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Information on EC 1.4.1.3 - glutamate dehydrogenase [NAD(P)+] and Organism(s) Saccharolobus solfataricus and UniProt Accession P80053

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Saccharolobus solfataricus
UNIPROT: P80053 not found.
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate))
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GDH
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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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Legdh1
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Membrane protein 50
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MP50
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NAD(P)-dependent glutamate dehydrogenase
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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reductive amination
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NAD(P)+ oxidoreductase (deaminating)
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CAS REGISTRY NUMBER
COMMENTARY hide
9029-12-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
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r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
2-oxoglutarate + NH3 + NADPH
L-glutamate + H2O + NADP+
show the reaction diagram
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r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
show the reaction diagram
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
show the reaction diagram
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r
norvaline + H2O + NADP+
2-oxovalerate + NH3 + NADPH
show the reaction diagram
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activity is 20% of that observed in the presence of 2-oxoglutarate and L-glutamate
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glutamate
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2 mM, 11% inhibition, 6 mM, 34% inhibition
o-phthalaldehyde
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0.1 mM, 98% inhibition after 5 min at 60°C, competitive vs. 2-oxoglutarate and NADH
Phenylglyoxal
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4 mM, 75% inhibition, uncompetitive vs. 2-oxoglutarate, noncompetitive vs. NADH
pyridoxal 5'-phosphate
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2 mM, complete loss of activity
additional information
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no inhibition or activation in the presence of ADP, GTP and leucine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 1.4
2-oxoglutarate
0.3 - 2.5
L-glutamate
0.063
NAD+
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+ L-glutamate
0.007 - 0.14
NADH
0.025
NADP+
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+ L-glutamate
0.01
NADPH
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.1
o-phthalaldehyde
5 - 6
Phenylglyoxal
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
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substrates: L-glutamate + H2O + NADP+
7.6
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NAD(P)H + 2-oxoglutarate + NH3
9
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substrates: 2-oxoglutarate + NH3 + NADPH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
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90-100% activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
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substrates: 2-oxoglutarate + NH3 + NADPH
70
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substrates: L-glutamate + H2O + NADP+
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 90
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30°C: about 90% of activity maximum, 90°C: about 35% of activity maximum
45 - 75
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45°C: about 35% of maximal activity, 75°C: about 20% of maximal activity, substrates: 2-oxoglutarate + NH3 + NADPH
60 - 75
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60°C: about 60% of maximal activity, 75°C: about 30% of maximal activity, substrates: L-glutamate + H2O + NADP+
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
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isoelectric focusing. Microheterogeneity shows three active bands corresponding to pI of 5.7, 5.5 and 5.4. The major band shows an isoelectric point of 5.7
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46078
x * 46078, calculated from sequence
270000
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gel filtration
44000
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6 * 44000, SDS-PAGE
45000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 46078, calculated from sequence
?
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x * 45000, SDS-PAGE
hexamer
monomer
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at 25°C the enzyme is mostly represented by monomeric subunits at concentrations lower than 0.02 mg/ml, while oligomers are predominant at concentrations higher than 0.12 mg/ml
oligomer
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at 25°C the enzyme is mostly represented by monomeric subunits at concentrations lower than 0.02 mg/ml, while oligomers are predominant at concentrations higher than 0.12 mg/ml
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
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at least 65% residual activity after 14 h
391621
5.2 - 6.8
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maximal stablility
678367
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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48 h, protein concentration of 0.2 mg/ml, stable
60
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48 h, protein concentration of 0.2 mg/ml, 20% loss of activity
70 - 100
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no loss in activity after 1 h at 90°C, 20% residual activity after 1 h at 100°C
80
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half-life: 15 h
85
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half-life: 2 h
95
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half-life: 15 min at 0.4 mg/ml, 30 min at 0.8 mg/ml. Temperature-dependent inactivation of the enzyme is irreversible, this process is accompanied by a progressive increase in hydrophobic surface area which leads to protein precipitation
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
guanidine-dependent inactivation of the enzyme at 20°C is irreversible above 1.5 M guanidine hydrochloride
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SDS: 0.1% v/v, no loss of activity after 12 h, 0.5%, half-life 5 h
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urea: 4 M, 10% loss of activity after 12 h, 7.5 M, half-life 9 h
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
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50% v/v, complete loss of activity
isopropanol
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50% v/v, complete loss of activity
Methanol
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50% v/v, complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 4°C, 25°C, 6 months, 5% loss of activity
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-70°C, stable for 6 months
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4°C, 1 mg/ml protein concentration, glutamate dehydrogenase remains stable for at least one month
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4°C, 20% loss of activity after 40 days
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4°C, more than 20 days, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
monomeric and oligomeric enzyme show distinct behaviour on guanidine hydrochloride perturbation at neutral pH. The monomer denaturation, although complex, is reversible. Two fluorescent tryptophan classes are detectable in the monomer, monitoring the independent unfolding of two regions through a multistate transition. The oligomeric protein shows a complex denaturation pattern with the tendency to aggregate irreversibly at high denaturant concentration
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schinkinger, M.F.; Redl, B.; Stffler, G.
Purification and properties of an extreme thermostable glutamate dehydrogenase from the archaebacterium Sulfolobus solfataricus
Biochim. Biophys. Acta
1073
142-148
1991
Saccharolobus solfataricus
Manually annotated by BRENDA team
Ahn, J.Y.; Lee, K.S.; Choi, S.Y.; Cho, S.W.
Regulatory properties of glutamate dehydrogenase from Sulfolobus solfataricus
Mol. Cells
10
25-31
2000
Saccharolobus solfataricus
Manually annotated by BRENDA team
Consalvi, V.; Chiaraluce, R.; Politi, L.; Pasquo, A.; De Rosa, M.; Scandurra, R.
Glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus: studies on thermal and guanidine-dependent inactivation.
Biochim. Biophys. Acta
1202
207-215
1993
Saccharolobus solfataricus
Manually annotated by BRENDA team
Consalvi, V.; Chiaraluce, R.; Politi, L.; Gambacorta, A.; De Rosa, M.; Scandurra, R.
Glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus.
Eur. J. Biochem.
196
459-467
1991
Saccharolobus solfataricus
Manually annotated by BRENDA team
Facchiano, A.M.; Ragone, R.; Consalvi, V.; Scandurra, R.; De Rosa, M.; Colonna, G.
Molecular properties of glutamate dehydrogenase from the extreme thermophilic archaebacterium Sulfolobus solfataricus
Biochim. Biophys. Acta
1251
170-176
1995
Saccharolobus solfataricus
Manually annotated by BRENDA team
Maras, B.; Consalvi, V.; Chiaraluce, R.; Politi, L.; De Rosa, M.; Bossa, F.; Scandurra, R.; Barra, D.
The protein sequence of glutamate dehydrogenase from Sulfolobus solfataricus, a thermoacidophilic archaebacterium. Is the presence of N-epsilon-methyllysine related to thermostability?
Eur. J. Biochem.
203
81-87
1992
Saccharolobus solfataricus (P80053), Saccharolobus solfataricus MT-4 / DSM 5833 (P80053)
Manually annotated by BRENDA team