4c50

Crystal Structure of the Catalase-Peroxidase (KatG) D137S mutant from Mycobacterium TuberculosisCrystal Structure of the Catalase-Peroxidase (KatG) D137S mutant from Mycobacterium Tuberculosis

FunctionFunction

[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]

About this StructureAbout this Structure

4c50 is a 2 chain structure. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ Zhao X, Hersleth HP, Zhu J, Andersson KK, Magliozzo RS. Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid. Chem Commun (Camb). 2013 Nov 4. PMID:24185282 doi:http://dx.doi.org/10.1039/c3cc47022a

↑ Mulder MA, Nair S, Abratt VR, Zappe H, Steyn LM. Involvement of the N- and C-terminal domains of Mycobacterium tuberculosis KatG in the protection of mutant Escherichia coli against DNA-damaging agents. Microbiology. 1999 Aug;145 ( Pt 8):2011-21. PMID:10463167

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OCA

[2] Zhao X, Hersleth HP, Zhu J, Andersson KK, Magliozzo RS. Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid. Chem Commun (Camb). 2013 Nov 4. PMID:24185282 doi:http://dx.doi.org/10.1039/c3cc47022a

[1] Mulder MA, Nair S, Abratt VR, Zappe H, Steyn LM. Involvement of the N- and C-terminal domains of Mycobacterium tuberculosis KatG in the protection of mutant Escherichia coli against DNA-damaging agents. Microbiology. 1999 Aug;145 ( Pt 8):2011-21. PMID:10463167

[1]

[xtra 1]