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Information on EC 1.4.1.3 - glutamate dehydrogenase [NAD(P)+] and Organism(s) Pyrococcus furiosus and UniProt Accession P80319

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Pyrococcus furiosus
UNIPROT: P80319 not found.
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The taxonomic range for the selected organisms is: Pyrococcus furiosus
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)-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
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
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?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
show the reaction diagram
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
show the reaction diagram
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?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
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?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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both NAD+ and NADP+ are utilized as cofactors. The inactive enzyme also binds cofactors
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
addition of Ca2+ and Mg2+ also shows enhancement of enzyme activity. 3.5fold increase in activity at 10 mM CaCl2 or MgSO4
Mg2+
addition of Ca2+ and Mg2+ also shows enhancement of enzyme activity. 3.5fold increase in activity at 10 mM CaCl2 or MgSO4
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4 - 4.5
2-oxoglutarate
1.6 - 1.66
L-glutamate
0.53
NAD+
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substrate L-glutamate
0.98
NADH
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substrate 2-oxoglutarate
0.18
NADP+
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substrate L-glutamate
0.56
NADPH
9.5
NH3
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cofactor NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32.5
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at 85°C
411
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native enzyme at 100°C
419
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recombinant enzyme at 75°C
423
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recombinant enzyme at 90°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
pH 7.0: about 50% of maximal activity, pH 9.0: about 35% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
97
specific activity increases up to 97°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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inactive at temperatures below 40°C, undergoes heat activation above 40°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47122
x * 47122, calculated from sequence
270000
46000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 47122, calculated from sequence
hexamer
electrostatic interactions play a key role in the relevant stability of Pyrococcus furiosus hlutamate dehydrogenase quaternary assembly at low pH although there may be other contributions involved in the complex mechanism of subunit association required for protein function
hexamer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
lysine methylation not found
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure is determined at 2.2 A resolution and compared with the structure of glutamate dehydrogenase from the mesophile Clostridium symbiosum
hanging-drop method of vapour diffusion using lithium sulfate as the precipitant. The crystals belong to the tetragonal system and are in space group P4(2)2(1)2 with unit-cell dimensions of a = b = 167.2, c = 172.9 A. Consideration of the values of Vm and possible packing of the molecules within the cell suggest that the asymmetric unit contains a trimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
up
show higher activities in cells grown on the peptides-plus-S(0) medium than in cells using maltose as the sole carbon source
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
half-life: 12 h. alignment of the sequences for the thermophilic glutamate dehydrogenases from Thermococcus litoralis and Pyrococcus furiosus against the sequence and the molecular structure of the glutamate dehydrogenase from the mesophile Clostridium symbiosum provides insights into the molecular basis of their thermostability. A relatively small number of amino acid substitutions is observed between the two thermophilic glutamate dehydrogenase sequences. The most frequent amino acid exchanges involves substitutions which increase the hydrophobicity and sidechain branching in the more thermostable enzyme. Particularly common is the substitution of valine to isoleucine. Examination of the sequence differences suggests that enhanced packing within the buried core of the protein plays an important role in maintaining stability at extreme temperatures. One hot spot for the accumulation of exchanges lies close to a region of the molecule involved in its conformational flexibility and these changes may modulate the dynamics of this enzyme and thereby contribute to increased stability
104
half-life: 67 min in absence of KCl, 562 min in presence of 1 M KCl
110
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thermal denaturation starts at 110°C and is completed at 118°C. The process of heat activation from 40 to 80°C is accompanied by a much smaller increase in absorbance at 280 nm and a reversible increase in heat capacity with DELTAcal = 187 Kcal/mol GDH and Tm = 57°C. This absorbance change as well as the moderate increase in heat capacity suggest that thermal activation leads to some exposure of hydrophobic groups to solvent water as the GDH structure is opened slightly. The increase in absorbance at 280 nm during activation is only 12% of that for denaturation
113
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Tm-value = 113°C
118
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thermal denaturation starts at 110°C and is comp1eted at 118°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 6 months, stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Robb, F.T.; Park, J.B.; Adams, M.W.W.
Characterization of an extremely thermostable glutamate dehydrogenase: a key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus
Biochim. Biophys. Acta
1120
267-272
1992
Pyrococcus furiosus
Manually annotated by BRENDA team
Diruggiero, J.; Robb, F.T.
Expression and in vitro assembly of recombinant glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
Appl. Environ. Microbiol.
61
159-164
1995
Pyrococcus furiosus
Manually annotated by BRENDA team
Yip, K.S.; Baker, P.J.; Britton, K.L.; Engel, P.C.; Rice, D.W.; Sedelnikova, S.E.; Stillman, T.J.; Pasquo, A.; Chiaraluce, R.; Consalvi, V.; Scandurra, R.
Crystallization of the NAD(P)-dependent glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus
Acta Crystallogr. Sect. D
51
240-242
1995
Pyrococcus furiosus
Manually annotated by BRENDA team
Chiaraluce, R.; Schwerdtfeger, R.M.; Scandurra, R.; Antranikian, G.; Consalvi, V.
Acid-induced disassembly of glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus occurs below pH 2.0
Eur. J. Biochem.
247
224-230
1997
Pyrococcus furiosus (P80319)
Manually annotated by BRENDA team
Klump, H.; Di Ruggiero, J.; Kessel, M.; Park, J.B.; Adams, M.W.; Robb, F.T.
Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus. Thermal denaturation and activation
J. Biol. Chem.
267
22681-22685
1992
Pyrococcus furiosus
Manually annotated by BRENDA team
Maras, B.; Valiante, S.; Chiaraluce, R.; Consalvi, V.; Politi, L.; de Rosa, M.; Bossa, F.; Scandurra, R.; Barra, D.
The amino acid sequence of glutamate dehydrogenase from Pyrococcus furiosus, a hyperthermophilic archaebacterium
J. Protein Chem.
13
253-259
1994
Pyrococcus furiosus (P80319)
Manually annotated by BRENDA team
Yip, K.S.; Stillman, T.J.; Britton, K.L.; Artymiuk, P.J.; Baker, P.J.; Sedelnikova, S.E.; Engel, P.C., Pasquo, A.; Chiaraluce, R.; Consalvi, V.; et al.
The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
Structure
15
1147-1158
1995
Pyrococcus furiosus (P80319)
Manually annotated by BRENDA team
Britton, K.; Baker, P.; Borges, K.; Engel, P.; Pasquo, A.; Rice, D.; Robb, F.; Scandurra, R.; Stillman, T.; Yip, K.
Insights into thermal stability from a comparison of the glutamate dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis
Eur. J. Biochem.
229
688-695
1995
Pyrococcus furiosus (P80319), Thermococcus litoralis (Q56304), Thermococcus litoralis DSM 5473 (Q56304)
Manually annotated by BRENDA team
Lee, M.; Gonzlez, J.; Robb, F.
Extremely thermostable glutamate dehydrogenase (GDH) from the freshwater archaeon Thermococcus waiotapuensis Cloning and comparison with two marine hyperthermophilic GDHs
Extremophiles
6
151-159
2002
Pyrococcus furiosus (P80319), Thermococcus litoralis (Q56304), Thermococcus litoralis DSM 5473 (Q56304)
Manually annotated by BRENDA team
Adams, M.; Holden, J.; Menon, A.; Schut, G.; Grunden, A.; Hou, C.; Hutchins, A.; Jenney F.E., J.; Kim, C.; Ma, K.; Pan, G.; Roy, R.; Sapra, R.; Story, S.; Verhagen, M.
Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
Pyrococcus furiosus (P80319)
Manually annotated by BRENDA team