PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10700381-4 2000 Controlled proteolysis of wild-type glucokinase by proteinase K revealed that the SH group oxidizing agent alloxan can induce the formation of multiple intramolecular disulfide bridges corresponding to a double-band pattern of glucokinase protein in nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Alloxan 107-114 glucokinase Homo sapiens 36-47 10700381-4 2000 Controlled proteolysis of wild-type glucokinase by proteinase K revealed that the SH group oxidizing agent alloxan can induce the formation of multiple intramolecular disulfide bridges corresponding to a double-band pattern of glucokinase protein in nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Alloxan 107-114 glucokinase Homo sapiens 227-238 3419426-0 1988 Inhibition of glucokinase by alloxan through interaction with SH groups in the sugar-binding site of the enzyme. Alloxan 29-36 glucokinase Homo sapiens 14-25 9048894-7 1997 The inhibition of glucokinase enzyme activity was reversed by dithiothreitol with an EC50 value of 9 microM for alloxan and of 50 microM for ninhydrin. Alloxan 112-119 glucokinase Homo sapiens 18-29 9048894-9 1997 The enzyme inhibition by alloxan was accompanied by a change in the electrophoretic mobility with a second lower molecular 49 kDa glucokinase band which can be interpreted as a compact glucokinase molecule locked by disulfide bonds. Alloxan 25-32 glucokinase Homo sapiens 130-141 9048894-9 1997 The enzyme inhibition by alloxan was accompanied by a change in the electrophoretic mobility with a second lower molecular 49 kDa glucokinase band which can be interpreted as a compact glucokinase molecule locked by disulfide bonds. Alloxan 25-32 glucokinase Homo sapiens 185-196 3207996-0 1988 Structural requirements of alloxan and ninhydrin for glucokinase inhibition and of glucose for protection against inhibition. Alloxan 27-34 glucokinase Homo sapiens 53-64 3207996-4 1988 With a half-maximal inhibitory concentration of 5 microM, alloxan was the most potent pyrimidine derivative inhibitor of glucokinase. Alloxan 58-65 glucokinase Homo sapiens 121-132 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. Alloxan 252-259 glucokinase Homo sapiens 92-103 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. Alloxan 252-259 glucokinase Homo sapiens 218-229 3207996-15 1988 DTT (dithiothreitol) protected glucokinase against inhibition by alloxan and reversed the inhibition of the enzyme induced by alloxan. Alloxan 65-72 glucokinase Homo sapiens 31-42 3207996-16 1988 Thus the mechanism of glucokinase inhibition by alloxan and other inhibitors, such as uramil and ninhydrin, is an oxidation of functionally essential SH groups of the enzyme, where the most reactive keto group of the inhibitor acts as the hydrogen acceptor. Alloxan 48-55 glucokinase Homo sapiens 22-33 3419426-2 1988 The dithiol 1,4-dithiothreitol (1,4-DTT) protected against and reversed the inhibition of glucokinase by alloxan. Alloxan 105-112 glucokinase Homo sapiens 90-101 3419426-4 1988 Only 1,3-dimercaptopropane, 1,4-dimercaptobutane, 1,4-dithioerythritol, and 1,4-DTT, with intermediate spacing between the SH groups, reversed the inhibition of glucokinase induced by alloxan. Alloxan 184-191 glucokinase Homo sapiens 161-172 3419426-8 1988 Like alloxan, other dithiol reagents such as ninhydrin, N-ethylmaleimide, and maleimide inhibited glucokinase. Alloxan 5-12 glucokinase Homo sapiens 98-109