Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Lebbink, J.H.G.; Eggen, R.I.L.; Geerling, A.C.M.; Consalvi, V.; Chiaraluce, R.; Scandurra, R.; de Vos, W.M.
    Exchange of domains of glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus and the mesophilic bacterium Clostridium difficile: Effects on catalysis, thermoactivity and stability (1995), Protein Eng., 8, 1287-1294.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.1.4 expression in Escherichia coli, hybrid proteins containing the Pyrococcus furiosus glutamate and the Clostridium difficile cofactor binding domain with reduced substrate binding affinity Pyrococcus furiosus
1.4.1.4 expression in Escherichia coli, hybrid proteins containing the Pyrococcus furiosus glutamate and the Clostridium difficile cofactor binding domain with reduced substrate binding affinity Clostridioides difficile

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.1.4 L-glutamate + NADP+ + H2O Pyrococcus furiosus
-
 2-oxoglutarate + NADPH + NH3
-
 r
1.4.1.4 L-glutamate + NADP+ + H2O Clostridioides difficile
-
 2-oxoglutarate + NADPH + NH3
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.4 Clostridioides difficile
-
-
-
1.4.1.4 Pyrococcus furiosus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.4 L-glutamate + NADP+ + H2O
-
 Pyrococcus furiosus 2-oxoglutarate + NADPH + NH3
-
 r
1.4.1.4 L-glutamate + NADP+ + H2O
-
 Clostridioides difficile 2-oxoglutarate + NADPH + NH3
-
 r

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.4 NADP+
-
 Pyrococcus furiosus
1.4.1.4 NADP+
-
 Clostridioides difficile
1.4.1.4 NADPH
-
 Pyrococcus furiosus
1.4.1.4 NADPH
-
 Clostridioides difficile