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PMID: 4372621 Published · ppublish English Journal Article

Reversibility of the pyrophosphoryl transfer from ATP to GTP by Escherichia coli stringent factor.

Sy J

Abstract

The stringent factor-catalyzed, ribosome-dependent synthesis of guanosine polyphosphates is found to be reversible. The reverse reaction specifically requires 5'-AMP as the pyrophosphoryl acceptor, and guanosine 5'-triphosphate-3'-diphosphate is preferentially utilized as the pyrophosphoryl donor. The primary products of the reaction are GTP and ATP. The reverse reaction is strongly inhibited by the antibiotics thiostrepton and tetracycline, and by ATP and beta-gamma-methylene-adenosine-triphosphate, but not by ADP, GTP, and GDP. The reverse reaction occurs under conditions for nonribosomal synthesis. The overall reaction for stringent factor-catalyzed guanosine polyphosphate formation may thus be formulated: (p)pp5'G + ppp5'A right harpoon over left harpoon (p)pp5'G3'pp + p5'A.

MeSH Terms
Adenosine Diphosphate/pharmacology Adenosine Monophosphate/metabolism Adenosine Triphosphate/analogs & derivatives,pharmacology Anti-Bacterial Agents/pharmacology Chromatography, DEAE-Cellulose Escherichia coli/enzymology Guanine Nucleotides/metabolism,pharmacology Guanosine Triphosphate/analogs & derivatives,metabolism,pharmacology Peptides/pharmacology Phosphoric Acids Phosphotransferases/metabolism Tetracycline/pharmacology
Chemicals
Anti-Bacterial Agents Guanine Nucleotides Peptides Phosphoric Acids Adenosine Monophosphate Adenosine Diphosphate Guanosine Triphosphate Adenosine Triphosphate Phosphotransferases Tetracycline
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Sy J
References (10)
10 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1974-09-00
Pages
3470-3
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC433795
Subset
IM
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