Oxidation of 3-hydroxyanthranilic acid to the phenoxazinone cinnabarinic acid by peroxyl radicals and by compound I of peroxidases or catalase

Christen, Stephan; Southwell-Keely, Peter T.; Stocker, Roland

doi:10.1021/bi00149a045

Cited by 39 publications

(40 citation statements)

References 39 publications

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“…The absorption maximum at 450 nm exhibited by samples from the P. cinnabarinus cultures was in good agreement with spectra reported previously for CA [3,4] as well as with the absorbance spectrum of CA chemically synthesized in our laboratory. TLC analysis of the culture samples found bands with Rf values identical with authentic CA (0.51 _+ 0.02).…”

Section: Resultssupporting

confidence: 91%

“…It seems highly likely that oxidative coupling of 3-HAA by laccase progresses along the same pathway that has been proposed for tyrosinase and peroxidase [3,4] (Fig. 6).…”

Section: Discussionmentioning

confidence: 62%

“…6. Hypothetical reaction mechanism for laccase-mediated conversion of 3-hydroxyanthranilic acid into cinnabarinic acid (adapted from [3,4]). …”

Section: Discussionmentioning

confidence: 99%

“…Conversion of 3-HAA into CA can proceed non-enzymatically through the action of active oxygen species and various transition metals [1,2], but it can also be mediated enzymatically. Thus, CA formation was catalyzed by compound I ofperoxidase or catalase as well as tyrosinase [3,4].…”

Section: Introductionmentioning

confidence: 99%

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Laccase‐mediated formation of the phenoxazinone derivative, cinnabarinic acid

et al. 1995

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The phenoxazinone chromophore occurs in a variety of biological systems, including numerous pigments and certain antibiotics. It also appears to form as part of a mechanism to protect mammalian tissue from oxidative damage. During cultivation of the basidiomycete, Pycnoporus cinnabarinus, a red pigment was observed to accumulate in the culture medium. It was identified as the phenoxazinone derivative, cinnabarinic acid (CA). Laccase was the predominant extracellular phenoloxidase activity in P. cinnabarinus cultures. In vitro studies showed that CA was formed after oxidation of the precursor, 3-hydroxyanthranilic acid (3-HAA), by laccases. Moreover, oxidative coupling of 3-HAA to form CA was also demonstrated for the mammalian counterpart of laccase, the blue copper oxidase, ceruloplasmin.

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Section: Resultssupporting

confidence: 91%

“…It seems highly likely that oxidative coupling of 3-HAA by laccase progresses along the same pathway that has been proposed for tyrosinase and peroxidase [3,4] (Fig. 6).…”

Section: Discussionmentioning

confidence: 62%

“…6. Hypothetical reaction mechanism for laccase-mediated conversion of 3-hydroxyanthranilic acid into cinnabarinic acid (adapted from [3,4]). …”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Laccase‐mediated formation of the phenoxazinone derivative, cinnabarinic acid

et al. 1995

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“…Secondly, this aminophenolic metabolite is a powerful antioxidant ( 17,46): it strongly inhibited LDL oxidation when added to both cell-free and cell-containing systems in the absence of IFN'y and at concentrations similar to those formed by IFN-ytreated mononuclear cells in vitro. Thirdly, incubation ofLDL and IFNy with PBMC or MDM under conditions that resulted in oxidative Trp degradation with concomitant formation of 3HAA, inhibited LDL oxidation to an extent similar to that observed with exogenously added 3HAA.…”

Section: Resultsmentioning

confidence: 99%

Inhibition by interferon-gamma of human mononuclear cell-mediated low density lipoprotein oxidation. Participation of tryptophan metabolism along the kynurenine pathway.

