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 (Activating Compound
Activating Compound on EC 1.4.1.3 - glutamate dehydrogenase [NAD(P)+]
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
APRTh
TTC1249 (APRTh), a 23-30 kDa protein, which is annotated as adenine phosphoribosyltransferase but lacks the enzymatic activity, forms a ternary complex with the enzyme heterodimer, heterocomplex formation and structure, interaction analysis and function, detailed overview. APRTh mediates the allosteric activation of GDH by AMP
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chymotrypsin
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0.2 mg/ml chymotrypsin cleaves glutamate dehydrogenase in such a fashion as to cause a rise in activity with NADP+ and NAD+ as coenzyme, over threefold activation in the NADP+ assay with TLCK-treated chymotrypsin, the distinguishing aspect with untreated chymotrypsin is that the activation is followed by a decrease in activity
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PMP-BCATm
pyridoxamine 5'-phosphate-form of the mitochondrial branched chain aminotransferase (PMP-BCATm) accelerates the oxidative deamination reaction of GDH1in the presence of branched-chain amino acids (Leu, Ile, Val). Reductive amination reaction is not affected
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Trypsin
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limited trypsin proteolyis activates the purified enzyme 8fold if the peptide is absent from the assay mixture, the native enzyme is 3fold activated if the cleaved peptide is present, activation may therefore be induced by loss of the peptide from the subunit of the native enzyme
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ADP
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ADP activation is almost abolished after treatment with TLCK-treated chymotrypsin
ADP
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allosteric activator, addition of ADP or leucine to the single cofactor assay results in a marked activation of NADPH oxidation, about 1100% activation by ADP. Relative activation by ADP of GDH-catalyzed NAD+reduction is 36%, compared with 198% for NADP+ reduction
ADP
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
ADP
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allosteric regulation, weak stimulation of the deamination reaction and strong activation of the amination reaction
ADP
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1 mM, pH 8.0, 3fold activation of wild-type enzyme, no significant actication of Tyr187 mutant enzymes
ADP
in absence of GTP the isoenzyme GLUD2 assumes a conformational state associated with little catalytic activity, it remains amenable to full activation by ADP and/or L-Leu
ADP
ADP is an activator of hGDH1 and hGDH2 which binds only to the open state
ADP
ADP is an activator of hGDH1 and hGDH2 which binds only to the open state. hGDH1mutant R443S/G456A exhibits a reduced ADP sensitivity compared both to hGDH1 and to hGDH2. The addition of the M415L and R470H mutations results in an even more pronounced drop in ADP affinity
ADP
the addition of FLAG tag to the C-terminus of GDH leaves the recombinant protein fivefold less sensitive to ADP activation
ADP
ADP induces an allosteric conformational change in GDH1, leading to a 2fold enhanced oxidative deamination
ADP
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allosteric regulation, weak stimulation of the deamination reaction and strong activation of the amination reaction
AMP
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activates NADH-linked glutamate synthesis, inhibits NADPH-linked activity
AMP
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1 mM, reaction velocity increases 15fold at saturating NAD+ and glutamate levels
AMP
AMP activated GDH activity of the ternary complex, but not the GdhA-GdhB binary complex. APRTh mediates the allosteric activation of GDH by AMP. Reductive amination and oxidative deamination activity is enhanced by up to 6.3 and 2.5fold, respectively, by the addition of 1 mM AMP.
ATP
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allosteric regulation, weak stimulation of the deamination reaction and strong activation of the amination reaction
ATP
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wild-type: activation at 1 mM, inhibition below and above, H454Y and S448P mutant enzymes: progressive increase in activity until 10 mM, inhibition above
ATP
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activates in presence of 3 M NaCl or in absence of salts, slight inhibition in presence of 3 M KCl
ATP
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allosteric regulation, weak stimulation of the deamination reaction and strong activation of the amination reaction
L-Leu
0.3-10 mM stimulates isoenzyme GLUD2 to a greater extent than isoenzyme GLUD1
L-Leu
0.3-10 mM stimulates isoenzyme GLUD2 to a greater extent than isoenzyme GLUD1. In absence of GTP the isoenzyme GLUD2 assumes a conformational state associated with little catalytic activity, it remains amenable to full activation by ADP and/or L-Leu
L-leucine
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allosteric activator, addition of ADP or leucine to the single cofactor assay results in a marked activation of NADPH oxidation, about 725% activation by L-leucine, respectively. Activation of NAD+ and NADP+ reduction by 40% and 135%, respectively
L-leucine
the crystal structure of GdhA/GdhB in a complex with leucine and biochemical analysis reveals that leucine is bound to the pockets at the GdhA-GdhA, GdhA-GdhB, and GdhB-GdhB interfaces. leucine binding increases the turnover of the GDH reaction, possibly through acceleration of the open-close cycle of the active-site cleft between the catalytic domain and NAD-binding domains
leucine
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the enzyme is subject to allosteric activation by leucine invlving ARg134, and Asp185, structural mechanism, overview
leucine
with 10 mM the activity increases by 1.55fold after 240 min and by 1.24fold when the enzyme is preincubated with methylglyoxal
leucine
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the enzyme is subject to allosteric activation by leucine, structural mechanism, overview
additional information
in reductive amination, the influence of AMP and leucine on the Km for NADH, 2-oxoglutarate, and ammonium is not large, although approximately 4.5, 5.3, and 10.2fold increases in Km for 2-OG are observed with AMP, leucine, and the copresence of AMP and leucine, respectively. Activation profiles of GDH activity of the TtGDH-APRTh complex by leucine and AMP, overview
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additional information
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in reductive amination, the influence of AMP and leucine on the Km for NADH, 2-oxoglutarate, and ammonium is not large, although approximately 4.5, 5.3, and 10.2fold increases in Km for 2-OG are observed with AMP, leucine, and the copresence of AMP and leucine, respectively. Activation profiles of GDH activity of the TtGDH-APRTh complex by leucine and AMP, overview
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