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Enzyme Nomenclature
Information on EC 1.4.1.4 - glutamate dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.4.1.4
Word Map on EC 1.4.1.4
- 1.4.1.4
- glutamine
- ammonia
- 2-oxoglutarate
- neurospora
- crassa
- chlorella
- gogat
- nad-gdhs
-
6.3.1.2
-
ammonium-inducible
- sorokiniana
- ectomycorrhizal
-
phosphate-specific
-
nad-glutamate
-
2.6.1.53
- agriculture
- molecular biology
- food industry
- synthesis
- medicine
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.4.1.4
-
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RECOMMENDED NAME
GeneOntology No.
glutamate dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
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oxidative deamination
-
-
-
-
redox reaction
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-
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reduction
-
-
-
-
reductive amination
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NADP+ oxidoreductase (deaminating)
-
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CAS REGISTRY NUMBER
COMMENTARY
9029-11-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
four putative GDH genes (OsGDH1-4) are present in the rice genome. The GDH sequences from rice and other species can be classified into two types (I and II). OsGDH1-3 belong to type II genes, whereas OsGDH4 belong to type I like gene
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two NADP+-dependent glutamate dehydrogenases encoded by GDH1 and GDH3
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strain ISP4, when grown on isophthalate, Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD show activity of NADP-dependent GDH, while cells grown on glucose, 2fold yeast extract-tryptone broth (2YT) or glutamate show activities of both NAD-dependent GDH and NADP-GDH
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GDH from Aspergillus terreus is kinetically distinct from GDH of Aspergilli niger
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GDH from Aspergillus terreus is kinetically distinct from GDH of Aspergilli niger
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two isoenzymes alpha-subunits at 2 mM ammonia and beta-subunits at 29 mM ammonia
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strain PP4, when grown on isophthalate, Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD show activity of NADP-dependent GDH, while cells grown on glucose, 2fold yeast extract-tryptone broth (2YT) or glutamate show activities of both NAD-dependent GDH and NADP-GDH; strain PPD, when grown on isophthalate, Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD show activity of NADP-dependent GDH, while cells grown on glucose, 2fold yeast extract-tryptone broth (2YT) or glutamate show activities of both NAD-dependent GDH and NADP-GDH
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two NADP+-dependent glutamate dehydrogenases encoded by GDH1 and GDH3
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
two industrial strains of Penicillium chrysogenum a penicillin (PC-pen)- and a cephalosporin producing (PC-ceph) are used in which the NADPH-dependent GDH is deleted by replacing 0.8 kb of the C-terminus of the gdhA gene with the hygromyin B resistance marker, resulting in PC-pen-DELTAgdhA and PC-ceph-DELTAgdhA. The two strains are isogenic except for the insertion of the Streptomyces clavuligerus expandase gene into the genome of PC-ceph. It is shown that this genetic modification results in a radical change in morphology
malfunction
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Gdh3-null cells show accelerated chronological aging and hypersusceptibility to thermal and oxidative stress during stationary phase. Upon exposure to oxidative stress, Gdh3-null strains display a rapid loss in viability associated with typical apoptotic hallmarks, i.e. reactive oxygen species accumulation, nuclear fragmentation, DNA breakage, and phosphatidylserine translocation. In addition, Gdh3-null cells, but not Gdh1-null cells, have a higher tendency toward GSH depletion and subsequent reactive oxygen species accumulation than did wild-type cells. GSH depletion is rescued by exogenous GSH or glutamate. The hypersusceptibility of stationary phase Gdh3-null cells to stress-induced apoptosis is suppressed by deletion of GDH2. Gdh1, but not Gdh3, is subjected to stationary phase-specific degradation in which the Lys-426 residue in the Box420Gdh1 region plays an essential role
malfunction
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Gdh3-null cells show accelerated chronological aging and hypersusceptibility to thermal and oxidative stress during stationary phase. Upon exposure to oxidative stress, Gdh3-null strains display a rapid loss in viability associated with typical apoptotic hallmarks, i.e. reactive oxygen species accumulation, nuclear fragmentation, DNA breakage, and phosphatidylserine translocation. In addition, Gdh3-null cells, but not Gdh1-null cells, have a higher tendency toward GSH depletion and subsequent reactive oxygen species accumulation than did wild-type cells. GSH depletion is rescued by exogenous GSH or glutamate. The hypersusceptibility of stationary phase Gdh3-null cells to stress-induced apoptosis is suppressed by deletion of GDH2. Gdh1, but not Gdh3, is subjected to stationary phase-specific degradation in which the Lys-426 residue in the Box420Gdh1 region plays an essential role
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metabolism
