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Mechanistic Studies of the Oxidation of Isoniazid by the Catalase Peroxidase from Mycobacterium tuberculosis

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Johnsson, Kai, Schultz, Peter G.·1994·Journal of the American Chemical Society

Abstract

The enzymic oxidn. of isoniazid by the catalase-peroxidase of Mycobacterium tuberculosi was studied. The reaction products suggest two reaction pathways involving both electrophilic and radical species. Labeling expts. are consistent with a reaction mechanism involving the formation of an acyldiimide intermediate followed by decompn. to the corresponding aldehyde and peracid. The results suggest that isoniazid is oxidized by the catalase-peroxidase to a reactive species that may act by inactivating an essential enzyme of M. tuberculosis. [on SciFinder (R)]

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Metadata

Authors
Johnsson, K., & Schultz, P. G.
Venue
Journal of the American Chemical Society
Published
1994-08
Volume
116
Issue
16
Pages
7425-7426
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
OpenAlex
W2093602098
Cited by
278
References
0
FWCI
9.11
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Mechanistic Studies of the Oxidation of Isoniazid by the Catalase Peroxidase from Mycobacterium tuberculosis. https://app.cochat.ai/papers/10.1021/ja00095a063
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Johnsson, K., & Schultz, P. G. (1994). Mechanistic Studies of the Oxidation of Isoniazid by the Catalase Peroxidase from Mycobacterium tuberculosis. Journal of the American Chemical Society. https://doi.org/10.1021/ja00095a063

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.