Effects of GTP,GDP[beta S] and glucose on adenylate cyclase activity of E. coli B.
Adenylate cyclase activity was measured in suspensions of E.coli B, rendered permeable with toluene. The enzyme was activated in a dose-dependent manner by GTP and by its non-hydrolysable analogue, GTP[gamma S]. In contrast, incubation with GDP[beta S], a non-phosphorylatable analogue of GDP, caused a dose-related inhibition of adenylate cyclase; this was partially overcome by addition of GTP. GTP did not relieve, and GDP[beta S] augmented, the non-competitive and dose-related inhibition of E.coli adenylate cyclase by glucose.
D000067956:Adenylyl Cyclase Inhibitors; D000262:Adenylyl Cyclases / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D004926:Escherichia coli / Q000201:enzymology*; D005947:Glucose / Q000494:pharmacology*; D006150:Guanine Nucleotides; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D006153:Guanosine Diphosphate / Q000031:analogs & derivatives* / Q000494:pharmacology; D006160:Guanosine Triphosphate / Q000031:analogs & derivatives / Q000494:pharmacology*; D013873:Thionucleotides / Q000494:pharmacology*; D014050:Toluene / Q000494:pharmacology
D000067956:Adenylyl Cyclase Inhibitors; D006150:Guanine Nucleotides; D013873:Thionucleotides; D006153:Guanosine Diphosphate; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D014050:Toluene; C023427:guanosine 5'-O-(2-thiodiphosphate); D006160:Guanosine Triphosphate; D000262:Adenylyl Cyclases; D005947:Glucose