Oxidation of Phenols by Yeast

Hashimoto, Komei

doi:10.2323/jgam.16.1_1

Cited by 7 publications

(3 citation statements)

References 8 publications

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“…Chloroperoxidase (CPO) is a glycosylated haemoprotein secreted by the fungus Caldariomyces fumago [1,2]. In vivo, this enzyme is involved in the synthesis of caldariomycin, a halogenated compound with antimicrobial function [3].…”

Section: Introductionmentioning

confidence: 99%

“…Carbohydrate moieties are incorporated at N-and O-glycosylation sites. Di¡erent isozymes are found in the extracellular medium of C. fumago cultures [8,9], which are indicated to be glycosylation variants of the same polypeptide [2,7]. In the major CPO isozyme, the most heavily glycosylated, three N-and 11 O-glycosylation sites are occupied with a total of 21 sugar groups [10].…”

Section: Introductionmentioning

confidence: 99%

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C‐terminal propeptide of the Caldariomyces fumago chloroperoxidase: an intramolecular chaperone?

et al. 2001

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The Caldariomyces fumago chloroperoxidase (CPO) is synthesised as a 372-aa precursor which undergoes two proteolytic processing events: removal of a 21-aa N-terminal signal peptide and of a 52-aa C-terminal propeptide. The Aspergillus niger expression system developed for CPO was used to get insight into the function of this C-terminal propeptide. A. niger transformants expressing a CPO protein from which the C-terminal propeptide was deleted failed in producing any extracellular CPO activity, although the CPO polypeptide was synthesised. Expression of the full-length gene in an A. niger strain lacking the KEX2-like protease PclA also resulted in the production of CPO cross-reactive material into the culture medium, but no CPO activity. Based on these results, a function of the C-terminal propeptide in CPO maturation is indicated. ß

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

C‐terminal propeptide of the Caldariomyces fumago chloroperoxidase: an intramolecular chaperone?

et al. 2001

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“…The present author reported that the cells of a yeast strain isolated from the soil could not utilize p-cresol for growth but they could oxidize p-cresol after the cells were incubated with phenol (7).…”

Section: Discussionmentioning

confidence: 99%

Oxidation of Phenols by Yeast

Hashimoto

1973

J. Gen. Appl. Microbiol.

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(2) showed that when, cresols were metabolized by certain species of Pseudomonas, the benzene ring was cleaved by extra-diol type fission after cresols were oxidized to methylcatechols. Furthermore, FEIST and HEGEMAN (3) showed that the bacteria grown on phenol contained an enzyme which catalyzed the benzene ring cleavage by an extra-diol type fission, and that the bacteria grown on benzoate contained an enzyme which catalyzed the cleavage by an intra-diol type fission. CAIN et al. (4) studied the oxidation of phenols that were related to lignin by various strains of fungi and yeasts using whole cells and cell-free extracts.They showed that a strain of fungi possessing the ability to grow on catechol forms cis, cis-muconic acid from catechol and this result suggests that the strain has catechol 1, 2-oxygenase.NEUJAHR and VARGA (5, 6) demonstrated by use of Trichospoyon cutaneum that the cells grown on phenol 171

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Biotransformation and Detoxification of Environmental Pollutants with Aromatic Structures by Yeasts

Schlüter

Schauer

2017

Yeast Diversity in Human Welfare

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Oxidation of Phenols by Yeast

Cited by 7 publications

References 8 publications

C‐terminal propeptide of the Caldariomyces fumago chloroperoxidase: an intramolecular chaperone?

C‐terminal propeptide of the Caldariomyces fumago chloroperoxidase: an intramolecular chaperone?

Oxidation of Phenols by Yeast

Biotransformation and Detoxification of Environmental Pollutants with Aromatic Structures by Yeasts

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