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Article

Impact of distal side water and residue 315 on ligand binding to ferric Mycobacterium tuberculosis catalase-peroxidase (KatG).

Biochemistry - 25 Nov 2008

Ranguelova Kalina, Suarez Javier, Metlitsky Leonid, Yu Shengwei, Brejt Shelly Zev, Brejt Sidney Zelig, Zhao Lin, Schelvis Johannes P M, Magliozzo Richard S

Abstract excerpt

The catalase-peroxidase (KatG) of Mycobacterium tuberculosis (Mtb) is important for the virulence of this pathogen and also is responsible for activation of isoniazid (INH), an antibiotic in use for over 50 years in the first line treatment against tuberculosis infection. Overexpressed Mtb KatG contains a heterogeneous population of heme species that present distinct spectroscopic properties and, as described...

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PMID: 18956888
DOI: 10.1021/bi801511u

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Impact of distal side water and residue 315 on ligand binding to ferric Mycobacterium tuberculosis catalase-peroxidase (KatG).PMID 18956888Read ↗

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