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InhA plays a key role in the synthesis of fatty acids, particularly in M. tuberculosis which, has type one fatty acid synthesis (FASI) and type two fatty acid synthesis (FASII) which together function in the synthesis of mycolic acids. FASI synthesizes C16-18 and C24-26 fatty acids.
InhA, representing 2-trans-enoyl-acyl carrier protein reductase and the target for the front-line antituberculous drug isoniazid, is involved in the activity of dissociative type 2 fatty acid synthase (FASII) that extends associative type 1 fatty acid synthase (FASI)-derived C20 fatty acids to form C60-to-C90 mycolic
INHA (Inhibin Subunit Alpha) is a Protein Coding gene. Diseases associated with INHA include Multidrug-Resistant Tuberculosis and Sertoli Cell Tumor. Among its related pathways are Signaling by TGFB family members and Peptide hormone metabolism.
Histidine ammonia-lyase is the first enzyme in the degradation pathway of l-histidine and catalyzes the nonoxidative deamination of histidine (12) to form trans-urocanic acid (13) plus ammonia (Equation (3)).
InhA, the primary target for the first line anti-tuberculosis drug isoniazid, is a key enzyme of the fatty-acid synthase II system involved in mycolic acid biosynthesis in Mycobacterium tuberculosis. In this study, we show that InhA is a substrate for mycobacterial serine/threonine protein kinases.
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