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1.4.1.2: glutamate dehydrogenase

This is an abbreviated version!
For detailed information about glutamate dehydrogenase, go to the full flat file.

Word Map on EC 1.4.1.2

Reaction

L-glutamate
+
H2O
 +
NAD+
=
2-oxoglutarate
 +
NH3
 +
NADH
 +
H+

Synonyms

At5g18170, AtGDH1, BpNADGDH, c, CCNA_00086, CsGDH, dehydrogenase, glutamate, GDH, GDH isoenzyme 1, GDH, NAD-dependent, gdh-1, gdh-2, GDH1, GDH2, Gdh2p, GDH3, GdhA, GDHB, GDHI, GdhZ, Glu dehydrogenase, GluD, GLUD1, GLUD2, GluDH, glutamate dehydrogenase, glutamate dehydrogenase (NAD), glutamate dehydrogenase 2, glutamate dehydrogenase alpha subunit, glutamate dehydrogenase beta subunit, glutamate dehydrogenase isoform 1, glutamate oxidoreductase, glutamic acid dehydrogenase, glutamic dehydrogenase, hGDH1, hGDH2-nerve-specific GDH, house-keeping GDH, L-glutamate dehydrogenase, L-glutamic acid dehydrogenase, More, NAD(+)-dependent glutamate dehydrogenase, NAD(H)-dependent glutamate dehydrogenase, NAD+-dependant glutamate dehydrogenase, NAD+-dependent GDH, NAD+-dependent GDHX, NAD+-dependent GluDH, NAD+-dependent glutamate dehydrogenase, NAD+-GDH, NAD+-glutamate dehydrogenase, NAD+-specific GDH, NAD+-specific glutamate dehydrogenase, NAD-dependent GDH, NAD-dependent glutamate dehydrogenase, NAD-dependent glutamic dehydrogenase, NAD-dependent L-glutamate dehydrogenase, NAD-GDH, NAD-glutamate dehydrogenase, NAD-linked glutamate dehydrogenase, NAD-linked glutamic dehydrogenase, NAD-specific glutamate dehydrogenase, NAD-specific glutamic dehydrogenase, NAD-ylGdh2p, NAD:glutamate oxidoreductase, NADH-dependent GDH, NADH-dependent glutamate dehydrogenase, NADH-GDH, NADH-glutamate dehydrogenase, NADH-linked glutamate dehydrogenase, OsGDH1, OsGDH2, OsGDH3, Pcal_1031, RocG, sco2999, Surface-associated protein PGAG1, t-GDH, type I GDH, YALI0E09603g, ylGDH2

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.1 With NAD+ or NADP+ as acceptor
                1.4.1.2 glutamate dehydrogenase

Temperature Stability

Temperature Stability on EC 1.4.1.2 - glutamate dehydrogenase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 4
-
complete inactivation
105
-
Pcal_1031retains full activity after incubation for 10 min at temperatures up to 105°C
20 - 25
-
no activity in cell extracts prepared at 0 to 4°C, high activities between 20°C and 25°C, 70% activity is retained after 2 h at 0°C in the presence of 20% glycerol
30
-
about 45% loss of activity after 15 min, about 60% loss of activity after 30 min
40
-
about 60% loss of activity after 5 min, about 80% loss of activity after 15 min
40 - 50
the enzyme is stable for 10 min at temperatures up to 40°C but is completely inactivated by incubation for 10 min at 50°C
40 - 70
recombinant purified enzyme, fully stable at 40°C
41
50% of its activity remains after incubation of the wild-type enzyme for 20 min
52
23 min, 56% loss of activity. 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
55
-
half-life: 60 min
65
-
20 min, 50% loss of activity
72
-
half-life: 410 min
75
-
15 min, complete inactivation
78
-
half-life: 50 min
82
-
half-life: 30 min
85
-
120 min, 50% activity loss
90
recombinant purified enzyme, 30 min, 56% remaining
additional information
-
the enzyme shows extremely high temperature stability, molecular mechanism and comparison to other hyperthermophilic enzymes from Pyrococcus furiosus and Thermococcus litoralis, overview