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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

Specific Activity

Specific Activity on EC 1.4.1.2 - glutamate dehydrogenase

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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0003
-
mutant D165N overexpressed at 8°C
0.012
-
2-oxoglutarate, mutant M101K
0.014
-
2-oxoglutarate, mutant K80R
0.019
-
2-oxoglutarate, mutant G82R and M101S
0.026
-
2-oxoglutarate, mutant G82K
0.034
-
mutant D165N overexpressed at 37°C
0.047
-
mutant D165N overexpressed at 23°C
0.0495 - 0.133
-
pH 8.2, 30°C
0.077
NADP-linked GDH activity
0.21
-
on L-aspartate, mutant M101S
0.29
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
0.32
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.34
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.35
-
control group
0.39
-
on L-aspartate, mutant G82K
0.49
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH using NAD+
0.5
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
0.51
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
0.57
-
with protopine
0.62
recombinant enzyme from crude cell extract, at 25°C
0.73
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
0.77
NAD-linked GDH activity
0.84
-
with alkalized extract from the tuber of Corydalis ternata
0.87
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.9
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
0.97
in the presence of antibiotics and ammonia
1.12
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
1.14
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
1.23
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
1.32
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
1.53
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
1.83
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
101.8
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
102
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
11
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
119.5
-
in the presence of 0.1 mM Hg
12
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
12.5
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
15
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
155
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
167
-
GDH I
17.6
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
170.6
-
in the presence of 0.1 mM Hg and in the presence of 5 mM glutamine
171.4
-
in the presence of 0.1 mM Hg and in the presence of 0.1 mM AlCl3
174
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
19
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
19.7
-
in the absence of Hg and in the presence of 0.1 mM AlCl3
2.16
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
2.26
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
2.3
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
2.98
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
20
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
20.1
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
20.6
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
243.4
-
in the presence of 0.1 mM Hg and in the presence of NH4NO3
25
-
in the presence of 0.001 mM Hg and in the presence of NH4NO3
25.3
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
26.7
-
in the presence of 0.001 mM Hg
3
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
3.05
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
3.1
purified recombinant enzyme, at 25°C
3.27
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
3.41
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
3.51
-
native enzyme
3.54
-
recombinant, urea-activated enzyme
3.65
-
recombinant, heat-activated enzyme
3.82
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
30
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
328.2
-
in the presence of 0.1 mM Hg and in the presence of 5 mM sucrose
34
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
34.2
-
in the absence of Hg
35
recombinant enzyme purified from Haloferax volcanii, pH 8.5, 40°C
38
-
GDH-I
4.1
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
4.93
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
440
-
2-oxoglutarate, wild-type
48.7
-
pH 8.0, 23°C
5
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
5.2
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
5.8
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
50
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
52.9
-
in the absence of Hg and in the presence of 5 mM sucrose
54.6
-
in the presence of 0.01 mM Hg
56
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
56.5
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
58
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH using NADP+
58.6
-
in the absence of Hg and in the presence of 5 mM glutathione
59.4
-
in the absence of Hg and in the presence of 5 mM glutamine
6.52
recombinant enzyme in Haloferax volcanii, pH 8.5, 40°C
6.78
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
62
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
65.8
-
in the absence of Hg and in the presence of NH4NO3
68
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
7.2
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
70.94
-
in the presence of 0.1 mM Hg and in the presence of 5 mM glutathione
72
-
in the presence of 0.01 mM Hg and in the presence of NH4NO3
89.3
purified recombinant enzyme
9.01
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
9.6
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
9.8
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
90
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
additional information