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
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
1.4.1.3 glutamate dehydrogenase [NAD(P)+]Advanced search results
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results (Inhibitors
Inhibitors on EC 1.4.1.3 - glutamate dehydrogenase [NAD(P)+]
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
8-azidoguanosine 5'-triphosphate
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used for affinity photolabeling, 0.1 mM, 95% inhibition
AlCl3
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increase in sensitivity to aluminium as pH decreases, inhibitory effect is predominant below pH 7.0, no effect above pH 8.5. Completely inactivated enzyme contains 2 mol of aluminum per mol of subunit. Citrate, NaF, N-(2-hydroxyethyl) ethylenediaminetriacetic acid or EDTA efficiently protects against inactivation. Citrate and NaF release aluminum from the completely inactivated aluminum-enzyme complex and fully recover enzyme activity. Binding of aluminum induces a decrease in alpha helices and beta sheets and an increase in random coil
Chloroquine
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potent inhibitor of isozymes GDH1 and GDH2 at a dose-dependent manner, the inhibitory effect of chloroquine on GDH2 is abolished by the presence of ADP and L-leucine, whereas GTP does not change the sensitivity to chloroquine inhibition, shows a non-competitive inhibition against 2-oxoglutarate and an uncompetitive inhibition against NADH
GDP
strong allosteric inhibitor of GDH1 leading to a 90% reduction of activity. Addition of increasing concentrations of pyridoxamine 5'-phosphate-form of the mitochondrial branched chain aminotransferase (PMP-BCATm) leads to an increasing protection from GDP inhibition
L-aspartate
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inhibition of NADPH linked reaction, activation of NAD(H) linked reaction
methylglyoxal
with 1 mM methylglyoxal, GDH activity significantly decreases at 30 min of incubation, and markedly drops by 37% within 5 h compared to control
o-phthalaldehyde
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0.1 mM, 98% inhibition after 5 min at 60°C, competitive vs. 2-oxoglutarate and NADH
oxalylglycine
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competitive vs. 2-oxoglutarate, uncompetitive vs. NADPH, noncompetitive vs. NH4+
p-chloromercuribenzoic acid
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progressive decrease in enzyme activity of both isoenzymes, inhibition is not affected by addition of GTP or ADP
p-hydroxymercuribenzoate
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5 mM, moderate inhibition of isozymes 1-3
Phenylglyoxal
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4 mM, 75% inhibition, uncompetitive vs. 2-oxoglutarate, noncompetitive vs. NADH
phosphate
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pH 8.0-9.0: activation, pH 6.0-7.6: almost complete inhibition with 400 mM
sodium dodecylsulfate
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time-dependent irreversible inhibition, 0.2 mM, 37% inhibition, 0.15 mM, 50% inhibition after 30 min, in the presence of 2-oxoglutarate after 370 min
ATP
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wild-type: inhibition at 0.1 mM and between 0.5-1.0 mM and above, activation at 1 mM, H454Y and S448P mutant enzyme: activation between 0.1-1 mM, inhibition above, R463A mutant enzyme: progressive inhibition between 0.01 and 10 mM
D-glutamate
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10 mM, 57% inhibition of NADP+-linked activity, 30% inhibition of NADPH-linked activity
Glutarate
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shows no affinity for N6-linked NAD+ but is biospecifically adsorbed to S6-linked NAD+ derivatives in the presence of its soluble kinetic-based enzyme capture ligand glutarate
GTP
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GTP inhibition is attenuated to some extent by the proteolysis with TLCK-treated chymotrypsin
GTP
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allosteric regulation, low inhibition of the deamination reaction and strong inhibition of the amination reaction
GTP
inhibition of wild-type enzyme and mutant enzymes r470H and N498S. No inhibition of mutant enzyme G456A. IC50 of wild-type enzyme is 0.00019 mM, IC50 of mutant enzyme G456A is 0.0028 mM, IC50 of mutant enzyme R470G is 0.00017 mM, IC50 of mutant enzyme N498S is 0.0002 mM
GTP
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IC50 for wild-type GLUD1: 0.0122 mM, IC50 for mutant enzyme R443S: 0.0162 mM, IC50 for mutant enzyme M415L: 0.0147 mM, IC50 for mutant enzyme M370L: 0.0113 mM, IC50 for mutant enzyme S331T: 0.0108 mM
GTP
potent inhibitor. IC50 for wild-type enzyme is 0.00019 mM, IC50 for mutant enzyme G456A is 0.0028 mM. ADP renders the GLUD1-derived enzyme less sensitive to GTP inhibition; totally insensitive to, it becomes amenable to GTP inhibition in presence of ADP
GTP
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efective inhibitor: activity below 10% of its full activity; GDH2 is resistent to GTP inhibition
GTP
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allosteric regulation, low inhibition of the deamination reaction and strong inhibition of the amination reaction
NAD+
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incubation with 0.1 mM for 60 min inhibits hGDH1 and hGDH2 by 75% and 70%, respectively, incubations for longer time periods up to 3 h, does not further increase the inhibition of hGDH isoenzymes, ADP-ribosylated hDGH isozymes are reactivated by Mg2+-dependent mitochondrial ADP-ribosylcysteine hydrolase
NADH
modeling of the NADH/ADP site for allosteric effects induced at a single site of binding inhibitor NADH versus activator ADP to GDH. ADP shows dissimilar binding conformations at each NADH/ADP site in the GDH trimer, while NADH shows similar inhibitory binding conformations at each NADH/ADP site
oxaloacetate
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5 mM, 20-25% inhibition of NADH- and NAD+-dependent activities
palmitoyl-CoA
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concentration-dependent inhibition, GDH1 is less sensitive to palmitoyl-CoA inhibition than GDH2
pyridoxal 5'-phosphate
dogfish
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NAD+ and NADP+ protect from inactivation in the presence of sodium glutarate
pyridoxal 5'-phosphate
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0.11 mM, approx. 30% inactivation after 10 min, 0.78 mM, 80% inactivation, inactivation is completely reversed by dialysis
additional information
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complex inhibition pattern for ATP, GTP, NaCl, KCl, sodium acetate, NaI, and potassium nitrate of forward and reverse reaction at 5°C and 37°C
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additional information
the isozyme hGDH2 is resistant against GTP inhibition
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additional information
the isozyme hGDH2 is resistant against GTP inhibition
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additional information
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the isozyme hGDH2 is resistant against GTP inhibition
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additional information
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no inhibition or activation in the presence of ADP, GTP and leucine
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additional information
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complex inhibition pattern for ATP, GTP, NaCl, KCl, sodium acetate, NaI, and potassium nitrate of forward and reverse reaction at 5°C and 37°C
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