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Literature summary extracted from

  • Bolivar, J.; Mateo, C.; Rocha-Martin, J.; Cava, F.; Berenguer, J.; Fernandez-Lafuente, R.; Guisan, J.
    The adsorption of multimeric enzymes on very lowly activated supports involves more enzyme subunits: Stabilization of a glutamate dehydrogenase from Thermus thermophilus by immobilization on heterofunctional supports (2009), Enzyme Microb. Technol., 44, 139-144.
No PubMed abstract available

Application

EC Number Application Comment Organism
1.4.1.2 biotechnology method describes immobilization of enzymes by the maximum amount of subunits and rigidification of the enzyme subunits involved in the immobilization Thermus thermophilus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.1.2 overexpressed in Escherichia coli Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.2 Thermus thermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.2 GDH is readily adsorbed on highly activated anionic exchangers (HAAE), but hardly adsorbed on lowly activated supports (LAAE) or on highly activated epoxy supports. Using amino-epoxy supports, GDH immobilizes on HAAE-epoxy and more slowly on LAAE-epoxy supports. Both immobilized biocatalysts are incubated at pH 10 for different times to increase the multipoint covalent attachment. Lowly activated anionic exchangers-epoxy-GDH is stable at pH 4 and 25°C, the enzyme stability does not depend on the enzyme concentration and does not release any subunit to the supernatant, in opposition to the results obtained using HAAE-epoxy supports Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.2 L-glutamate + H2O + NAD+
-
 Thermus thermophilus 2-oxoglutarate + NH3 + NADH
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.1.2 homotrimer method not specified Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
1.4.1.2 GDH
-
 Thermus thermophilus
1.4.1.2 glutamate dehydrogenase
-
 Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.1.2 25
-
 lowly activated anionic exchangers-epoxy-GDH is stable at pH 4 and 25°C Thermus thermophilus
1.4.1.2 66
-
 assay at Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.2 4
-
 lowly activated anionic exchangers-epoxy-GDH is stable at pH 4 and 25°C Thermus thermophilus
1.4.1.2 8
-
 assay at Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.2 NAD+
-
 Thermus thermophilus