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- W2024590930 abstract "Mycelium from cultures of the red polypore Pycnoporus coccineus (Fr.) Bond. and Sing, contains an enzyme which catalyzes the oxidative condensation of 2 molecules of 2-aminophenol to yield 2-amino-3H-isophenoxazin-3-one. Fractionation of the crude extract has given a preparation with an 893-fold increase in specific activity. The purified enzyme has a pH optimum in citrate-phosphate buffer of 5.0, and a temperature optimum of 55°. The K m value is 4.35 × 10 −4 M. FMN and Mn ++ ions were required for maximum activity. FAD also served as an electron acceptor. Of the metal ions tested only Mn ++ activated the reaction. Hg ++ and Fe ++ inhibited strongly. The course of the reaction when cofactors were added separately suggested that flavin mononucleotide is the initial electron acceptor and that Mn ++ ions are required for reoxidation of the flavin. The enzyme has narrow specificity, and does not catalyze the oxidation of 3-hydroxyanthranilic acid, 3-hydroxykynurenine, or pyrocatechol." @default.
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- W2024590930 date "1964-11-01" @default.
- W2024590930 modified "2023-09-27" @default.
- W2024590930 title "AN ISOPHENOXAZINE SYNTHASE FROM PYGNOPORUS COCCINEUS (FR.) BOND. AND SING." @default.
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- W2024590930 doi "https://doi.org/10.1139/o64-162" @default.
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