The enzymes of N-acetyl-D-glucosamine (GlcNAc) metabolism, GlcNAc-6-phosphate deacetylase and GlcN-6-phosphate deaminase were found to be inducible in Candida albicans. The pattern of induction for these enzymes was the same under conditions of germ-tube formation (37 degrees C) and where yeast cells metabolized GlcNAc with no change in morphology (28 degrees C); this indicates that these enzymes are not control points in the dimorphic development of C. albicans. During induction there was a 40-and 25-fold increase in specific activity for the deacetylase and the deaminase, respectively, and the maximum specific activity correspond to the time when all the GlcNAc had been metabolized. The presence of lomofungin (an inhibitor of transcription) or trichodermin (an inhibitor of translation) in cell suspensions of C. albicans containing GlcNAc prevented the increase in specific activity of these enzymes. 2-Deoxyglucose inhibited germ-tube formation, partially inhibited the induction of the deacetylase (43%) and the deaminase (60%), but did not affect the growth of C. albicans on either Glc or GlcNAc. GlcN-6-phosphate was a competitive inhibitor of the deacetylase with a Ki of 1.4 mM while the other product of the reaction, acetate, did not inhibit the enzyme. The Km value for GlcN-6-phosphate on GlcN-6-phosphate deaminase was 0.24 mM. Incubation of starved yeast cells with GlcNAc produced a four-fold increase in the specific activity of UDP-GlcNAc-pyrophosphorylase at either 28 degrees C or 37 degrees C.