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Literature summary for 2.7.7.65 extracted from

  • Korovashkina, A.; Rymko, A.; Kvach, S.; Zinchenko, A.
    Enzymatic synthesis of c-di-GMP using inclusion bodies of Thermotoga maritima full-length diguanylate cyclase (2013), J. Biotechnol., 164, 276-280.
    View publication on PubMed
Search for more literature for 2.7.7.65

Cloned(Commentary)

Cloned (Comment) Organism
recombinantly expressed in Escherichia coli. Target protein is produced mainly in the form of inclusion bodies. Both native and mutant enzymes are not inhibited by the target product during conversion of 1 mM GTP into c-di-GMP Thermotoga maritima

Protein Variants

Protein Variants Comment Organism
R158A mutant shows increased enzymatic activity compared to wild-type, mutant shows 4fold lower expression level compared to wild-type which might be due to higher enzymatic activity of mutant R158A and its increased toxicity for cells Thermotoga maritima

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Mg2+ required, optimal activity at 2.5 mM MgCl2 Thermotoga maritima
NaCl optimal activity at 300-500 mM NaCl Thermotoga maritima

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
151
-
 pH 10, 60°C, mutant R158A Thermotoga maritima

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
DGC
-
 Thermotoga maritima
diguanylate cyclase
-
 Thermotoga maritima

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Thermotoga maritima

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
 Thermotoga maritima