Inactivation of Isoniazid by Peroxidase

Tirunarayanan, M. O.; Vischer, W. A.

doi:10.1038/183681a0

Cited by 5 publications

(2 citation statements)

References 6 publications

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“…Enzyme I is probably the hydroperoxidase enzyme which has been shown to be missing in resistant strains of mycobacteria (Middlebrook, Cohn & Schaeffer, 1954;Tirunarayanan & Vischer 1959). This enzyme is heat-labile, sensitive to cyanide and also to azide (Youatt, 1958b).…”

Section: J W T Wimpenny Discussionmentioning

confidence: 99%

The uptake and fate of Isoniazid in Mycobacterium tuberculosis var. bovis BCG

Wimpenny

1967

Journal of General Microbiology

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S U M M A R YThe incorporation of 14C INH into sensitive and resistant bacteria has been investigated. Only organisms susceptible to INH took up the drug. Uptake was irreversible and became saturated at higher INH concentrations. Uptake was heat-labile, KCN-sensitive, partially inhibited by dinitrophenol and stimulated by SH group reagents. The activation energy of binding was of the same order as the activation energy of an enzyme catalysed reaction. Uptake at 37" was rapidly inhibited although at 4" it was not. The INH binding mechanism had many of the properties of catalase and peroxidase. It seems likely that all these functions were part of one enzyme which was missing from INH-resistant BCG.Chromatographic studies on hot-water extracts of INH-treated BCG indicated that INH was converted into several unidentified products within the organism. I N T R O D U C T I O NThe effect of isoniazid (INH) on the biosynthesis of a number of components of BCG has been examined in an earlier paper (Wimpenny, 1967). However, in attempting to elucidate both the mode of action and the specificity of INH as an anti-tubercular agent, the fate of the drug itselfin the sensitive organism must be traced. Several papers have been published which throw some light on this aspect of the problem. Barclay, Ebert & Koch-Weser (1953) showed that Mycobacterium tuberculosis var. hominis strain H 37 RV sensitive to INH took up the drug, whilst a resistant variant did not. In later experiments (Barclay, Koch-Weser & Ebert, 1954) using the same organism, they investigated the uptake of 14C isonicotinic acid, 14C nicotinamide and 14C nicotinic acid. Of these compounds, 14C INH was bound and then only by the drug-sensitive strain. Organisms killed by heat or with formalin did not fix INH. These workers indicated that uptake of INH was greater at 5" than at 37" in living bacteria and concluded that INH was bound by physical adsorption. Youatt ( 1 9 5 8~) confirmed that 14C INH was bound only by sensitive mycobacteria. She showed that the drug was fixed only under actively metabolizing conditions and that uptake in sensitive mycobacteria was sensitive to cyanide, azide and heat. She found that Staphylococcus aureus, Escherichia coli, Mycobacterium phlei, Proteus mirabilis, Bacillus megatherium and Candida albicans took up very little INH. In addition Youatt showed (19583) that the rate of breakdown of INH was greater in living BCG than in heat killed organisms.

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Section: J W T Wimpenny Discussionmentioning

confidence: 99%

The uptake and fate of Isoniazid in Mycobacterium tuberculosis var. bovis BCG

Wimpenny

1967

Journal of General Microbiology

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“…[28][29][30][31] It has been shown that HRP selectively removes phenylhydrazine protecting group under mild conditions. 32 Previous reports have demonstrated that peroxidase is able to use a number of hydrazine derivatives as substrates, [33][34][35] including 3-aminophthalhydrazide 36 known as luminol.…”

Section: Introductionmentioning

confidence: 99%

Ultrasensitive optical detection of hydrogen peroxide by triggered activation of horseradish peroxidase

Virel¹,

Saá²,

Köster³

et al. 2010

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Hydrogen peroxide is a very reactive byproduct of many metabolic pathways. We describe an ultra-sensitive colorimetric method to detect hydrogen peroxide based on the reconstitution of apo-horseradish peroxidase with the hemin derivative, hemin di(N,N'-acetyl-hydrazide). Oxidation of the latter by hydrogen peroxide yields hemin, which is able to reconstitute apo-horseradish peroxidase, forming an active peroxidase. We have also applied this analyte-triggered reconstitution of horseradish peroxidase to detect the activity of the enzyme glucose oxidase.

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Isonicotinic Acid Hydrazide

Murti¹

1975

Mechanism of Action of Antimicrobial and Antitumor Agents

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Inactivation of Isoniazid by Peroxidase

Cited by 5 publications

References 6 publications

The uptake and fate of Isoniazid in Mycobacterium tuberculosis var. bovis BCG

The uptake and fate of Isoniazid in Mycobacterium tuberculosis var. bovis BCG

Ultrasensitive optical detection of hydrogen peroxide by triggered activation of horseradish peroxidase

Isonicotinic Acid Hydrazide

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