Characterization and metabolism of cyclic guanosine 3'5'-monophosphate in Mycobacterium smegmatis.
Cyclic guanosine 3'5'-monophosphate was isolated and purified from Mycobacterium smegmatis TMC 1515 using ion exchange chromatography. It was characterized by thin layer chromatography and radioimmunoassay. Guanylate cyclase and cGMP phosphodiesterase were detected in the cytosolic and particulate (37,000 X g pellet) fractions respectively. On the basis of our observations, cGMP appears to play a dual role (i) at the time of induction of cell proliferation and (ii) protects the bacteria against unfavourable surroundings during stationary phase of the growth. This is the first report demonstrating presence of cGMP, guanylate cyclase and cGMP phosphodiesterase in mycobacteria.
D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000302:isolation & purification; D002852:Chromatography, Ion Exchange; D006152:Cyclic GMP / Q000378:metabolism*; D006162:Guanylate Cyclase / Q000302:isolation & purification; D007700:Kinetics; D009161:Mycobacterium / Q000201:enzymology / Q000254:growth & development / Q000378:metabolism*
D015106:3',5'-Cyclic-GMP Phosphodiesterases; D006162:Guanylate Cyclase; D006152:Cyclic GMP