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Soluble uridine diphospho-D-glucose: mycosporin glucosyltransferase from spores of Ascochyta fabae Speg. |
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| Authors: | Jean-Louis Pittet Robert Létoublon Jacques Frot-Coutaz Noël Arpin |
| Affiliation: | 1. Départment de Biologie Végétale, Université C. Bernard, Lyon I, 43 Boulevard du 11 Novembre 1918, F-69622, Villeurbanne Cedex, France 2. LBTM, Université C. Bernard, Lyon I, 43 Boulevard du 11 Novembre 1918, F-69622, Villeurbanne Cedex, France |
| Abstract: | The enzyme properties of a soluble uridine 5′-diphosphate (UDP) glucose: mycosporin-2 glucosyltransferase from spores of Ascochyta fabae 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 (Mn2+ being more efficient than Ca2+ or Mg2+). The reaction was not reversible in presence of large amounts of UDP. |
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