Acid phosphatase Neurospora crassa

An acid phosphatase from the mycelium of the fungus Neurospora crassa has been purified 1400-fold with a 40% recovery. The pH maximum is 5.6 with j3-glycerophosphate as substrate. Fluoride and D-(-f-)-tartrate are competitive inhibitors so that this enzyme fits into a rather general pattern for others of its type which have been described (116). 

D-Glucosamine 6-phosphate is hydrolyzed by the D-glucose-6-phosphatase of rat-liver mitochondria. The rate of this hydrolysis is about 8 % of that of D-glucose 6-phosphate hydrolysis. A phosphatase which preferentially catalyzes the hydrolysis of D-glucosamine 6-phosphate has been prepared from Neurospora crassa. This enzyme is not stimulated by magnesium ions and has an optimum activity between pH 6 and 7.5. It appears to be distinct from acid, alkaline, and other specific phosphatases. 

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