KM for the cofactor by a factor of 13
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Y158F
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mutation improves the KM for the cofactor by a factor of 33
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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
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
I21V
similar to wild-type InhA, cross-linking of the isoniazid resistant mutant gives three bands on SDS-PAGE assigned to monomer, dimer, and tetrameric forms of the protein. The inhibition of the enzyme with the isoniazid-NAD adduct results in loss of the band assigned to tetramer. In contrast, cross-linking in the presence of saturating concentrations of NADH yields a lower amount of the tetramer upon SDS-PAGE
S94A
mutation confers resistance to both isoniazid and ethionamide. Binding of NADH to the mutant is altered
S94A
similar to wild-type InhA, cross-linking of the isoniazid resistant mutant gives three bands on SDS-PAGE assigned to monomer, dimer, and tetrameric forms of the protein. The inhibition of the enzyme with the isoniazid-NAD adduct results in loss of the band assigned to tetramer. In contrast, cross-linking in the presence of saturating concentrations of NADH yields a lower amount of the tetramer upon SDS-PAGE
I21V
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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
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I21V
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similar to wild-type InhA, cross-linking of the isoniazid resistant mutant gives three bands on SDS-PAGE assigned to monomer, dimer, and tetrameric forms of the protein. The inhibition of the enzyme with the isoniazid-NAD adduct results in loss of the band assigned to tetramer. In contrast, cross-linking in the presence of saturating concentrations of NADH yields a lower amount of the tetramer upon SDS-PAGE
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