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BRENDA support

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)+]

Engineering

Engineering 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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I397V/I406L/S411A
mutation to residues found in isoforms Gdh1 and Gdh2, increase in thermal stability
I406L/S411A
mutation to residues found in isoforms Gdh1 and Gdh2, increase in thermal stability
S411A
mutation to residue found in isoforms Gdh1 and Gdh2, increase in thermal stability
HH454Y
mutation causes the hyperinsulinism/hyperammonemia syndrome (HHS) where insulin is hypersecreted upon consumption of protein due to loss of GLZD1 function. Mutation lies in the GTP binding pocket
A456G
-
mutant of isoenzyme hGDH2 shows no change in heat inactivation process compared to wild-type enzyme
C119A
-
reduction in the ADP-ribosylation
C119G
-
reduction in the ADP-ribosylation
C119Y
-
reduction in the ADP-ribosylation
C274A
-
reduction in the ADP-ribosylation
C274G
-
reduction in the ADP-ribosylation
C274Y
-
reduction in the ADP-ribosylation
C323G
-
decreased turnover rate of both isoenzymes as compared to wild-type
C323L
-
decreased turnover rate of both isoenzymes as compared to wild-type
C323M
-
decreased turnover rate of both isoenzymes as compared to wild-type
C323R
-
decreased turnover rate of both isoenzymes as compared to wild-type
C323Y
-
decreased turnover rate of both isoenzymes as compared to wild-type
C59A
-
reduction in the ADP-ribosylation
C59G
-
reduction in the ADP-ribosylation
D172Y
D185A
-
site-directed mutagenesis, the mutant shows no activation by leucine in contrast to the wild-type enzyme
E279G
E279L
-
14.1fold increase in Km-value for NAD+
E279M
-
14.1fold increase in Km-value for NAD+
E279R
-
10.7fold increase in Km-value for NAD+
E279Y
-
11.8fold increase in Km-value for NAD+
G446C
-
a one-month-old boy with a rare form of congenital hyperinsulinism characterised by hypoglycaemia and hyperammonaemia is described. The patient is heterozygous for a novel de novo mutation in the GLUD1 gene in exon 11 of chromosome 10, which encodes glutamate dehydrogenase (GDH). This point mutation alters the corresponding guanine-guanine-thymine (GGT) codon to thymine-guaninethymine (TGT), changing the glycine at position 446 to cysteine (Gly446Cys), which is located on the allosteric domain of the enzyme. The result confirmed the diagnosis of hyperinsulinism and hyperammonaemia syndrome. The patient is treated with diazoxide (12 mg/kg/day) and the glucose infusion is gradually decreased over four days. Blood glucose is maintained around 4 mmol/l. However, the infant┬ĺs ammonia level remain above 120 mmol/l
G446D
-
kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis
G456A
H454Y
H470R
-
mutant of isoenzyme hGDH2 shows no change in heat inactivation process compared to wild-type enzyme
K118Y
K130Y
K333L
-
kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis
K337L
-
kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis
K344L
-
kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis
K346L
-
kinetic parameters are almost identical to that of the wild-type enzyme. Subunit composition and polymerisation process are not affected by matagenesis
K450E
-
mutation in the pivot helix, mutant shows diminished basal activity and a strongly decreased maximal activity, no activation by L-leucine, ADP restores the decreased activity of K450E but this occurs at substantially higher concentrations compared to wild-type, mutant shows an increased resistance to GTP inhibition, mutation makes the enzyme extremely heat-labile compared to wild-type. IC50 (GTP): 180
K450G
-
mutant enzyme is unable to bind GTP, no difference in sensitivity to aluminum binding between wild-type and mutant enzyme
L415M
-
mutant of isoenzyme hGDH2 shows no change in heat inactivation process compared to wild-type enzyme
L415M/S443R/A456G
-
triple mutant hGDH2(hGDH1390-465)hGDH2 (amino acid segment 390-465 of hGDH2 replaced by the corresponding hGDH1 segment)
M370L
-
mutation does not abolish basal activity and does not abrogate the activation of the enzyme by L-Leu
M415L
-
mutation does not abolish basal activity and does not abrogate the activation of the enzyme by L-Leu
M415L/R443S/G456A
-
triple mutant hGDH1(hGDH2390-465)hGDH1 (amino acid segment 390-465 of hGDH1 replaced by the corresponding hGDH2 segment)
M415L/R443S/G456A/R470H
site-directed mutagenesis
N498S
mutation does not render the enzyme resistant to GTP inhibition
Q441R
R151M
-
site-directed mutagenesis, the mutant shows reduced activation by leucine compared to the wild-type enzyme
R443S
R443S/G456A
-
resistant to GTP inhibition
R463A
-
stimulatory effect of ADP is eliminated
R470H
S331T
-
mutation does not abolish basal activity and does not abrogate the activation of the enzyme by L-Leu
S443R
-
mutant of isoenzyme hGDH2 shows a dramatic increase in thermal stability from 45 min at 45┬░C for the wild-type enzyme to 300 min for the mutant enzyme. KM-values and turnover-numbers are nearly identical to wild-type enzyme
S445A
site-directed mutagenesis, the specific antibody, generated from 12-amino acid hGDH2-specific peptide PTAEFQDSISGA, corresponding to residues 436-447 of the mature human protein, shows reduced reactivity with the enzyme mutant
S445L
S448P
Y187E
-
KM-values for NADH and 2-oxoglutareta are similar to wild-type values, about 4fold decrease of Vmax
Y187G
Y187M
-
KM-values for NADH and 2-oxoglutareta are similar to wild-type values, about 4fold decrease of Vmax, no significant actication by ADP
Y187S
-
KM-values for NADH and 2-oxoglutareta are similar to wild-type values, about 4fold decrease of Vmax, no significant actication by ADP
Y197R
-
KM-values for NADH and 2-oxoglutareta are similar to wild-type values, about 4fold decrease of Vmax, no significant actication by ADP
up
show higher activities in cells grown on the peptides-plus-S(0) medium than in cells using maltose as the sole carbon source
A72D
-
site-directed mutagenesis, the mutant shows no activation by leucine in contrast to the wild-type enzyme
D166A
-
site-directed mutagenesis, the mutant shows reduced activation by leucine compared to the wild-type enzyme
I71T
-
site-directed mutagenesis, the mutant shows reduced activation by leucine compared to the wild-type enzyme
R134A
-
site-directed mutagenesis, the mutant shows no activation by leucine in contrast to the wild-type enzyme
Y38S
-
site-directed mutagenesis, the mutant shows reduced activation by leucine compared to the wild-type enzyme
additional information