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Literature summary for 2.7.7.65 extracted from

  • Zaehringer, F.; Massa, C.; Schirmer, T.
    Efficient enzymatic production of the bacterial second messenger c-di-GMP by the diguanylate cyclase YdeH from E. coli (2011), Appl. Biochem. Biotechnol., 163, 71-79.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli as a His-tagged fusion protein is established and allows production of 2.5 mg of pure c-di-GMP per milligram of YdeH with standard biochemical lab equipment Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information the reaction shows non-competitive product inhibition only at comparatively large c-di-GMP concentration Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Li+ activity reduced about 20% in 50 mM LiCl Escherichia coli
Na+ 50 mM NaCl is used Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP
-
Escherichia coli cyclic di-3',5'-guanylate + diphosphate
-
?

Subunits

Subunits Comment Organism
dimer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
diguanylate cyclase
-
Escherichia coli
YdeH
-
Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Escherichia coli