Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Reaction

L-glutamate
+
H2O
+
NADP+
=
2-oxoglutarate
+
NH3
+
NADPH
+
H+

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

Engineering

Engineering 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.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C141S
reductive amination activity of C141S alone is insensitive to treatment with 2-hydroxyethyl disulfide
C415S
mutant loses its reductive amination activity in a manner very similar to the native enzyme
K116A
almost complete loss of activity
K128A
almost complete loss of activity
K136A
residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH, fourfold increase in the Km value for NADH with a concomitant 1.6fold increase in the kcat value
K92A
almost complete loss of activity
N347A
almost complete loss of activity
R208A
almost complete loss of activity
R290A
residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH
S265A
residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH
S379A
almost complete loss of activity
K116A
-
almost complete loss of activity
-
K128A
-
almost complete loss of activity
-
K92A
-
almost complete loss of activity
-
R208A
-
almost complete loss of activity
-
S379A
-
almost complete loss of activity
-
K136A
-
residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH, fourfold increase in the Km value for NADH with a concomitant 1.6fold increase in the kcat value
-
R290A
-
residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH
-
S265A
-
residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH
-
C321A
site-directed mutagenesis, the mutant shows reduced NADP-related GDH activity, the mutation causes a greater than a 2fold drop in Vmax and more than a 2fold increase in Km for NADP+
K286Q
site-directed mutagenesis, the mutant shows increased KM for NADP+ compared to the wild-type enzyme
K286Q/R289Q/R292Q
site-directed mutagenesis, the mutant shows highly increased KM for NADP+ compared to the wild-type enzyme
K286Q/R289Q/R292Q/S264L
site-directed mutagenesis, the mutant shows highly increased KM for NADP+ compared to the wild-type enzyme
K286Q/R289Q/R292Q/S264L/S240A
site-directed mutagenesis, the mutant shows highly increased KM for NADP+ compared to the wild-type enzyme
K341L
site-directed mutagenesis, the mutant shows reduced NADP-related GDH activity compared to wild-type
K92C
altering substrate specificity from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway, 5.5fold increase in speific activity with homoserine
K92M
altering substrate specificity from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway, 2.8fold increase in speific activity with homoserine
K92V
altering substrate specificity from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway, 7.2fold increase in speific activity with homoserine
P320A
site-directed mutagenesis, the mutant shows reduced NADP-related GDH activity, the mutation causes a greater than a 2fold drop in Vmax and more than a 2fold increase in Km for NADP+. The mutant is not inhibited by propylselen
R289Q
site-directed mutagenesis, the mutant shows increased KM for NADP+ compared to the wild-type enzyme
R292Q
site-directed mutagenesis, the mutant shows increased KM for NADP+ compared to the wild-type enzyme
K110L
a naturally occurring mutation responsible for the inactivation of the catalytic site of Gdh1
K419A
-
site-directed mutagenesis of GDH1
K420A
-
site-directed mutagenesis of GDH1
K423A
-
site-directed mutagenesis of GDH1
K426A
-
site-directed mutagenesis of GDH1
K110L
-
a naturally occurring mutation responsible for the inactivation of the catalytic site of Gdh1
-
K419A
-
site-directed mutagenesis of GDH1
-
K420A
-
site-directed mutagenesis of GDH1
-
K423A
-
site-directed mutagenesis of GDH1
-
K426A
-
site-directed mutagenesis of GDH1
-
E158Q
-
3.3% as active as wild-type
T138E
-
1.6% as active as wild-type
D167T
the mutant enzyme is slightly more thermostable than the wild-type enzyme
T138E
the mutant enzyme is much less thermostable than the wild-type enzyme
D167T
-
the mutant enzyme is slightly more thermostable than the wild-type enzyme
-
T138E
-
the mutant enzyme is much less thermostable than the wild-type enzyme
-
N117R
-
80% activity of wild-type at optimum temperature for catalysis
R190A/E231A/K193A
-
mutation has no effect on the overall conformation of the protein
S128R
-
same activity as wild-type at optimum temperature for catalysis
S128R/T158E
-
120% activity of wild-type at optimum temperature for catalysis
S128R/T158E/N117R
-
same activity as wild-type at optimum temperature for catalysis
S128R/T158E/N117R/S160E
-
same activity as wild-type at optimum temperature for catalysis
S128R/T158E/S160E
-
same activity as wild-type at optimum temperature for catalysis
T158E
-
60% activity of wild-type at optimum temperature for catalysis
additional information