ISSN:
1432-2048
Schlagwort(e):
UDP-glucose
;
Glucosyltransferase
;
Cyanidin
;
Anthocyanidin
;
Flavonol
;
Haplopappus
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
Notizen:
Abstract From cell cultures of Haplopappus gracilis, an enzyme, catalyzing the glucosylation of cyanidin at the 3 position using uridine diphosphate-D-glucose (UDPG) as glucosyl-donor, has been isolated and purified 50-fold. The enzyme was not specific for cyanidin alone, but also glucosylated other anthocyanidins and flavonols in position 3. However, apigenin, luteolin, naringenin and dihydroquercetin were not glucosylated. The reaction has an optimum pH of approximately 8, and the apparent K m values for UDPG and cyanidin were 0.5 and 0.33 mM respectively. The enzyme reaction is strongly inhibited by cyanidin (above 0.25 mM).
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00386004
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