Information on EC 1.4.1.2 - glutamate dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
1.4.1.2
-
RECOMMENDED NAME
GeneOntology No.
glutamate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
formation of an enzyme-NAD-oxoglutarate dead end complex; fully ordered reaction mechanism; NAD+ binds first followed by L-glutamate
-
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
bi uni uni ping-pong addition sequence
-
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
partially random mechanism
-
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reductive amination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
4-aminobutyrate degradation V
-
alanine degradation II (to D-lactate)
-
Alanine, aspartate and glutamate metabolism
-
Arginine and proline metabolism
-
ethylene biosynthesis IV
-
glutamate degradation I
-
glutamate degradation V (via hydroxyglutarate)
-
Metabolic pathways
-
methylaspartate cycle
-
Nitrogen metabolism
-
Taurine and hypotaurine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NAD+ oxidoreductase (deaminating)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dehydrogenase, glutamate
-
-
-
-
GDH
-
-
-
-
GDH
P00366
-
GDH isoenzyme 1
-
-
GDH isoenzyme 1
-
-
GDH, NAD-dependent
Q977U6
-
GDH, NAD-dependent
Haloferax mediterranei R-4
Q977U6
-
-
GDH1
-
beta subunit
GDH1
-
isozyme
GDH1
Q67C43
-
GDH1
Q852M0
-
GDH2
-
alpha subunit
GDH2
-
isozyme
GDH2
Q67C42
-
GDH2
Q852M0
-
GDH3
Q852M0
-
GdhA
-
alpha subunit
GDHB
-
beta subunit
Glu dehydrogenase
-
-
GLUD1
B5AAK2
isozyme
GLUD1
B5AAK3
isozyme
GLUD1
-
isozyme
GLUD1
B5AAJ9
isozyme
GLUD1
B5AAK0
isozyme
GLUD1
B5AAK1
isozyme
GLUD2
-
isozyme
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
P00366
-
glutamate dehydrogenase
Q50JE9
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
Q0E5H9, Q0E5I0
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
Q852M0
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase (NAD)
-
-
-
-
glutamate dehydrogenase alpha subunit
Q67C43
-
glutamate dehydrogenase beta subunit
Q67C42
-
glutamate oxidoreductase
-
-
-
-
glutamic acid dehydrogenase
-
-
-
-
glutamic dehydrogenase
-
-
-
-
hGDH1
-
-
hGDH2-nerve-specific GDH
-
-
house-keeping GDH
-
-
L-glutamate dehydrogenase
-
-
-
-
L-glutamate dehydrogenase
-
-
NAD(+)-dependent glutamate dehydrogenase
Q9TVN3
-
NAD(H)-dependent glutamate dehydrogenase
-
-
NAD(H)-dependent glutamate dehydrogenase
Q67C42, Q67C43
-
NAD(H)-dependent glutamate dehydrogenase
-
-
NAD+-dependant glutamate dehydrogenase
A0R1C2
-
NAD+-dependent GDH
-
-
NAD+-dependent GDH
-
-
NAD+-dependent GDH
-
-
NAD+-dependent GDH
-
-
NAD+-dependent GDH
-
-
-
NAD+-dependent GDHX
P29051
-
NAD+-dependent GDHX
Halobacterium salinarum NRC-36014
P29051
-
-
NAD+-dependent GluDH
-
-
NAD+-dependent glutamate dehydrogenase
-
-
NAD+-dependent glutamate dehydrogenase
-
-
NAD+-dependent glutamate dehydrogenase
P29051
-
NAD+-dependent glutamate dehydrogenase
Halobacterium salinarum NRC-36014
P29051
-
-
NAD+-dependent glutamate dehydrogenase
-
-
NAD+-GDH
A0R1C2
-
NAD+-glutamate dehydrogenase
-
-
NAD+-specific GDH
-
-
NAD+-specific glutamate dehydrogenase
P282997
-
NAD-dependent glutamate dehydrogenase
-
-
-
-
NAD-dependent glutamate dehydrogenase
-
-
NAD-dependent glutamate dehydrogenase
A5LH94
-
NAD-dependent glutamate dehydrogenase
-
-
NAD-dependent glutamic dehydrogenase
-
-
-
-
NAD-dependent L-glutamate dehydrogenase
A5LH94
-
NAD-dependent L-glutamate dehydrogenase
Janthinobacterium lividum UTB1302
A5LH94
-
-
NAD-GDH
-
-
-
-
NAD-GDH
Aspergillus niger NCIM 565
-
-
-
NAD-GDH
-
-
NAD-GDH
Q977U6
-
NAD-GDH
Haloferax mediterranei R-4
Q977U6
-
-
NAD-GDH
Janthinobacterium lividum UTB1302
A5LH94
-
-
NAD-glutamate dehydrogenase
-
-
-
-
NAD-glutamate dehydrogenase
-
-
NAD-glutamate dehydrogenase
Aspergillus niger NCIM 565
-
-
-
NAD-glutamate dehydrogenase
-
-
NAD-glutamate dehydrogenase
Q977U6
-
NAD-glutamate dehydrogenase
Haloferax mediterranei R-4
Q977U6
-
-
NAD-linked glutamate dehydrogenase
-
-
-
-
NAD-linked glutamic dehydrogenase
-
-
-
-
NAD-specific glutamate dehydrogenase
-
-
-
-
NAD-specific glutamic dehydrogenase
-
-
-
-
NAD:glutamate oxidoreductase
-
-
-
-
NADH-dependent GDH
-
-
NADH-dependent glutamate dehydrogenase
-
-
-
-
NADH-dependent glutamate dehydrogenase
-
-
NADH-dependent glutamate dehydrogenase
-
-
NADH-GDH
-
-
NADH-GDH
Q5BU42, Q5BU43, Q5BU44, Q5QDM6
-
NADH-GDH
-
-
NADH-GDH
Solanum lycopersicum Micro-Tom