NADP+-GDH is involved in nitrogen assimilation due to a constitutive aminating activity, specific activity of the aminating NADP+-GDH reaction is independent of nitrogen availability, it does not change significantly in response to prolonged exposure to nitrogen limitation, in contrast to the deaminating activity, which is 2fold increased exposed to ammonium starvation conditions. The deaminating reaction changes in response to varying ammonium concentrations and is regulated in response to nitrogen availability. NADP+-GDH is not regulated on the transcriptional level. The enzyme is invovled in the additional nitrogen assimilatory pathway via glutamate dehydrogenase, GDH, regulation of NADP+-GDH specific activity, overview
metabolism
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both NADP(H)-GDH (gdhA) and glutamine synthetase play important roles in ammonium assimilation
physiological function
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to test the effect of decreased hGDH expression, small interfering hGDH RNAs are expressed intracellularly in BE(2)C human neuroblastoma cells. hGDH mRNA knockdown is confirmed by immunoblotting and RT-PCR. TUNEL and DNA fragmentation assays 48 h after transfection reveal that inhibition of hGDH expression induces cellular apoptosis and activates phospho-ERK1/2 (phospho-extracellular-signal-regulated kinase 1/2)
physiological function
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carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Time-dependent changes in the activity of NADP-GDH at 60°C are analysed: isophthalate-, glucose-, 2YT- or mHB-grown cells retain 100% of the activity of NADP-GDH
physiological function
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carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD; carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Time-dependent changes in the activity of NADP-GDH at 60°C are analysed: GDHI from isophthalate- and mHB-grown cells retain 70% and 90% of its activity, respectively; carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Time-dependent changes in the activity of NADP-GDH at 60°C are analysed: In Pseudomonas aeruginosa strain PPD, isophthalate-, glucose-, 2YT- or mHB-grown cells retain 100% of the activity of NADP-GDH, while PPD cells grown on pHB and benzoate show 25% and 40% loss of activity
physiological function
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involvement of GDH3-encoded NADP+-dependent glutamate dehydrogenase in yeast cell resistance to stress-induced apoptosis in stationary phase cells, overview. GDH1, but not GDH3, is responsible for the resistance against stress-induced apoptosis in logarithmic phase cells, Necessity of GDH3 for the resistance to stress-induced apoptosis and chronological aging is due to the stationary phase-specific expression of GDH3 and concurrent degradation of Gdh1 in which the Lys-426 residue plays an essential role
physiological function
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Gdh1p is the primary GDH enzyme and Gdh3p plays an evident role during aerobic glutamate metabolism
physiological function
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involvement of GDH3-encoded NADP+-dependent glutamate dehydrogenase in yeast cell resistance to stress-induced apoptosis in stationary phase cells, overview. GDH1, but not GDH3, is responsible for the resistance against stress-induced apoptosis in logarithmic phase cells, Necessity of GDH3 for the resistance to stress-induced apoptosis and chronological aging is due to the stationary phase-specific expression of GDH3 and concurrent degradation of Gdh1 in which the Lys-426 residue plays an essential role
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additional information
modelling of NADP+ in domain II reveals the potential contribution of positively charged residues from a neighbouring alpha-helical hairpin to phosphate recognition, sequence-structure relationship, overview. A single sequence accommodates both coenzymes in the dual-specificity GDHs of animals
additional information
the parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes; the three-dimensional structure of hexameric PfGDH2 is solved to 3.1 A resolution, overview. The parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes
additional information
the parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes; the three-dimensional structure of hexameric PfGDH2 is solved to 3.1 A resolution, overview. The parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminopentanoate + H2O + NADP+
2-oxopentanoate + NH3 + NADPH + H+
-
activity with 2-oxovalerate amd 2-aminopentanoate is 25% and 17% compared to the activity with 2-oxoglutarate and L-glutamate
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-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
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weak activity
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-
?
2-oxovalerate + NADPH + NH3
L-2-aminovalerate + NADP+ + H2O
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15% of the activity with 2-oxoglutarate
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-
?
2-oxoadipate + NADPH + NH3
L-2-aminoadipate + NADP+ + H2O
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6.3% of the activity with 2-oxoglutarate
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-
?
2-oxoadipate + NADPH + NH3
L-2-aminoadipate + NADP+ + H2O
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6.3% of the activity with 2-oxoglutarate
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-
?
2-oxobutyrate + NADPH + NH3
L-2-aminobutyrate + NADP+ + H2O
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12% of the activity with 2-oxoglutarate
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?
