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Issue 99, 2013
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Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid

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Abstract

Peroxidatic 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.

Graphical abstract: Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid

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Article information


Submitted
13 Sep 2013
Accepted
17 Oct 2013
First published
18 Oct 2013

Chem. Commun., 2013,49, 11650-11652
Article type
Communication

Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid

X. Zhao, H. Hersleth, J. Zhu, K. K. Andersson and R. S. Magliozzo, Chem. Commun., 2013, 49, 11650
DOI: 10.1039/C3CC47022A

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