New insight into the mechanism of action of and resistance to isoniazid: interaction of Mycobacterium tuberculosis enoyl-ACP reductase with INH-NADP.
Argyrou
Argyrides
A
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.
Vetting
Matthew W
MW
Blanchard
John S
JS
D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism; D024881:Drug Resistance, Bacterial / Q000187:drug effects*; D050753:Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology; D006834:Hydrazines / Q000737:chemistry*; D007538:Isoniazid / Q000494:pharmacology*; D008958:Models, Molecular; D015394:Molecular Structure; D009169:Mycobacterium tuberculosis / Q000187:drug effects* / Q000201:enzymology*; D009249:NADP / Q000378:metabolism*; D009525:Niacin / Q000737:chemistry; D010088:Oxidoreductases / Q000037:antagonists & inhibitors / Q000378:metabolism
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D006834:Hydrazines; D009525:Niacin; C029424:hydrazine; D009249:NADP; D010088:Oxidoreductases; D050753:Enoyl-(Acyl-Carrier-Protein) Reductase (NADH); C085257:InhA protein, Mycobacterium; D007538:Isoniazid