Christen¹,

Thomas²,

Garner³

et al. 1994

J. Clin. Invest.

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In this study we examined the potential inhibition by interferon-y (IFN'y) of the early stages of low density lipoprotein (LDL) oxidation mediated by human peripheral blood mononuclear cells (PBMC) and monocyte-derived macrophages (NMDMN) in Ham's F-10 medium supplemented with physiological amounts of L-tryptophan (Trp). We assessed LDL oxidation by measuring the consumption of LDL's major antioxidant (i.e., a-tocopherol) and targets for oxidation (cholesteryllinoleate and cholesterylarachidonate), together with the accumulation of cholesterylester hydroperoxides and the increase in relative electrophoretic mobility of the lipoprotein particle. Exposure of PBMC or MDM to IFNy induced the degradation of extracellular Trp with concomitant accumulation of kynurenine, anthranilic and 3-hydroxyanthranilic acid (3HAA) in the culture medium. Formation of 3HAA, but neither Trp degradation nor formation ofkynurenine and anthranilic acid, was inhibited by low amounts of diphenylene iodonium (DPI) in a concentration-dependent manner. In contrast to oxidative Trp metabolism, exposure of human PBMC or MDM to IFN-y failed to induce degradation ofarginine, and nitrite was not detected in the cell supernatant, indicating that nitric oxide synthase was not induced under these conditions. Incubation of LDL in Trpsupplemented F-10 medium resulted in a time-dependent oxidation of the lipoprotein that was accelerated in the presence of PBMC or MDM but inhibited strongly in the presence of both cells and IFNy, i.e., when Trp degradation and formation of 3HAA were induced. In contrast, when IFNy was added to PBMC or MDM in F-10 medium that was virtually devoid of Trp, inhibition of cell-accelerated LDL oxidation was not observed. Exogenous 3HAA added to PBMC or purified monocytes in the absence of IFNy also strongly and in a concentration-dependent manner inhibited LDL oxidation. Selective inhibition of IFNy-induced formation of 3HAA by DPI caused reversion of the inhibitory action of this cytokiine on both PBMC-and MDM-mediated LDL oxidation. These results show that IFN'y treatment of human PBMC or MDM in vitro attenuates the extent of LDL oxidation caused by these cells,

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Synthesis of cinnabarinic acid by metabolically engineered Pseudomonas chlororaphis GP72

Yue

Song

et al. 2019

Biotech & Bioengineering

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Cinnabarinic acid is a valuable phenoxazinone that has broad applications in the pharmaceutical, chemical, and dyeing industries. However, few studies have investigated the production of cinnabarinic acid or its derivatives using genetically engineered microorganisms. Herein, an efficient synthetic pathway of cinnabarinic acid was designed and constructed in Pseudomonas chlororaphis GP72 for the first tim, which was more straightforward and robust than the known eukaryotic biosynthetic pathways. First, we screened and identified trans‐2,3‐dihydro‐3‐hydroxyanthranilic acid (DHHA) dehydrogenases from Escherichia coli MG1655 (encoded by entA), Streptomyces sp. NRRL12068 (encoded by bomO) and Streptomyces chartreusis NRRL3882 (encoded by calB3) based on the structural similarity of the substrate and product, and the DHHA dehydrogenase encoded by calB3 was selected for the synthesis of cinnabarinic acid due to its high DHHA conversion rate. Subsequently, cinnabarinic acid was synthesized by the expression of the DHHA dehydrogenase CalB3 and the phenoxazinone synthase CotA in the DHHA‐producing strain P. chlororaphis GP72, resulting in a cinnabarinic acid titer of 20.3 mg/L at 48 hr. Further fermentation optimization by the addition of Cu2+, H2O2, and with adding glycerol increased cinnabarinic acid titer to 136.2 mg/L in shake flasks. The results indicate that P. chlororaphis GP72 may be engineered as a microbial cell factory to produce cinnabarinic acid or its derivatives from renewable bioresources.

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Oxidation of 3-hydroxyanthranilic acid to the phenoxazinone cinnabarinic acid by peroxyl radicals and by compound I of peroxidases or catalase

Cited by 39 publications

References 39 publications

Laccase‐mediated formation of the phenoxazinone derivative, cinnabarinic acid

Laccase‐mediated formation of the phenoxazinone derivative, cinnabarinic acid

Inhibition by interferon-gamma of human mononuclear cell-mediated low density lipoprotein oxidation. Participation of tryptophan metabolism along the kynurenine pathway.

Synthesis of cinnabarinic acid by metabolically engineered Pseudomonas chlororaphis GP72

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