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

被引：25

作者：

Zhao, Xiangbo ^{[1
,2
]}

Hersleth, Hans-Petter ^{[3
]}

Zhu, Janan ^{[1
,2
]}

Andersson, K. Kristoffer ^{[3
]}

Magliozzo, Richard S. ^{[1
,2
]}

机构：

[1] CUNY Brooklyn Coll, Dept Chem, Brooklyn, NY 11210 USA

[2] CUNY, Grad Ctr, Brooklyn, NY 11210 USA

[3] Univ Oslo, Dept Biosci, POB 1066, NO-0316 Oslo, Norway

来源：

CHEMICAL COMMUNICATIONS | 2013年 / 49卷 / 99期

基金：

美国国家科学基金会;

关键词：

COMPOUND-II; WILD-TYPE; MUTANT; RESISTANCE; INHA; NADH; CONVERSION; OXIDATION; RADICALS; PROTEIN;

D O I：

10.1039/c3cc47022a

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：11650 / 11652

页数：3

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