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- W1991485382 abstract "A threefold glucuronidation of luteolin terminates the biosynthesis of luteolin 7-O-[β-d-glucuronosyl(1→2)β-d-glucuronide] 4′-O-β-d-glucuronide, the major flavone of the mesophyll of 5-day-old rye primary leaves. The strictly sequential transfer of glucuronate is catalysed by three specific enzymes: UDP-glucuronate: luteolin 7-O-glucuronosyltransferase (LGT), UDP-glucuronate: luteolin 7-O-glucuronide-glucuronosyl-transferase (LMT) and UDP-glucuronate: luteolin 7-O-diglucuronide-glucuronosyltransferase (LDT). The three enzymes were separated on Ultrogel AcA-44 and DEAE-cellulose. The LGT was purified 170-fold and the LDT 23-fold, while the LMT was further chromatographed on hydroxylapatite, yielding a 99-fold purification. The Mrs were 34 000 (LGT), 37 000 (LMT) and 29 000 (LDT). The isoelectric points of LGT and LDT were identical at a pH of 4.75, and an IEP of 4.80 was found for LMT. The pH optima were at 6.5 (LGT) 6.5 and 8.5 (LMT), and at pH 7 (LDT). Temperature optima were 50° for LGT, 52° for LMT and 40° for LDT; the energies of activation were 50, 23 and 38 kJ/Mol, respectively. Each of the enzymes is highly specific for its natural substrate. Luteolin and UDP both had a strong inhibitory effect. For UDP, an uncompetitive inhibition was found, when the concentration of the glucuronate acceptor was varied. The LDT was not significantly influenced by the divalent cations Ca2+ and Mg2+, whereas LGT and LMT were stimulated by Mg2+ ions (LGT: ca 20% up to 1 mM; LMT: up to 50% at 0.75 to 1 mM) and by Ca2+-ions (LGT: ca 25% at 0.25 mM; LMT: ca 20% at 0.5 mM). The reactions are irreversible under the standard assay conditions." @default.
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- W1991485382 date "1988-01-01" @default.
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- W1991485382 title "Three specific UDP-glucuronate: Flavone-glucuronosyl-transferases from primary leaves of Secale cereale" @default.
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- W1991485382 doi "https://doi.org/10.1016/0031-9422(88)80175-4" @default.
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