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EC Tree
The taxonomic range for the selected organisms is: Rattus norvegicus The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
hgdh2, glutamate dehydrogenase 1, gdhii, nad(p)-dependent glutamate dehydrogenase, legdh1, nad(p)+-dependent glutamate dehydrogenase, nad(p)-glutamate dehydrogenase, nad(p)h-dependent glutamate dehydrogenase, ttgdh,
more
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glutamate dehydrogenase
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glutamate dehydrogenase 1
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dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate))
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glutamic acid dehydrogenase
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glutamic dehydrogenase
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L-glutamate dehydrogenase
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L-glutamic acid dehydrogenase
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Membrane protein 50
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NAD(P)-glutamate dehydrogenase
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NAD(P)H-dependent glutamate dehydrogenase
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NAD(P)H-utilizing glutamate dehydrogenase
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reductive amination
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L-glutamate:NAD(P)+ oxidoreductase (deaminating)
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L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
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?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
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L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
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r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
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alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H
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very low activity
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L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
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r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
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r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
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r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
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r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
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r
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additional information
cofactor specificity not mentioned
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NAD+
utilizes NAD+ for nitrogen liberation
NAD+
GDH1 uses NAD+ or NADP+ as coenzyme
NADP+
utilizes NADP+ for nitrogen incorporation
NADP+
GDH1 uses NAD+ or NADP+ as coenzyme
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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
Glyoxal
67% inhibition at 1 mM
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
GTP
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GTP
8.23% activity in the presence of 0.01 mM ATP
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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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ADP
120.88% activity in the presence of 0.25 mM ATP
ADP
ADP induces an allosteric conformational change in GDH1, leading to a 2fold enhanced oxidative deamination
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
enhances the oxidative deamination reaction of GDH1
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additional information
additional information
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4.61
glutamate
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mitochondrial enzyme, cofactor NAD+
5.93
glutamate
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enzyme from rough ER, cofactor NAD+
20.7
glutamate
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mitochondrial enzyme, cofactor NADP+
23.8
glutamate
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enzyme from rough ER, cofactor NADP+
0.364
NAD+
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mitochondrial enzyme
0.924
NAD+
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enzyme from rough ER
0.443
NADP+
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enzyme from rough ER
0.637
NADP+
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mitochondrial enzyme
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0.00005
GTP
GTP alone
0.00156
GTP
molar ratio pyridoxamine 5'-phosphate-form of the mitochondrial branched chain aminotransferase (PMP-BCATm)/GDH1: 1
0.00312
GTP
molar ratio pyridoxamine 5'-phosphate-form of the mitochondrial branched chain aminotransferase (PMP-BCATm)/GDH1: 2
0.00795
GTP
molar ratio pyridoxamine 5'-phosphate-form of the mitochondrial branched chain aminotransferase (PMP-BCATm)/GDH1: 6
0.00806
GTP
molar ratio pyridoxamine 5'-phosphate-form of the mitochondrial branched chain aminotransferase (PMP-BCATm)/GDH1: 4
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8
oxidative deamination at
9 - 9.5
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glutamte deamination
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7.5 - 8
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half activity of glutamate deamination compared to pH 9.5
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8.05
isoelectric focusing
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UniProt
brenda
precursor
UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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peripheral membrane protein
brenda
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metabolism
GDH1 is the protein partner for pyridoxamine 5'-phosphate-form of the mitochondrial branched chain aminotransferase (PMP-BCATm). Facilitating the recycling of BCATm to form metabolon, GDH1 acts as a catalytic machine
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DHE3_RAT
558
0
61416
Swiss-Prot
Mitochondrion (Reliability: 3 )
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300000 - 350000
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liver, sedimentation equilibrium
56000
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x * 56000, enzymes from mitochondria and endoplasmic reticulum
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homohexamer
method of determination not further specified
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x * 56000, enzymes from mitochondria and endoplasmic reticulum
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42
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mitochondrial enzyme loses 80% activity after 20 min, enzyme from endoplasmic reticulum loses 20% activity
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DEAE-Sepharose, ATP-agarose, Resource Q
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complete loss of activity after incubation with 6 M guanidine hydrochloride or 7 M urea, no renaturation after dilution into 200 mM phosphate buffer
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nutrition
restricted feeding with food access for 2 h each day for three weeks promotes higher levels of mitochondrial glutamate dehydrogenase protein and activity, as well as a loss of 24-h rhythmicity, in comparison to ad libitum conditions. The rhythmicity of glutamate dehydrogenase activity detected in serum is changed
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Smith, E.L.; Austen, B.M.; Blumenthal, K.M.; Nyc, J.F.
Glutamate dehydrogenase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
11
293-367
1975
Acholeplasma laidlawii, Auxenochlorella pyrenoidosa, Bos taurus, Gallus gallus, Homo sapiens, Lithobates catesbeianus, Rattus norvegicus, Squalus acanthias, Sus scrofa, Thunnus thynnus
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brenda
Arnold, H.; Maier, K.P.
Glutamate dehydrogenase from rat liver
Biochim. Biophys. Acta
251
133-140
1971
Rattus norvegicus
brenda
Graham, L.D.; Griffin, T.O.; Beatty, R.E.; McCarthy, A.D.; Tipton, K.F.
Purification of liver glutamate dehydrogenase by affinity precipitation and studies on its denaturation
Biochim. Biophys. Acta
828
266-269
1985
Bos taurus, Rattus norvegicus
brenda
Rajas, F.; Rousset, B.
A membrane-bound form of glutamate dehydrogenase possesses an ATP-dependent high-affinity microtubule-binding activity
Biochem. J.
295
447-455
1993
Bos taurus, Rattus norvegicus, Sus scrofa
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brenda
Lee, W.K.; Shin, S.; Cho, S.S.; Park, J.S.
Purification and characterization of glutamate dehydrogenase as another isoprotein binding to the membrane of rough endoplasmic reticulum
J. Cell. Biochem.
76
244-253
1999
Rattus norvegicus
brenda
Zhang, X.; Vincent, A.S.; Halliwell, B.; Wong, K.P.
A mechanism of sulfite neurotoxicity: direct inhibition of glutamate dehydrogenase
J. Biol. Chem.
279
43035-43045
2004
Rattus norvegicus
brenda
Hamelin, M.; Mary, J.; Vostry, M.; Friguet, B.; Bakala, H.
Glycation damage targets glutamate dehydrogenase in the rat liver mitochondrial matrix during aging
FEBS J.
274
5949-5961
2007
Rattus norvegicus (P10860)
brenda
Islam, M.M.; Nautiyal, M.; Wynn, R.M.; Mobley, J.A.; Chuang, D.T.; Hutson, S.M.
The branched chain amino acid (BCAA) metabolon: Interaction of glutamate dehydrogenase with the mitochondrial branched chain aminotransferase (BCATm)
J. Biol. Chem.
285
265-276
2010
Rattus norvegicus (P10860)
brenda
Vazquez-Martinez, O.; Mendez, I.; Turrubiate, I.; Valente-Godinez, H.; Perez-Mendoza, M.; Garcia-Tejada, P.; Diaz-Munoz, M.
Restricted feeding modulates the daily variations of liver glutamate dehydrogenase activity, expression, and histological location
Exp. Biol. Med. (Maywood)
242
945-952
2017
Rattus norvegicus (P10860)
brenda