2-oxobutyrate + NADPH + NH3
L-2-aminobutyrate + NADP+ + H2O
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12% of the activity with 2-oxoglutarate
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?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
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-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
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-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
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ammonia-assimilating enzyme
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-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
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ammonia-assimilating enzyme
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-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
the enzyme primary functions to assimilate ammonium when its extracellular concentration is in a narrow range. The enzyme may not be the main enzyme for ammonia assimilation in Kluyveromyces marxianus
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-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
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the enzyme primary functions to assimilate ammonium when its extracellular concentration is in a narrow range. The enzyme may not be the main enzyme for ammonia assimilation in Kluyveromyces marxianus
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?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
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-
-
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?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
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r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
referred reaction
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r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
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-
-
-
ir
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
-
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
usage of NH4Cl as substrate for the reverse reaction
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-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
usage of NH4Cl as substrate for the reverse reaction
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r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
the enzyme shows a strict specificity for L-glutamate and NADP+ on oxidative deamination and for 2-oxoglutarate and NADPH on reductive amination. No activity with the following amino acids in oxidative deamination: D-glutamate, L-norvaline, L-2-aminobutyrate, L-valine, L-alanine, L-aspartate, L-serine, L-cysteine, L-lysine, or L-phenylalanin. No activity with the following amino acids in reductive amination: pyruvate, 2-oxovalerate, 2-oxoisocaproate, 2-oxobutyrate, or 2-oxoisovalerate
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-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
the enzyme shows a strict specificity for L-glutamate and NADP+ on oxidative deamination and for 2-oxoglutarate and NADPH on reductive amination
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
the enzyme shows a strict specificity for L-glutamate and NADP+ on oxidative deamination and for 2-oxoglutarate and NADPH on reductive amination
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-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
reaction cycle, specificities of forward and reverse reactions, overview
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
reaction cycle, overview
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
usage of NH4Cl as substrate for the reverse reaction
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
usage of NH4Cl as substrate for the reverse reaction
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia, biphasic kinetic behavior for L-glutamate
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
Sphaerostilbe repens
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia
r
additional information
?
-
-
glutamate dehydrogenase functions physiologically for the synthesis of L-glutamate from 2-oxoglutarate and ammonia
-
-
-
additional information
?
-
-
no reaction with D-glutamate, L-glutamine or DL-2-hydroxyglutarate as possible substrates in place of L-glutamate, methylamine is unable to replace ammonium in the biosynthetic reaction
-
-
-
additional information
?
-
-
no reaction with D-glutamate, L-glutamine or DL-2-hydroxyglutarate as possible substrates in place of L-glutamate, methylamine is unable to replace ammonium in the biosynthetic reaction
-
-
-
additional information
?
-
-
the yeast form specific isoenzyme is induced in presence of glucose, the mycelium-form is not induced. Possible involvement of the enzyme in yeast-mycelium transition
-
-
-
additional information
?
-
-
enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
-
-
additional information
?
-
-
enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
-
-
additional information
?
-
-
no activity with 2-oxoisovalerate and pyruvate
-
-
-
additional information
?
-
-
no activity with 2-oxoisovalerate and pyruvate
-
-
-
additional information
?
-
-
the enzyme is encoded by gdhA. In strains expressing high levels of gdhA mRNA, two promoters, gdhA P1 and gdhA P2, initiate transcription of gdhA. In strains expressing low mRNA levels, gdhA P2 is not active because of weak expression of GdhR, an associated regulatory gene. 2-Oxoglutarate inhibits binding of GdhR to gdhA P2
-
-
-
additional information
?
-
Like PfGDH1, PfGDH2 is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH1 but with slightly higher Km values for its substrates
-
-
-
additional information
?
-
Like PfGDH1, PfGDH2 is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH1 but with slightly higher Km values for its substrates
-
-
-
additional information
?
-
PfGDH1, like PfGDH2, is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH2 but with slightly lower Km values for its substrates
-
-
-
additional information
?
-
PfGDH1, like PfGDH2, is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH2 but with slightly lower Km values for its substrates
-
-
-
additional information
?
-
the enzyme also shows low activity with NAD+/NADH, 17% and 7% of the activity with NADP+ and NADPH, respectively. The enzyme also shows low activity with L-norvaline as substrates for oxidative deamination, and with 2-oxovalerate and 2-oxobutyrate for reducive amination, substrate specificity, overview. No activity with L-glutamine, L-alanine, L-aspartate, L-cysteine, L-serine, L-lysine, L-phenylalanine, and L-tryptophan, or with 2-oxoisocaproate, 2-oxocaproate, and pyruvate
-
-
-
additional information
?
