Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cu,Zn.superoxide dismutase (SOD) enhanced the toxicity of 3-hydroxyanthranilic acid (3-HAT) to Salmonella typhimurium strain TA 102, evaluated as ability to form colonies. MnSOD showed the same effect. Inactivated Cu.ZnSOD had no effect. SODs accelerated the oxidation of 3-HAT, but inactivated Cu.ZnSOD caused little acceleration. It is proposed that the acceleration of 3-HAT oxidation leads to the enhancement of the 3-HAT toxicity. Catalase protected the bacteria from the toxicity of 3-HAT enhanced by Cu,ZnSOD, indicating that hydrogen peroxide generated in the oxidation of 3-HAT is involved in the toxicity. SODs accelerate the oxidation of 3-HAT and generate more hydrogen peroxide, that causes the enhancement of the 3-HAT toxicity to the bacteria. However, hydrogen peroxide alone was not so toxic. Hydrogen peroxide with 3-HAT was more toxic to the bacteria.
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PMID:Superoxide dismutase enhances the toxicity of 3-hydroxyanthranilic acid to bacteria. 206 Aug 64

The autoxidation of 3-hydroxyanthranilate to cinnabarinate at 37 degrees C and at pH 7.4 is hastened by superoxide dismutase (SOD). The Cu,Zn-containing enzyme from bovine erythrocytes and the Mn-containing enzyme from Escherichia coli were equally effective in this regard; whereas the H2O2-inactivated Cu,Zn enzyme was ineffective. Catalase appears to augment the effect of superoxide dismutase, because it prevents the bleaching of cinnabarinate by H2O2. It follows that O2-, which is a product of the autoxidation, slows the net autoxidation by engaging in back reactions and that SOD increases the rate of autoxidation by removal of O2- and thus by prevention of these back reactions.
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PMID:Superoxide dismutases enhance the rate of autoxidation of 3-hydroxyanthranilic acid. 240 53

The oxidative reactivities of four tryptophan metabolites in the kynurenine pathway were examined as a potential mechanism for their reported neurotoxicities and carcinogenicities. Neither quinolinic acid, a neurotoxin, nor its monocarboxylic analogue, picolinic acid, auto-oxidized over a wide pH range. However, 3-hydroxyanthranilic acid (3-HAT), a carcinogen, readily auto-oxidized and the reaction rate increased exponentially with increasing pH. 3-HAT auto-oxidation likely involves two steps: auto-oxidation of 3-HAT to the semiquinoneimine (anthranilyl radical) which oxidizes to the quinoneimine, followed by condensation and oxidation reactions to yield a second carcinogen, cinnabarinic acid. 3-HAT auto-oxidation to cinnabarinate required molecular oxygen and generated superoxide radicals and H2O2. Superoxide dismutase (SOD) accelerated 3-HAT auto-oxidation 4-fold, probably by preventing back reactions between superoxide and either the anthranilyl radical or the quinoneimine formed during the initial step of auto-oxidation. Catalase did not accelerate 3-HAT auto-oxidation, but it did prevent destruction of cinnabarinate by H2O2. Interconversion between oxyhemoglobin and methemoglobin occurred during 3-HAT auto-oxidation, although neither form of hemoglobin altered rates of 3-HAT auto-oxidation. Mn2+, Mn3+ and Fe3+-EDTA did not directly catalyze cinnabarinate formation in the absence of O2, but they did accelerate cinnabarinate formation under aerobic conditions.
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PMID:Oxidative reactivity of the tryptophan metabolites 3-hydroxyanthranilate, cinnabarinate, quinolinate and picolinate. 294 52

The formation of cinnabarinate in the presence of manganese ions and catalase was investigated spectrophotometrically. The absorption peak of cinnabarinate at 460 nm appeared only in a reaction system containing manganese ions and catalase. If catalase was omitted, a new absorption peak at 360 nm was observed while the absorption peak of cinnabarinate reached a plateau. Furthermore, in the presence of hydrogen peroxide, the absorption spectrum of cinnabarinate changed; catalase suppressed this absorption change. We conclude that in the course of cinnabarinate formation in the presence of manganese ions hydrogen peroxide is produced, which decomposes cinnabarinate. Catalase prevents the accumulation of hydrogen peroxide, which results in the steady increase of cinnabarinate. Cinnabarinate formation by manganese ions shows an initial lag phase. This lag phase disappeared by preincubating 3-hydroxyanthranilate under aerobic conditions. Incubation of 3-hydroxyanthranilate resulted in the generation of superoxide anions. When both manganese ions and superoxide anions were present, the lag phase of cinnabarinate formation disappeared. In the process of cinnabarinate formation, manganese ions serve to dismutate superoxide anions, as does superoxide dismutase; manganese (II) ions were oxidized to manganese (III) ions by superoxide anions. From these results we have proposed a mechanism of cinnabarinate formation catalysed by manganese ions.
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PMID:Cinnabarinate formation in malpighian tubules of the silkworm. Bombyx mori: reaction mechanism of cinnabarinate formation in the presence of catalase and manganese ions. 666

Accumulation of L-kynurenine and 3-hydroxyanthranilic acid (3HAA) occurs in the monocyte-derived cells following immune stimulation, and may derive from L-tryptophan following induction of indoleamine-2,3-dioxygenase. In the present study, we evaluate the possibility that 3HAA acts as an endogenous inducer of monocyte/macrophage apoptosis. Supplementation with 200 microM of 3HAA, but not other L-tryptophan metabolites tested, significantly increased the number of apoptotic cells in both THP-1 and U937 cells. Catalase, superoxide dismutase and manganese ions markedly enhanced apoptosis in the presence of 3HAA in these cells. The present results suggest that 3HAA induces the macrophage/monocyte apoptosis under certain conditions, which may be relevant to pathophysiology of inflammatory conditions.
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PMID:L-tryptophan-kynurenine pathway metabolite 3-hydroxyanthranilic acid induces apoptosis in macrophage-derived cells under pathophysiological conditions. 1072 Nov