An alkaline phosphomonoesterase from Neurospora crassa

An alkaline phosphomonoesterase was purified 40-fold from mycelium of Neurospora crassa. The enzyme had a pH maximum of 8.9-9.0 with [beta]-glucerol phosphate as substrate and exhibited maximal activity in the presnece of Mg2+. The enzyme was nearly completely resolved with respect to its Mg2+ requirement and was very sensitive to inhibition with Be2+. The substrate specificity of the enzyme was studied using 21 compounds and the properties of the enzyme were compared with those of the acid phosphomonoesterase previously isolated from the same organism.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/32344/1/0000414.pd