-
-
-
NADH-glutamate dehydrogenase
-
-
NADH-linked glutamate dehydrogenase
-
-
-
-
OsGDH1
-
-
OsGDH2
-
-
OsGDH3
-
-
Pcal_1031
-
gene name
Pcal_1031
-
gene name
-
Surface-associated protein PGAG1
-
-
-
-
L-glutamate dehydrogenase
-
-
-
additional information
A0R1C2
NAD+-specific glutamate dehydrogenases belongs to the L_180 class, that is affected by the binding of a small protein, GarA
CAS REGISTRY NUMBER
COMMENTARY
9001-46-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Achlya sp.
-
-
-
Manually annotated by BRENDA team
Apodachlya sp.
-
-
-
Manually annotated by BRENDA team
genes GDH1-3
-
-
Manually annotated by BRENDA team
three genes GDH1, GDH2, and GDH3 encoding the enzyme subunits
-
-
Manually annotated by BRENDA team
strain NCIM 565
-
-
Manually annotated by BRENDA team
Aspergillus niger NCIM 565
strain NCIM 565
-
-
Manually annotated by BRENDA team
strain DSM 31
-
-
Manually annotated by BRENDA team
strain ISW1214
Uniprot
Manually annotated by BRENDA team
Bacillus subtilis ISW1214
strain ISW1214
Uniprot
Manually annotated by BRENDA team
two enzymes GDHA and GDHB
-
-
Manually annotated by BRENDA team
cultivar Bronowski
-
-
Manually annotated by BRENDA team
GDH isoenzymes 1 and 7, genes GDH1 and GDH2 encoding subunits alpha and beta
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
Clostridium botulinum 113B
113B
-
-
Manually annotated by BRENDA team
Clostridium difficile
-
-
-
Manually annotated by BRENDA team
Clostridium sp. SB4
SB4
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
strain DSMZ 2266T
SwissProt
Manually annotated by BRENDA team
the sequence has errornously been assigned as NADP+-dependent glutamate dehydrogenase in Benachenhou, N., Baldacci, G.: Mol. Gen. Genet, 230, 345-352 (1991)
SwissProt
Manually annotated by BRENDA team
Halobacterium salinarum NRC-36014
-
SwissProt
Manually annotated by BRENDA team
strain R4 (ATCC 33500)
SwissProt
Manually annotated by BRENDA team
Haloferax mediterranei R-4
strain R4 (ATCC 33500)
SwissProt
Manually annotated by BRENDA team
fragment; strain UTB1302
UniProt
Manually annotated by BRENDA team
Janthinobacterium lividum UTB1302
fragment; strain UTB1302
UniProt
Manually annotated by BRENDA team
European yellow lupine
UniProt
Manually annotated by BRENDA team
fragment; European yellow lupine
UniProt
Manually annotated by BRENDA team
glutamate dehydrogenase 1, fragment; European yellow lupine
UniProt
Manually annotated by BRENDA team
glutamate dehydrogenase 2, fragment; European yellow lupine
UniProt
Manually annotated by BRENDA team
gene msmeg_4699
UniProt
Manually annotated by BRENDA team
cv. Xanthi XHFD8 and cv. Xanthi G28
-
-
Manually annotated by BRENDA team
line A63-H
-
-
Manually annotated by BRENDA team
transgenic tobacco lines S4-H and S49-H, lines A63-NS and S49-NS as isogenic controls
-
-
Manually annotated by BRENDA team
var.Ti68, sense lines S4, S49 and S77 and antisense lines A44, A62, A63, A68 and A69
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
; four putative GDH genes (OsGDH1-4) are present in the rice genome. The GDH sequences from rice and other species can be classified into two types (I and II). OsGDH1-3 belong to type II genes, whereas OsGDH4 belong to type I like gene
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
Scots pine
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
strain TAD1
-
-
Manually annotated by BRENDA team
TAD 1, two enzymes
-
-
Manually annotated by BRENDA team
strain TAD1
-
-
Manually annotated by BRENDA team
gene pcal_1031
-
-
Manually annotated by BRENDA team
three genes encoding the alpha-subunit, Slgdh-NAD;A1-3, and one additional gene encoding the beta-subunit of GDH, Slgdh-NAD;B1
-
-
Manually annotated by BRENDA team
Solanum lycopersicum Micro-Tom
three genes encoding the alpha-subunit, Slgdh-NAD;A1-3, and one additional gene encoding the beta-subunit of GDH, Slgdh-NAD;B1
-
-
Manually annotated by BRENDA team
Sulfolobus solfataricus MT-4
-
-
-
Manually annotated by BRENDA team
fragment; also named Symphalangus syndactylus
UniProt
Manually annotated by BRENDA team
PCC 6803
-
-
Manually annotated by BRENDA team
strain HB8
-
-
Manually annotated by BRENDA team
cultivar Yumai 34
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the family of amino acid dehydrogenases
evolution
-
