1.4.1.4: glutamate dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about glutamate dehydrogenase (NADP+), go to the full flat file.
Word Map on EC 1.4.1.4
-
1.4.1.4
-
ammonia
-
2-oxoglutarate
-
neurospora
-
crassa
-
6.3.1.2
-
gogat
-
nad-gdhs
-
sorokiniana
-
ammonium-inducible
-
ectomycorrhizal
-
phosphate-specific
-
molecular biology
-
analysis
-
biotechnology
-
synthesis
-
agriculture
-
medicine
-
food industry
- 1.4.1.4
- ammonia
- 2-oxoglutarate
- neurospora
- crassa
-
6.3.1.2
- gogat
- nad-gdhs
- sorokiniana
-
ammonium-inducible
- ectomycorrhizal
-
phosphate-specific
- molecular biology
- analysis
- biotechnology
- synthesis
- agriculture
- medicine
- food industry
Reaction
Synonyms
APE1386, BpNADPGDH I, BpNADPGDH II, dehydrogenase, glutamate (nicotinamide adenine dinucleotide phosphate), EcGDH, GDH, GDH1, Gdh1p, GDH2, GDH3, Gdh3p, GDH4, GdhA, GDHB, GDHC, GDHI, GDHI', GDHII, GDHP, GluDH, glutamate dehydrogenase, glutamate dehydrogenase 1, glutamate dehydrogenase 2, glutamate dehydrogenase 3, glutamic acid dehydrogenase, glutamic dehydrogenase, GW612_14215, H-form specific BpNADPGDH II, hGDH, hyphal-form specific BpNADPGDH II, L-glutamate dehydrogenase, NAD(P)H-dependent glutamate dehydrogenase, NADP(+)-dependent glutamate dehydrogenase, NADP(H)-dependent glutamate dehydrogenase, NADP(H)-GDH, NADP(H)-specific glutamate dehydrogenase, NADP+ - dependant-glutamate dehydrogenase, NADP+-dependent GDH, NADP+-dependent glutamate dehydrogenase, NADP+-Gdh, NADP-dependent GDH, NADP-dependent GluDH, NADP-dependent glutamate dehydrogenase, NADP-dependent glutamate dehydrogenase 1, NADP-dependent glutamate dehydrogenase 2, NADP-GDH, NADP-GDH 1, NADP-GDH 2, NADP-glutamate dehydrogenase, NADP-linked glutamate dehydrogenase, NADP-specific glutamate dehydrogenase, NADP-specific L-glutamate dehydrogenase, NADP-ylGdh1p, NADPH-dependent GDH, NADPH-dependent glutamate dehydrogenase, OsGDH4, Pcal_1606, RocG, TrGDH, Y-form specific BpNADPGDH I, YALI0F17820g, yeast-form specific BpNADPGDH I, ylGDH1
ECTree
1.4.1.4 glutamate dehydrogenase (NADP+)Advanced search results
results (
results (Temperature Stability
Temperature Stability on EC 1.4.1.4 - glutamate dehydrogenase (NADP+)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
100
102
104
105
115
37
40
50
55
65
67
-
t1/2 in presence of 2 M KCl is about 27 min, while in 4 M KCl the t1/2 is 70 h
70
80
85
86
t1/2 at 5 atm at 86°C is 68 min withjout trehalose and 50 min in presence of 0.5 M trehalose, mutant enzyme T138E
90
95
98
additional information
100
-
wild-type and T138E 50% activity after 2 h and 3 h respectively
100
t1/2 at 5 atm at 100°C is 79 min without trehalose and 185 min in presence of 0.5 M trehalose, wild-type enzyme
102
t1/2 at 5 atm at 101.5°C is 80 min without trehalose and 129 min in presence of 0.5 M trehalose, mutant enzyme D167T
104
half-life is 4.2 min in absence of KCl and 3.3 min in presence of 1 M KCl
105
-
half-life: 13 min at 5 atm, 170 min at 275 atm, 360 min at 500 atm, 470 min at 750 atm, recombinant enzyme
37
-
60 min, yeast enzyme retains 41% of its activity, mycelial enzyme retains 9% of its activity
90
Pcal_1606 retains full activity after incubation for 10 min at temperatures up to 90°C
98
-
recombinant enzyme retains 50% activity after 1.5 h of incubation
additional information
-
the thermostability decreases significantly as the salt concentration is lowered
additional information
-
time-dependent changes in the activity of NADP-GDH at 60°C are analysed: GDHII loses activity completely within 10 min
additional information
wild-type enzyme and mutant enzymes D167T and T138E are thermostabilized, although to different degrees, by the application of 500 atm. The degree of pressure stabilization correlated with GDH stability as well as the magnitude of electrolyte is proposed that pressure stabilizes against thermoinactivation by shifting the equilibrium between conformational substrates of the glutamate dehydrogenase hexamer, thus inhibiting irreversible aggregation
