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- W1984579119 abstract "The aerobic degradation of 5,6,7,8-tetrahydrobiopterin at neutral pH is catalysed by peroxidase (EC 1.11.1.7) and provides quinonoid 7,8-dihydro(6H)biopterin which readily loses the side chain to yield 7,8-dihydro(3H)pterin. The latter is in equilibrium with trace amounts of 6-hydroxy-5,6,7,8-tetrahydropterin (covalent hydrate) Which is irreversibly oxidised to quinonoid 6-hydroxy-7, 8-dihydro(6H)pterin, and this finally rearranges to 7,8-dihydroxanthopterin. Spectroscopic evidence (ultraviolet, 1H NMR and 13C NMR) is presented for the reversible addition of water across the 5,6-double bond of 7,8-dihydro(3H)pterin. The intermediate quinonoid 6-hydroxy-7,8-dihydro(6H)pterin is a good substrate for dihydropteridine reductase (EC 1.6.99.7) with a Km of 16.3 μM and kcat of 22.5s−1. The rate of aerobic degradation (oxidation and loss of the side chain) of natural (6R)-5,6,7,8-tetrahydrobiopterin is several times slower than the rate for the unnatural (6S) isomer. By using a modified assay procedure the kinetic parameters for dihydropteridine reductase are as follows: with (6R)-7,8-dihydro(6H)biopterin Km= 1.3μM and kcat= 22.8s−1; with (6S)-7,8-dihydro(6H)biopterin Km= 13.5μM and kcat= 51.6s−1; and with (6RS)-7,8-dihydro(6H)neopterin km= 19.2μM and kcat= 116s−1." @default.
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- W1984579119 date "1983-10-01" @default.
- W1984579119 modified "2023-10-16" @default.
- W1984579119 title "Peroxidase catalysed aerobic degradation of 5,6,7,8-tetrahydrobiopterin at physiological pH" @default.
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- W1984579119 doi "https://doi.org/10.1111/j.1432-1033.1983.tb07666.x" @default.
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