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Information on EC 1.4.1.4 - glutamate dehydrogenase (NADP+)
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EC Tree
1.4.1.4 glutamate dehydrogenase (NADP+)Specify your search results
Word Map
- 1.4.1.4
- ammonia
- 2-oxoglutarate
- neurospora
- crassa
-
6.3.1.2
- gogat
-
ammonium-inducible
- nad-gdhs
- sorokiniana
-
glucuronyltransferase
- ectomycorrhizal
-
phosphate-specific
-
2.6.1.53
-
nad-glutamate
- synthesis
- agriculture
- molecular biology
- medicine
- food industry
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nadp-gdh, nadp-dependent glutamate dehydrogenase, nadp-glutamate dehydrogenase, nadp-specific glutamate dehydrogenase, nadp-linked glutamate dehydrogenase, nadph-dependent glutamate dehydrogenase, nadp+-dependent gdh, nadp(+)-dependent glutamate dehydrogenase, nadp+-gdh, nadp+-dependent glutamate dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
APE1386
dehydrogenase, glutamate (nicotinamide adenine dinucleotide phosphate)
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-
-
-
GDH
GDH1
GdhA
GDHB
-
activity staining, inhibition and thermal stability studies indicate the carbon source-dependent presence of three (GDHA, GDHB and GDHC) forms of NADP-GDH in Pseudomonas aeruginosa strain PPD
GDHC
-
activity staining, inhibition and thermal stability studies indicate the carbon source-dependent presence of three (GDHA, GDHB and GDHC) forms of NADP-GDH in Pseudomonas aeruginosa strain PPD
GDHI
GDHI'
GDHII
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activity staining, inhibition and thermal stability studies indicate the carbon source-dependent presence of two (GDHI and GDHII) forms of NADP-GDH in Pseudomonas aeruginosa strain PP4
GDHP
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activity staining, inhibition and thermal stability studies indicate the carbon source-dependent presence of one GDHP form of NADP-GDH in Acinetobacter lwoffii strain ISP4
GluDH
glutamate dehydrogenase
glutamic acid dehydrogenase
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glutamic dehydrogenase
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L-glutamate dehydrogenase
NAD(P)H-dependent glutamate dehydrogenase
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NADP(+)-dependent glutamate dehydrogenase
NADP(H)-specific glutamate dehydrogenase
NADP+-dependent GDH
NADP+-dependent glutamate dehydrogenase
NADP+-Gdh
NADP-dependent GluDH
NADP-dependent glutamate dehydrogenase
NADP-dependent glutamate dehydrogenases
-
2 isoenzymes: a yeast-form isoenzyme and a mycelium-form isoenzyme
NADP-GDH
NADP-glutamate dehydrogenase
NADP-linked glutamate dehydrogenase
NADPH-dependent glutamate dehydrogenase
Pcal_1606
RocG
GdhA
-
activity staining, inhibition and thermal stability studies indicate the carbon source-dependent presence of three (GDHA, GDHB and GDHC) forms of NADP-GDH in Pseudomonas aeruginosa strain PPD
GDHI
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activity staining, inhibition and thermal stability studies indicate the carbon source-dependent presence of two (GDHI and GDHII) forms of NADP-GDH in Pseudomonas aeruginosa strain PP4
L-glutamate dehydrogenase
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NADP-GDH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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oxidative deamination
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redox reaction
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reduction
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reductive amination
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PATHWAY SOURCE
PATHWAYS
KEGG
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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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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
-
-
r
2-oxovalerate + NADPH + NH3
L-2-aminovalerate + NADP+ + H2O
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15% of the activity with 2-oxoglutarate
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-
?
L-homoserine + H2O + NAD+
4-hydroxy-2-oxobutanoate + NH3 + NADH
-
-
-
?
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-oxobutanoate + NH3 + NADPH + H+
L-2-aminobutanoate + H2O + NADP+
2.6% of the activity with 2-oxoglutarate
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-
r
2-oxobutanoate + NH3 + NADPH + H+
L-2-aminobutanoate + H2O + NADP+
2.6% of the activity with 2-oxoglutarate
-
-
r
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
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-
-
?
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
-
-
-
-
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
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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 + 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 + NADH + H+
L-glutamate + H2O + NAD+
A0A1B4WMB5
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-
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r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
A0A1B4WMB5
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-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
weak activity
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?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
AKQ74236
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-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
AKQ74236
-
-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
A0A1B4WMB5
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-
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r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
A0A1B4WMB5
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-
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r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
136% of the activtiy with L-glutamate
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r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
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136% of the activtiy with L-glutamate
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r
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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-
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r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
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-
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r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
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ir
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
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-
-
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r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
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r
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
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-
-
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-
2-oxovalerate + NH3 + NADPH + H+
L-valine + H2O + NADP+
4.2% of the activity with 2-oxoglutarate
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r
2-oxovalerate + NH3 + NADPH + H+
L-valine + H2O + NADP+
4.2% of the activity with 2-oxoglutarate
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r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
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-
-
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?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
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usage of NH4Cl as substrate for the reverse reaction
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r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
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-
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r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
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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
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-
?
