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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Abbreviations
- UDP:
-
uridine 5′-diphosphate
References
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Pittet, JL., Létoublon, R., Frot-Coutaz, J. et al. Soluble uridine diphospho-D-glucose: mycosporin glucosyltransferase from spores of Ascochyta fabae Speg.. Planta 159, 159–164 (1983). https://doi.org/10.1007/BF00392987
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DOI: https://doi.org/10.1007/BF00392987