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Literature summary 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)

EC Number Cloned (Comment) Organism
2.7.7.65 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

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

Metals/Ions

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

Organism

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.7.7.65 dimer
-
 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.7.7.65 diguanylate cyclase
-
 Escherichia coli
2.7.7.65 YdeH
-
 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.65 7.5
-
-
 Escherichia coli