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Membrane-bound chitin synthase from FuscUium graminearum A315 had a pH optimum of 6.5, an apparent temperature optimum of 30 "C and an apparent K,,, for UDP-N-acetylglucosamine (UDP-GlcNAc) of 2.5 mM. Digitonin-solubilized chitin synthase had a lower (about 25% of the original activity) and more variable activity than the membrane-bound chitin synthase from which it was prepared. The activity of solubilized chitin synthase was stabilized by incorporating Allosamidin (a chitinase inhibitor) into the reaction mixture, and an approximately 3.6-fold increase in activity was observed when the reaction mixture contained dimyristoylphosphatidylcholine. Concentrations of the organophosphorus fungicide edifenphos (Hinosan) up to 25 p~ had no effect on the in vitro activity of membrane-bound chitin synthase, but between 25 and 145 p~, chitin synthase activity decreased with increase in fungicide concentration. Edifenphos caused non-competitive inhibition of chitin synthase activity with an apparent Ki of 50 PM. Membrane-bound chitin synthase preparations from cultures of F. graminearurn grown in 250 pM-edifenphos had a much lower in vitro activity than preparations from cultures grown in the absence of the fungicide. Pre-growth of F. grdnearum in 250 p~ (but not 80 p~) edifenphos also caused a reduction in incorporation of (3H)GlcNAc into chitin in uivo (washed biomass was incubated in (3H)GlcNAc-containing medium lacking fungicide).

Chitin synthesis in Fusarium graminearum and its inhibition by edifenphos (Hinosan)