-
the enzyme also shows low activity with NAD+/NADH, 17% and 7% of the activity with NADP+ and NADPH, respectively. The enzyme also shows low activity with L-norvaline as substrates for oxidative deamination, and with 2-oxovalerate and 2-oxobutyrate for reducive amination, substrate specificity, overview. No activity with L-glutamine, L-alanine, L-aspartate, L-cysteine, L-serine, L-lysine, L-phenylalanine, and L-tryptophan, or with 2-oxoisocaproate, 2-oxocaproate, and pyruvate
-
-
-
additional information
?
-
-
in yeast, NADP+-dependent enzymes, EC 1.4.1.4, encoded by GDH1 and GDH3, are reported to synthesize glutamate from 2-oxtoglutarate, while an NAD+-dependent enzyme, EC 1.4.1.2, encoded by GDH2, catalyzes the reverse reaction. Gdh1p is the primary GDH enzyme and Gdh2p and Gdh3p play evident roles during aerobic glutamate metabolism
-
-
-
additional information
?
-
-
glutamate dehydrogenase represents an enzymatic link between major catabolic and biosynthetic pathways via the tricarboxylic acid cycle intermediate 2-oxoglutarate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
ammonia-assimilating enzyme
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
ammonia-assimilating enzyme
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
the enzyme primary functions to assimilate ammonium when its extracellular concentration is in a narrow range. The enzyme may not be the main enzyme for ammonia assimilation in Kluyveromyces marxianus
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
the enzyme primary functions to assimilate ammonium when its extracellular concentration is in a narrow range. The enzyme may not be the main enzyme for ammonia assimilation in Kluyveromyces marxianus
-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
Q8ILF7, Q8ILT0
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
-
ir
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
Q2WCS9
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
Q2WCS9
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
A0R3E3
reaction cycle, specificities of forward and reverse reactions, overview
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
Q8ILF7, Q8ILT0
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
A3MWK6
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
A3MWK6
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
additional information
?
-
-
glutamate dehydrogenase functions physiologically for the synthesis of L-glutamate from 2-oxoglutarate and ammonia
-
-
-
additional information
?
-
-
the yeast form specific isoenzyme is induced in presence of glucose, the mycelium-form is not induced. Possible involvement of the enzyme in yeast-mycelium transition
-
-
-
additional information
?
-
-
enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
-
-
additional information
?
-
-
enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
-
-
additional information
?
-
-
the enzyme is encoded by gdhA. In strains expressing high levels of gdhA mRNA, two promoters, gdhA P1 and gdhA P2, initiate transcription of gdhA. In strains expressing low mRNA levels, gdhA P2 is not active because of weak expression of GdhR, an associated regulatory gene. 2-Oxoglutarate inhibits binding of GdhR to gdhA P2
-
-
-
additional information
?
-
Q8ILF7
Like PfGDH1, PfGDH2 is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH1 but with slightly higher Km values for its substrates
-
-
-
additional information
?
-
Q8ILT0
Like PfGDH1, PfGDH2 is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH1 but with slightly higher Km values for its substrates
-
-
-
additional information
?
-
Q8ILF7
PfGDH1, like PfGDH2, is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH2 but with slightly lower Km values for its substrates
-
-
-
additional information
?
-
Q8ILT0
PfGDH1, like PfGDH2, is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH2 but with slightly lower Km values for its substrates
-
-
-
additional information
?
-
-
in yeast, NADP+-dependent enzymes, EC 1.4.1.4, encoded by GDH1 and GDH3, are reported to synthesize glutamate from 2-oxtoglutarate, while an NAD+-dependent enzyme, EC 1.4.1.2, encoded by GDH2, catalyzes the reverse reaction. Gdh1p is the primary GDH enzyme and Gdh2p and Gdh3p play evident roles during aerobic glutamate metabolism
-
-
-
additional information
?
