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Isoniazid is a prodrug that inhibits the formation of the mycobacterial cell wall. Isoniazid must be activated by KatG, a bacterial catalase-peroxidase enzyme in Mycobacterium tuberculosis. [53] KatG catalyzes the formation of the isonicotinic acyl radical, which spontaneously couples with NADH to form the nicotinoyl-NAD adduct.
Enzyme Inhibitors Inducers; CYP1A1: Certain foods (e.g., cumin, turmeric) Certain herbs/herbal teas (e.g., peppermint, German chamomile, dandelion, Kava) Amiodarone ...
1559 72303 Ensembl ENSG00000138109 ENSMUSG00000067231 UniProt P11712 n/a RefSeq (mRNA) NM_000771 NM_028191 RefSeq (protein) NP_000762 n/a Location (UCSC) Chr 10: 94.94 – 94.99 Mb Chr 19: 39.05 – 39.08 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Cytochrome P450 family 2 subfamily C member 9 (abbreviated CYP2C9) is an enzyme protein. The enzyme is involved in the metabolism, by ...
Isoniazid is a prodrug and once it has entered the bacteria, it is activated by a peroxidase enzyme, which oxidizes the compound into a free radical form. [99] This radical then reacts with NADH, to produce adducts that are very potent inhibitors of the enzymes enoyl-acyl carrier protein reductase, [100] and dihydrofolate reductase. [101]
1576 n/a Ensembl ENSG00000160868 n/a UniProt P08684 n/a RefSeq (mRNA) NM_001202855 NM_001202856 NM_001202857 NM_017460 n/a RefSeq (protein) NP_001189784 NP_059488 n/a Location (UCSC) Chr 7: 99.76 – 99.78 Mb n/a PubMed search n/a Wikidata View/Edit Human Cytochrome P450 3A4 (abbreviated CYP3A4) (EC 1.14.13.97) is an important enzyme in the body, mainly found in the liver and in the intestine ...
A group of enzymes located in the endoplasmic reticulum, known as cytochrome P-450, is the most important family of metabolizing enzymes in the liver. Cytochrome P-450 is not a single enzyme, but rather consists of a closely related family of 50 isoforms; six of them metabolize 90% of drugs.
The active site of CYP2E1 is the smallest observed in human P450 enzymes, with its small capacity attributed in part to the introduction of an isoleucine at position 115. The side-chain of this residue protrudes out above the heme center, restricting active site volume compared to related enzymes that have less bulky residues at this position. [14]
N-acetyltransferase (NAT) is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to arylamines, arylhydroxylamines and arylhydrazines. [1] [2] [3] They have wide specificity for aromatic amines, particularly serotonin, and can also catalyze acetyl transfer between arylamines without CoA.