Activation of ppGpp-3'-pyrophosphohydrolase by a supernatant factor and ATP.
作者： J. Sy
DOI: 10.1016/S0021-9258(19)70426-8
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摘要: Abstract The breakdown of guanosine 5'-diphosphate, 3'-diphosphate (ppGpp) into GDP and PPi is catalyzed by a Mn2+-dependent 3'-pyrophosphohydrolase, the translation product spoT gene. escherichia coli enzyme normally found to be associated with "crude" ribosome fraction. It reported here that 3'-pyrophosphohydrolase activity in this fraction activated ATP presence relatively heat-stable, low molecular weight, supernatant factor (BS100). This stimulation not due removal reaction products such as phosphorylation GTP or hydrolysis PPi. Hydrolysis probably required because neither adenosine 5'-(3-thio)triphosphate nor 5'-(beta, gamma-imido)triphosphate can substitute for ATP. Levallorphan, morphine analog, which had been shown inhibit vivo ppGpp degradation, inhibits specifically factor. possible relationship system energy-dependent control degradation discussed.
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