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
-
1.3.1.118
-
tuberculosis
-
mycobacterium
-
isoniazid
-
ethionamide
-
antituberculous
-
isonicotinic
-
drug-targeted
-
pharmacology
-
fas-ii
-
antitubercular
- 1.3.1.118
- tuberculosis
- mycobacterium
- isoniazid
- ethionamide
-
antituberculous
-
isonicotinic
-
drug-targeted
- pharmacology
- fas-ii
-
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
Advanced search results
Posttranslational Modification
Posttranslational Modification on EC 1.3.1.118 - meromycolic acid enoyl-[acyl-carrier-protein] reductase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
phosphoprotein
InhA is phosphorylated in vitro by multiple Ser/Thr kinases on residue Thr266.. Activity of InhA is controlled via phosphorylation. Thr266 is the unique kinase phosphoacceptor, both in vitro and in vivo. The physiological relevance of Thr266 phosphorylation is demonstrated using inhA phosphoablative (T266A) or phosphomimetic (T266D/E) mutants. Enoyl reductase activity is severely impaired in the mimetic mutants in vitro, as a consequence of a reduced binding affinity to NADH. Introduction of inhA_T266D/E 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. Phosphorylation of InhA may represent an unusual mechanism that allows Mycobacterium tuberculosis to regulate its mycolic acid content, thus offering a new approach to future anti-tuberculosis drug development
phosphoprotein
-
InhA is phosphorylated in vitro by multiple Ser/Thr kinases on residue Thr266.. Activity of InhA is controlled via phosphorylation. Thr266 is the unique kinase phosphoacceptor, both in vitro and in vivo. The physiological relevance of Thr266 phosphorylation is demonstrated using inhA phosphoablative (T266A) or phosphomimetic (T266D/E) mutants. Enoyl reductase activity is severely impaired in the mimetic mutants in vitro, as a consequence of a reduced binding affinity to NADH. Introduction of inhA_T266D/E 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. Phosphorylation of InhA may represent an unusual mechanism that allows Mycobacterium tuberculosis to regulate its mycolic acid content, thus offering a new approach to future anti-tuberculosis drug development
-