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+
AKQ74236
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-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
AKQ74236
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-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
A0A1B4WMB5
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
A0A1B4WMB5
-
-
-
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+
A0R3E3
reaction cycle, specificities of forward and reverse reactions, overview
-
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r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
A0R3E3
reaction cycle, overview
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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
-
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+
-
-
-
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
Aeropyrum pernix K1 JCM 9820
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-
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
-
-
-
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
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-
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-norvaline + H2O + NADP+
2-oxopentanoate + NH3 + NADPH + H+
3% of the activity with L-glutamate
-
-
r
L-norvaline + H2O + NADP+
2-oxopentanoate + NH3 + NADPH + H+
3% of the activity with L-glutamate
-
-
r
additional information
?
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-
glutamate dehydrogenase functions physiologically for the synthesis of L-glutamate from 2-oxoglutarate and ammonia
-
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-
additional information
?
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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
?
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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
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-
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additional information
?
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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
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-
additional information
?
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enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
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-
additional information
?
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enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
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additional information
?
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-
enzyme additionally shows activity towards hexanol and isoamyl alcohol
-
-
-
additional information
?
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-
enzyme additionally shows activity towards hexanol and isoamyl alcohol
-
-
-
additional information
?
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-
no activity with 2-oxoisovalerate and pyruvate
-
-
-
additional information
?
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-
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
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-
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
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-
-
additional information
?
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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
-
-
-
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NATURAL SUBSTRATE
NATURAL 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-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
Bacillus sp. (in: Bacteria) KSM-635
-
-
-
-
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
the ratio of turnover-number to KM-value for NADP+ is 72679fold higher than the ratio for NAD+
NADH
-
the ratio of turnover-number to KM-value for NADPH is 6fold higher than the ratio for NADH
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
NADP+
the NADP-binding pocket is mainly formed by the cofactor-binding domain, with partial contribution by the substrate-binding domain
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-hydroxyethyl disulfide
attenuation of reductive amination (forward) activity but a negligible effect on oxidative deamination (reverse) activity
cystine
strongly and selectively inhibits the reductive amination reaction
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
not inhibitory/activating: oxidized glutathione
-
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Over-expression of a glutamate dehydrogenase gene, MgGDH, from Magnaporthe grisea confers tolerance to dehydration stress in transgenic rice.
Infection
Regulation and differential expression of gdhA encoding NADP-specific glutamate dehydrogenase in Neisseria meningitidis clinical isolates.
Starvation
[Features of the interconversion of alpha-ketoglutarate--glutamate in brain mitochondria of exothermic animals during hibernation]
Starvation
[Glutamate dehydrogenases of unicellular green algae: effects of nitrate and ammonium in vivo]
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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
1.48
2-oxoglutarate
-
isoform Gdh3, S0.5 value, Hill coefficient 2.4, pH 5.8, 30°C
4
2-oxoglutarate
-
reductive amination
4
2-oxoglutarate
mutant C141S, S0.5 value, Hill coefficient 2.3, pH 8.0, temperature not specified in the publication
4.78
2-oxoglutarate
wild-type, S0.5 value, Hill coefficient 3.2, pH 8.0, temperature not specified in the publication
5.7
2-oxoglutarate
recombinant wild-type, S0.5 value, Hill coefficient 3.5, pH 8.0, temperature not specified in the publication
15.5
2-oxoglutarate
mutant C415S, S0.5 value, Hill coefficient 4.9, pH 8.0, temperature not specified in the publication
25.1
2-oxoglutarate
wild-type inactivated by 2-hydroxyethyl disulfide, S0.5 value, Hill coefficient 2.4, pH 8.0, temperature not specified in the publication
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
28.6
L-glutamate
mutant C141S, pH 9.3, temperature not specified in the publication
30.9
L-glutamate
recombinant wild-type, pH 9.3, temperature not specified in the publication
34.6
L-glutamate
wild-type, pH 9.3, temperature not specified in the publication
36.8
L-glutamate
mutant C415S, pH 9.3, temperature not specified in the publication
49.8
L-glutamate
wild-type inactivated by 2-hydroxyethyl disulfide, S0.5 value, Hill coefficient 1.9, pH 9.3, temperature not specified in the publication
1349
L-glutamate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 121.9 micromol/min/mg, pH 8.0, 25°C
0.017
NADP+
wild-type, pH 9.3, temperature not specified in the publication
0.0184
NADP+
-
wild-type enzyme, pH 8.0, temperature not specified in the publication
0.022
NADP+
wild-type inactivated by 2-hydroxyethyl disulfide, pH 9.3, temperature not specified in the publication
0.028
NADP+
recombinant wild-type, pH 9.3, temperature not specified in the publication
0.0328
NADP+
-
mutant K289Q, pH 8.0, temperature not specified in the publication
0.0819
NADP+
-
mutant K292Q, pH 8.0, temperature not specified in the publication
0.129
NADP+
-
mutant K286Q, pH 8.0, temperature not specified in the publication
0.163
NADP+
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 80.8 micromol/min/mg, pH 8.0, 25°C
0.929
NADP+
-
mutant K286Q/R289Q/R292Q , pH 8.0, temperature not specified in the publication
18.3
NADP+
-
mutant K286Q/R289Q/R292Q/S264L/S240A, pH 8.0, temperature not specified in the publication
19.06
NADP+
-
mutant K286Q/R289Q/R292Q/S264L, pH 8.0, temperature not specified in the publication