[Guanylate cyclase in E. coli. III. Purification and possible physiological role of GTPase].
A phosphohydrolase with a preferential activity for GTP has been isolated and partially purified from E. coli extracts. The enzyme purification has been achieved through precipitation by ammonium sulfate and chromatography on DEAE-cellulose, DEAE-Sephadex, Ultragel and a second DEAE-cellulose column. The phosphohydrolase activity is poly (C) dependent. The chromatographic analysis on PEI-cellulose has shown that the main product of GTP hydrolysis is GDP. The possibility that the enzyme partially purified in this work has an important role in the control of GTP availability as substrate for guanylate cyclase into the cells has been discussed.
D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D004926:Escherichia coli / Q000201:enzymology*; D020558:GTP Phosphohydrolases / Q000302:isolation & purification / Q000378:metabolism*; D006162:Guanylate Cyclase / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D013379:Substrate Specificity
D010744:Phosphoric Monoester Hydrolases; D020558:GTP Phosphohydrolases; D006162:Guanylate Cyclase
Guanylate cyclase chez E. coli. III. Purification et rôle physiologique possible de la GTPase.