Aromatic hydroxylation during the myeloperoxidase-oxidase oxidation of hydrazines

Walt, B. J. Van Der; Zyl, Johann M. van; Kriegler, A.

doi:10.1016/0006-2952(94)90415-4

Cited by 18 publications

(10 citation statements)

References 32 publications

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“…It has been reported that a G-to -A polymorphism located 463 bp upstream of exon 1 in the promoter region of MPO strongly decreased MPO mRNA expression and enzyme activity (Piedrafita et al 1996). On the basis of this latter observation and the implication of a role for MPO in the metabolic activation of aromatic organic compounds ( Van der Walt et al 1994), the MPO polymorphism may act as a susceptibility factor for some malignant diseases of environmental origins (Schabath et al 2000). Benzene is first metabolized in the liver and then is further activated in bone marrow by MPO to benzoquinones and related free radicals, the ultimate genotoxic metabolites (Ross 1996).…”

Section: Discussionmentioning

confidence: 96%

Genetic polymorphisms involved in toxicant-metabolizing enzymes and the risk of chronic benzene poisoning in Chinese occupationally exposed populations

Chen

Yin

et al. 2007

Xenobiotica

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Benzene is a recognized haematotoxin and leukaemogen, but its mechanism of action and the role of genetic susceptibility are still unclear. Cytochrome P450 2E1 (CYP2E1) and myeloperoxidase (MPO) are involved in benzene activation; and NAD (P)H:quinine oxidoreductase 1 (NQO1), glutathione S-transferase theta 1 (GSTT1) and glutathione S-transferase mu 1 (GSTM1) participate in benzene detoxification. The common, well-studied single-nucleotide polymorphisms (SNPs) were analysed in these genes drawn from the toxicant-metabolizing pathways. A total of 100 workers with chronic benzene poisoning (CBP) and 90 controls were enrolled in China. There was a 2.82-fold (95% CI = 1.42-5.58) increased risk of CBP in the subjects with the NQO1 609C > T mutation genotype (T/T) compared with those carrying heterozygous (C/T) and wild-type (C/C). The subjects with the GSTT1 null genotype had a 1.91-fold (95% CI = 1.05-3.45) increased risk of CBP compared with those with GSTT1 non-null genotype. There was no association of CYP2E1 and MPO genotype with CBP. A three genes' interaction showed that there was a 20.41-fold (95% CI = 3.79-111.11) increased risk of CBP in subjects with the NQO1 609C > T T/T genotype and with the GSTT1 null genotype and the GSTM1 null genotype compared with those carrying the NQO1 609C > T C/T and C/C genotype, GSTT1 non-null genotype, and GSTM1 non-null genotype. The study provides evidence of an association of a gene-gene interaction with the risk of CBP.

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Section: Discussionmentioning

confidence: 96%

Genetic polymorphisms involved in toxicant-metabolizing enzymes and the risk of chronic benzene poisoning in Chinese occupationally exposed populations

Chen

Yin

et al. 2007

Xenobiotica

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“…(164) Aromatic hydroxylation is also observed during the metabolism of the hydrazide derivative isoniazid by MPO where Compound III is generated. (127) As discussed above, it is now established that O 2 •− can react with some of the radicals generated by MPO, to yield hydroperoxides, and subsequent decomposition of these species may account for the formation of some of these hydroxylated products.…”

Section: Modulation Of Myeloperoxidase Catalytic Activity By Other Oxmentioning

confidence: 95%

“…Some radicals can also reduce native MPO to Fe 2+ MPO, which generates Compound III upon reaction with O 2 . This occurs, for example, during MPO-mediated metabolism of hydroquinone, (124,125) amsacrine, (126) hydrazines (127) and hydrazides. (128) Other fates of MPO-generated radicals include reaction with the parent proteins to generate protein-derived radicals (129) and covalent addition to heme.…”

Section: Reactions Of Hypohalous Acidsmentioning

confidence: 99%

Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention

Davies

2010

J. Clin. Biochem. Nutr.

354

228

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There is considerable interest in the role that mammalian heme peroxidase enzymes, primarily myeloperoxidase, eosinophil peroxidase and lactoperoxidase, may play in a wide range of human pathologies. This has been sparked by rapid developments in our understanding of the basic biochemistry of these enzymes, a greater understanding of the basic chemistry and biochemistry of the oxidants formed by these species, the development of biomarkers that can be used damage induced by these oxidants in vivo, and the recent identification of a number of compounds that show promise as inhibitors of these enzymes. Such compounds offer the possibility of modulating damage in a number of human pathologies. This reviews recent developments in our understanding of the biochemistry of myeloperoxidase, the oxidants that this enzyme generates, and the use of inhibitors to inhibit such damage.

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“…Other sources suggest (see Figure 1) that oxidation and acylation are due to biotransformation of an acyl-isonicotinic anion or an isonicotinic acyl radical, respectively [31]. Earlier, Walt and coworkers [32] excluded experimentally under non-enzymatic conditions an iron-catalyzed hydroxyl radical mediated oxidation of isoniazid from the discussion of the mechanism. MtKatG catalyzed activation of isoniazid to form hydrazil radical of isoniazid, and finally isonicotinic acyl radical [28,31,43,91].…”

Section: Katg Genementioning

confidence: 99%

Antitubercular Isoniazid and Drug Resistance of Mycobacterium tuberculosis — A Review

Scior

Morales

Eisele

et al. 2002

Archiv der Pharmazie

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Isoniazid is one of the most potent drugs available for tuberculosis treatment. As a pro-drug it requires activation, which is performed by catalase/peroxidase. The active principle, whose identity has not yet been determined unambiguously, then acts on at least one target molecule, the enoyl-acyl carrier protein, required for the synthesis of the vital mycolic acids present in the cell wall of the bacterium. Some other targets have been proposed in order to explain the unusual potency of isoniazid; however, the supporting data are still controversial. We thoroughly discuss the action of isoniazid, resistance mechanisms, and the possible active product, which includes an isonicotinic acid-NADH adduct as well as a meta-isomer of NADH. Both structures have been probed positively in a 3D modeling analysis.

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Aromatic hydroxylation during the myeloperoxidase-oxidase oxidation of hydrazines

Cited by 18 publications

References 32 publications

Genetic polymorphisms involved in toxicant-metabolizing enzymes and the risk of chronic benzene poisoning in Chinese occupationally exposed populations

Genetic polymorphisms involved in toxicant-metabolizing enzymes and the risk of chronic benzene poisoning in Chinese occupationally exposed populations

Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention

Antitubercular Isoniazid and Drug Resistance of Mycobacterium tuberculosis — A Review

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