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1.4.1.3: glutamate dehydrogenase [NAD(P)+]

This is an abbreviated version!
For detailed information about glutamate dehydrogenase [NAD(P)+], go to the full flat file.

Reaction

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L-glutamate
+
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H2O
+
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NAD(P)+
=
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2-oxoglutarate
+
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NH3
+
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NAD(P)H
+
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H+

Synonyms

At5g07440, At5g18170, dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)), dual-coenzyme specific glutamate dehydrogenase, GDH, gdh-1, GDH1, GDH2, GDH3, GdhA, gdhA_1, GDHB, GDHII, GLDH, GLUD1, GLUD2, GluDH, glutamate dehydrogenase, glutamate dehydrogenase 1, glutamate dehydrogenase 2, glutamic acid dehydrogenase, glutamic dehydrogenase, hGDH1, hGDH2, hGLUD1, hGLUD2, housekeeping glutamate dehydrogenase, L-glutamate dehydrogenase, L-glutamic acid dehydrogenase, Legdh1, Membrane protein 50, MP50, NAD(P)+-dependent glutamate dehydrogenase, NAD(P)-dependent GDH, NAD(P)-dependent glutamate dehydrogenase, NAD(P)-glutamate dehydrogenase, NAD(P)H-dependent glutamate dehydrogenase, NAD(P)H-utilizing glutamate dehydrogenase, NADH-GDH, NADH-glutamate dehydrogenase, TTC1211, TTC1212, TtGDH

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.1 With NAD+ or NADP+ as acceptor
                EC 1.4.1.31.4.1.3 glutamate dehydrogenase [NAD(P)+]

Temperature Stability

Temperature Stability on EC 1.4.1.3 - glutamate dehydrogenase [NAD(P)+]

for references in articles please use BRENDA:EC1.4.1.3

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
complete loss of activity after 5 h, 20% glycerol protects from inactivation
100 - 105
-
1 mg/ml enzyme, half-life of 10.5 h at 100┬░C, 3.5 h at 105┬░C, and 20 h at 90┬░C, thermal denaturation at 113┬░C
113
-
Tm-value = 113┬░C
118
-
thermal denaturation starts at 110┬░C and is comp1eted at 118┬░C
120
-
half-life: 2.5 min
25
-
48 h, protein concentration of 0.2 mg/ml, stable
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
37
-
complete loss of activity
42
-
mitochondrial enzyme loses 80% activity after 20 min, enzyme from endoplasmic reticulum loses 20% activity
47.5
-
GDH2 has a half-life of 38 min at 47.5┬░C, GDH1 has a half-life of 348 min at 47.5┬░C, high concentrations of phosphate (300 mM) have a protective effect on the thermal denaturation of both wild type hGDHs, this effect being more pronounced for GDH2
5
-
moderately stable above
55
-
short periods
60
-
48 h, protein concentration of 0.2 mg/ml, 20% loss of activity
66
-
10 min, 50% loss of activity
70 - 100
-
no loss in activity after 1 h at 90┬░C, 20% residual activity after 1 h at 100┬░C
74
-
10 min, complete loss of activity
85
-
half-life: 2 h
95
-
half-life: 15 min at 0.4 mg/ml, 30 min at 0.8 mg/ml. Temperature-dependent inactivation of the enzyme is irreversible, this process is accompanied by a progressive increase in hydrophobic surface area which leads to protein precipitation
98
half-life: 2 h. alignment of the sequences for the thermophilic glutamate dehydrogenases from Thermococcus litoralis and Pyrococcus furiosus against the sequence and the molecular structure of the glutamate dehydrogenase from the mesophile Clostridium symbiosum provides insights into the molecular basis of their thermostability. A relatively small number of amino acid substitutions is observed between the two thermophilic glutamate dehydrogenase sequences. The most frequent amino acid exchanges involves substitutions which increase the hydrophobicity and sidechain branching in the more thermostable enzyme. Particularly common is the substitution of valine to isoleucine. Examination of the sequence differences suggests that enhanced packing within the buried core of the protein plays an important role in maintaining stability at extreme temperatures. One hot spot for the accumulation of exchanges lies close to a region of the molecule involved in its conformational flexibility and these changes may modulate the dynamics of this enzyme and thereby contribute to increased stability
additional information