PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30590153-7 2019 The hotspot-associated variations, which decreased cooperativity, also increased the half-maximal inhibitory concentrations of the competitive GCK inhibitor, N-acetylglucosamine. Acetylglucosamine 158-177 glucokinase Homo sapiens 143-146 2210070-4 1990 CHX-induced inactivation of glucokinase was blocked by the presence of its substrates (glucose and mannose) and an inhibitor (N-acetylglucosamine), all of which also protected against the inhibitory effect of the drug on glucose-induced insulin secretion. Acetylglucosamine 126-145 glucokinase Homo sapiens 28-39 3207996-12 1988 Only glucose derivatives with a sufficiently bulky substituent in position C-2, such as the glucokinase substrates glucose and mannose and the inhibitors mannoheptulose, glucosamine, and N-acetylglucosamine, protected glucokinase against inhibition by alloxan by binding to the active site of the enzyme. Acetylglucosamine 187-206 glucokinase Homo sapiens 218-229 6257679-7 1981 When the phosphorylation of hexoses was blocked by the addition of N-acetylglucosamine to the culture medium, an intermediate level of glucokinase activity was observed in response to insulin. Acetylglucosamine 67-86 glucokinase Homo sapiens 135-146 11076949-7 2001 We show by computer simulation that such a model can account for the kinetic properties of glucokinase, including the differential ability of mannoheptulose and N-acetylglucosamine to suppress cooperativity (Agius, L., and Stubbs, M. (2000) Biochem. Acetylglucosamine 161-180 glucokinase Homo sapiens 91-102