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Literature summary for 3.1.7.2 extracted from

  • Xiao, H.; Kalman, M.; Ikehara, K.; Zemel, S.; Glaser, G.; Cashel, M.
    Residual guanosine 3',5'-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations (1991), J. Biol. Chem., 266, 5980-5990.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
preparation of mutants with null alleles at both, spoT and relA Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ppGpp + H2O Escherichia coli the enzyme may be a bifunctional protein catalyzing either ppGpp synthesis or degradation ppG + diphosphate
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ppGpp + H2O i.e. guanosine-3',5'-bis(diphosphate) Escherichia coli ppG + diphosphate i.e. guanosine 5'-diphosphate ?
ppGpp + H2O the enzyme may be a bifunctional protein catalyzing either ppGpp synthesis or degradation Escherichia coli ppG + diphosphate
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?