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Literature summary extracted from

  • Heinemeyer, E.A.; Richter, D.
    Characterization of the guanosine 5-triphosphate 3-diphosphate and guanosine 5-diphosphate 3-diphosphate degradation reaction catalyzed by a specific pyrophosphorylase from Escherichia coli (1978), Biochemistry, 17, 5368-5372.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.7.2 LiCl
-
Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.7.2 K+ 200-300 mM required for optimal activity Escherichia coli
3.1.7.2 Mn2+ activation Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.7.2 ppGpp + H2O Escherichia coli
-
ppG + diphosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.7.2 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.7.2 ppGpp + H2O
-
Escherichia coli ppG + diphosphate
-
?
3.1.7.2 ppGpp + H2O i.e. guanosine-3',5'-bis(diphosphate) Escherichia coli ppG + diphosphate i.e. guanosine 5'-diphosphate ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.7.2 37
-
-
Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.7.2 7.5 8
-
Escherichia coli