Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

Degradation of guanosine tetraphosphate (ppGpp) involves an enzyme associated with the ribosomal fraction from spoT+ strains of Escherichia coli. Double-label experiments with pp[3h]gpp, pp[3H]Gpp, or pp[3H]Gpp as substrate strongly suggest that ppG is the degradation product and that the enzyme releases two phosphates coordinately from the 3' position of ppGpp. In the absence of pppA this reaction proceeds in an uncoupled fashion, yielding ppG and PPi, but in the presence of pppA the decay is considerably enhanced and a pppA-ppi exchange reaction occurs in which the 3'-pyrophosphoryl group of ppGpp displaces the gamma and beta phosphates of pppA. Sodium PPi at 4 m7 inhibits decay of ppGpp regardless of whether or not pppA is present.

Bibliography

Heinemeyer, E. A., & Richter, D. (1978). Mechanism of the in vitro breakdown of guanosine 5’-diphosphate 3’-diphosphate in Escherichia coli. Proceedings of the National Academy of Sciences, 75(9), 4180–4183.

Authors 2
  1. E A Heinemeyer (first)
  2. D Richter (additional)
References 0 Referenced 38

None

Dates
Type When
Created 19 years, 3 months ago (May 31, 2006, 3:47 a.m.)
Deposited 3 years, 4 months ago (April 13, 2022, 10:58 a.m.)
Indexed 1 year ago (Aug. 7, 2024, 3:04 a.m.)
Issued 47 years ago (Sept. 1, 1978)
Published 47 years ago (Sept. 1, 1978)
Published Online 47 years ago (Sept. 1, 1978)
Published Print 47 years ago (Sept. 1, 1978)
Funders 0

None

@article{Heinemeyer_1978, title={Mechanism of the in vitro breakdown of guanosine 5’-diphosphate 3’-diphosphate in Escherichia coli.}, volume={75}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.75.9.4180}, DOI={10.1073/pnas.75.9.4180}, number={9}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Heinemeyer, E A and Richter, D}, year={1978}, month=sep, pages={4180–4183} }