✦ LIBER ✦
Soluble uridine diphospho-D-glucose: mycosporin glucosyltransferase from spores ofAscochyta fabaeSpeg.
✍ Scribed by Jean-Louis Pittet; Robert Létoublon; Jacques Frot-Coutaz; Noël Arpin
- Book ID
- 104753367
- Publisher
- Springer-Verlag
- Year
- 1983
- Tongue
- English
- Weight
- 508 KB
- Volume
- 159
- Category
- Article
- ISSN
- 0032-0935
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✦ Synopsis
The enzyme properties of a soluble uridine 5'-diphosphate (UDP) glucose: mycosporin-2 glucosyltransferase from spores of Ascochytafabae Speg. (Fungi imperfecti) were studied. The optimal conditions for the glucose transfer from UDP-glucose to the mycosporin-2 (the amide form being the best acceptor) were determined; for maximal activity the glucosyltransferase requires a pH of about 8.5 and the presence of divalent cations (Mn 2+ being more efficient than Ca z+ or Mg2+). The reaction was not reversible in presence of large amounts of UDP.