4c50: Difference between revisions
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==See Also== | ==See Also== | ||
*[[Catalase|Catalase]] | *[[Catalase 3D structures|Catalase 3D structures]] | ||
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Revision as of 12:18, 30 October 2019
Crystal Structure of the Catalase-Peroxidase (KatG) D137S mutant from Mycobacterium TuberculosisCrystal Structure of the Catalase-Peroxidase (KatG) D137S mutant from Mycobacterium Tuberculosis
Structural highlights
Function[KATG_MYCTU] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid (INH) lyase and isonicotinoyl-NAD synthase activity. May play a role in the intracellular survival of mycobacteria. May be involved in DNA repair. Partly complements recA-deficient E.coli cells exposed to UV radiation, mitomycin C or hydrogen peroxide. Increases resistance to mitomycin C in E.coli cells deficient for either uvrA, uvrB or uvrC.[1] Publication Abstract from PubMedPeroxidatic activation of the anti-tuberculosis pro-drug isoniazid by Mycobacterium tuberculosis catalase-peroxidase (KatG) is regulated by gating residues of a heme access channel. The steric restriction at the bottleneck of this channel is alleviated by replacement of residue Asp137 with Ser, according to crystallographic and kinetic studies. Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid.,Zhao X, Hersleth HP, Zhu J, Andersson KK, Magliozzo RS Chem Commun (Camb). 2013 Nov 4. PMID:24185282[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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