-
-
glutamate dehydrogenase represents an enzymatic link between major catabolic and biosynthetic pathways via the tricarboxylic acid cycle intermediate 2-oxoglutarate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
the ratio of turnover-number to KM-value for NADPH is 6fold higher than the ratio for NADH
NAD+
-
the ratio of turnover-number to KM-value for NADP+ is 72679fold higher than the ratio for NAD+
NADP+
no acrivity with NAD+; the enzyme requires NADP+ as the coenzyme for the oxidation of L-glutamate, which can not be replaced by NAD+
NADP+
-
preferred coenzyme. The ratio of turnover-number to KM-value for NADP+ is 72679fold higher than the ratio for NAD+
NADP+
binding structure involving Asp263 and Ser264, residues P7 and P8, molecular modelling of NADP+ onto the free enzyme structure, overview
NADPH
for the reduction of 2-oxoglutarate, NADPH is the coenzyme and NADH is inert; no activity with NADP+
NADPH
-
preferred coenzyme. The ratio of turnover-number to KM-value for NADPH is 6fold higher than the ratio for NADH
additional information
no activity with NAD+; no activity with NAD+
-
additional information
no activity with NAD+; no activity with NAD+
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K2SO4
enhances the activity by a maximum of about 280-300% at a concentration of 150-200 mM
KCl
Na3PO4
enhances the activity by a maximum of about 280-300% at a concentration of 150-200 mM
NaCl
Zn2+
-
forward reaction of GDH from Aspergillus terreus is 80% inhibited by 5 mM ZnCl2
additional information
-
Ca2+ has no effects on the aminating activity of NADP(H)-GDH
KCl
maximum enhancement of about 170–200% of the relative activity at a concentration of 50–100 mM
KCl
-
stimulating effect of KCl is slightly higher than the effect of identical concentrations of NaCl
NaCl
maximum enhancement of about 170–200% of the relative activity at a concentration of 50–100 mM
NaCl
-
stimulating effect of KCl is slightly higher than the effect of identical concentrations of NaCl
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dimethyl ester of isophthalic acid
-
dimethyl ester of isophthalate (DMIP), but not isophthalate, inhibits Aspergillus niger growth on agar as well as in liquid culture. This is ascribed to the inability of isophthalate to enter fungal mycelia. Dimethyl ester of isophthalic acid is hydrolysed intracellularly to isophthalate. Subsequent to DMIP addition, intracellular isophthalate can be demonstrated. Addition of NH4+ to DMIP-treated Aspergillus niger mycelia results in intensive vacuolation, retraction of cytoplasm and autolysis
Hexachlorophene
15% inhibition at 0.016 mM; 80% inhibition at 0.016 mM
hydroxylamine
-
competitive inhibitor with ammonia and uncompetitive inhibitor with both 2-oxoglutarate and NADPH
L-homoserine
-
competitive inhibitor with respect to both ammonia and glutamine
nitrogen assimilation control protein
-
represses the transcription of the gene gdhA
-
p-Chloromercuriphenyl sulfonate
-
inactivetes, can be reversed by addition of cysteine
sodium dodecylsulfate
-
at 0.7% w/v after 1 h 5% activity
succinate
-
competitive inhibitor with 2 oxoglutarate, uncompetitive with NADPH and non-competitive with ammonia
2-oxoglutarate
-
shows allosteric properties and a sigmoid response (nH=2.5) towards 2-oxoglutarate saturation
4-chloromercuribenzoate
-
at 1 mM and 10 mM, 30% inhibition and 100% inhibition
ADP
-
at 1 mM, 57% inhibition for oxidative deamination and 23% inhibition for reductive amination respectively
Isophthalate
-
a competitive inhibitor of glutamate dehydrogenase, is involved in C and N metabolism
Isophthalate
-
a competitive inhibitor of glutamate dehydrogenase, is involved in C and N metabolism
NaCl
-
50 mM, 50% inhibition. 100 mM, about 60% inhibition. 500 mM, about 90% inhibition by high ionic strength
NH4+
-
inhibits the oxidative deamination activity as a product, inhibition is non-competitive with respect to L-glutamate
p-hydroxymercuribenzoic acid
-
at 10 mM, 90% inhibition after 40 min
pyridoxal 5'-phosphate
-
at 10 mM, 90% inhibition, complete protection when 16.8 mM 2-oxoglutarate and 1.68 mM NADP+ are added
additional information
-
not inhibited by D-glutamate, L-glutamine or DL-2-hydroxyglutarate
-
additional information
inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1; inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1
-
additional information
inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1; inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1
-
additional information
-
no effect: EDTA, o-phenanthroline, sodium azide, 8-hydroxyquinoline in the concentration raneg of 1-10 mM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,5-pyrazoledicarboxylate
-
activates at lower 2-oxoglutarate concentration
3,5-pyridinedicarboxylate
-
activates at lower 2-oxoglutarate concentration
additional information
-
exhibits 2.5-fold-higher GDH activity than cells are grown in milk, instead of glucose
-
CaCl2
-
at 20 mM, 25% and 108% activation of reductive amination and oxidative deamination respectively
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.68
2-oxoglutarate
-
wild-type EcGDH, Vmax: 464 micromol/min/mg, pH 8.0, 25°C
4
2-oxoglutarate
-
reductive amination
285
2-oxoglutarate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 781 mM NH4Cl, Vmax: 2260 micromol/min/mg, pH 8.0, 25°C
606
2-oxoglutarate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 1800 mM NH4Cl, Vmax: 200 micromol/min/mg, pH 8.0, 25°C