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Literature summary extracted from

  • Bolivar, J.M.; Cava, F.; Mateo, C.; Rocha-Martin, J.; Guisan, J.M.; Berenguer, J.; Fernandez-Lafuente, R.
    Immobilization-stabilization of a new recombinant glutamate dehydrogenase from Thermus thermophilus (2008), Appl. Microbiol. Biotechnol., 80, 49-58.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.1.3 expressed in Escherichia coli BL21DE3 cells Thermus thermophilus

General Stability

EC Number General Stability Organism
1.4.1.3 glyoxyl agarose-GDH immobilization is more stable than CNBr-agarose preparations or than the soluble enzyme, glyoxyl agarose derivative, prepared at 4°C for 15 min, immobilizes around 50% of the enzyme, but the enzyme retains almost full activity after the immobilization Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.3 0.02
-
NAD+ in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C Thermus thermophilus
1.4.1.3 0.035
-
NADP+ in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C Thermus thermophilus
1.4.1.3 0.04
-
NADH in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C Thermus thermophilus
1.4.1.3 3
-
L-glutamate in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C Thermus thermophilus
1.4.1.3 3.5
-
2-oxoglutarate in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C Thermus thermophilus
1.4.1.3 10
-
NH3 in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C Thermus thermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.3 42000
-
SDS-PAGE Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.3 Thermus thermophilus
-
-
-
1.4.1.3 Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.3 heat denaturation at 70°C and Ni-agarose affinity column chromatography Thermus thermophilus

Storage Stability

EC Number Storage Stability Organism
1.4.1.3 25°C, soluble enzyme in the presence of 25% v/v acetone at pH 7, 1 week, no loss of activity Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.3 L-glutamate + H2O + NAD(P)+
-
Thermus thermophilus 2-oxoglutarate + NH3 + NAD(P)H
-
?
1.4.1.3 L-glutamate + H2O + NAD(P)+
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 2-oxoglutarate + NH3 + NAD(P)H
-
?

Subunits

EC Number Subunits Comment Organism
1.4.1.3 trimer analytical ultracentrifugation Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
1.4.1.3 dual-coenzyme specific glutamate dehydrogenase
-
Thermus thermophilus
1.4.1.3 GDH
-
Thermus thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.1.3 25 70 the thermostability of the enzyme at neutral pH is very high even at 70°C, but at acidic pH values, the dissociation of enzyme subunits produces the rapid enzyme inactivation even at 25°C, immobilized preparations, as well as the soluble enzyme, remain fully active after 24 h of incubation at 60°C and pH 7, the optimal glyoxyl agarose derivative obtained is fully stable at pH 4 and 25°C, retaining more than 90% of its activity after incubation at 45°C for 24 h at pH 4 and more than 75% of the activity after the same period at 50°C Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.3 9
-
immobilized enzyme, using NAD+ as a cofactor Thermus thermophilus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.4.1.3 4 7 the immobilized enzyme is very stable at pH 4, the enzyme activity does not decrease after 12 h at 45°C at pH 4, immobilized preparations, as well as the soluble enzyme, remain fully active after 24 h of incubation at 60°C and pH 7 Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.3 NAD+ activity with NAD+ is 3-5fold higher than using NADP+ Thermus thermophilus
1.4.1.3 NADP+ lower activity with NADP+ compared to NAD+ Thermus thermophilus