NAD+-dependent, NADP+-dependent and dual-specificity GDHs, EC 1.4.1.2-1.4.1.4 are closely related and a few site-directed mutations can reverse specificity, overview. Specificity for NAD+ or for NADP+ has probably emerged repeatedly during evolution, using different structural solutions on different occasions. an acidic P7 residue usually hydrogen bonds to the 2'- and 3'-hydroxyls, may permit binding of NAD+ only, NADP+ only, or in higher animals both
malfunction
-
a gdh1-2-3 triple mutant exhibits major differences to the wild-type in gene transcription and metabolite concentrations, and these differences appear to originate in the roots, metabolic profile of the gdh1-2-3 triple mutant, overview
malfunction
-
when one or two of the three root isoenzymes are missing from the mutants, the remaining isoenzymes compensate for this deficiency
metabolism
A0R1C2
NAD+-GDH plays an important role in nitrogen assimilation rather than glutamate catabolism, and is involved in the additional nitrogen assimilatory pathway via glutamate dehydrogenase, GDH. The specific activity of the deaminating NAD+-GDH reaction is mostly independent of nitrogen availability, overview, overview
physiological function
-
glucose deprivation in SF-188 cells results in an enhanced GDH activity. This results from the loss of glycolysis. Inhibition of Akt signaling, which facilitates glycolysis, increases GDH activity whereas overexpression of Akt suppresses it. Suppression of GDH activity with RNA interference or an inhibitor shows that the enzyme is dispensable in cells able to metabolize glucose but is required for cells to survive impairments of glycolysis brought about by glucose deprivation, 2-deoxyglucose, or Akt inhibition. Inhibition of GDH converts these glutamine-addicted SF-188 cells to glucose-addicted cells
physiological function
-
transgenic mice, betaGlud1-/-, are generated bearing a beta-cell-specific GDH deletion. In situ pancreatic perfusion reveals that glucose-stimulated insulin secretion is reduced by 37% in transgenic mice. Isolated islets with either constitutive or acute adenovirus-mediated knock-out of GDH show a 49 and 38% reduction in glucose-induced insulin release, respectively. Adenovirus-mediated re-expression of GDH in transgenic mice fully restores glucose-induced insulin release. In transgenic mice reduced secretory capacity results in lower plasma insulin levels in response to both feeding and glucose load, while body weight gain is preserved
physiological function
-
GDH enzymes of 19 Streptococcus suis serotype 2 strains, consisting of 18 swine isolates and 1 human clinical isolate from a geographically varied collection, are analyzed by activity staining on a nondenaturing gel. DNA sequences contain base pair differences, but most are silent. Cluster analysis of the deduced amino acid sequences separated the isolates into three groups (ETI, ETII, ETIII). Gene exchange studies results in the change of ETI to ETII and vice versa. A spectrophotometric activity assay for GDH do not show significant differences between the groups
physiological function
-
sucrose starvation of lupine embryos leads to a rapid increase in the specific activity of GDH, immunoreactive beta-polypeptide and it is accompanied by appearance of new cathodal isoforms of enzyme, suggesting that isoenzymes induced in lupine embryos by sucrose starvation combine into GDH hexamers with the predominance of beta-GDH subunits synthetized under GDH1 gene control, treatment of cultivated embryos with 0.01 mM Cd2+ or Pb2+ results in ammonium accumulation in the tissues, accompanied by an increase in anabolic activity of GDH and activity of anodal isoenzymes
physiological function
-
transgenic tobacco plants overexpressing the two genes encoding the enzyme are generated. Using an in vivo real time 15 N-nuclear magnetic resonance (NMR) spectroscopy approach it is shown that, when the two GDH genes are overexpressed individually or simultaneously, the transgenic plant leaves do not synthesize glutamate in the presence of NH4+ when glutamine synthetase is inhibited. When the two GDH unlabeled substrates ammonium and glutamate are provided simultaneously with either (15N) glutamate or 15NH4+ respectively, it is found that the ammonium released from the deamination of glutamate is reassimilated by the enzyme glutamine synthase, suggesting the occurrence of a futile cycle recycling both ammonium and glutamate
physiological function
-
a quantitative genetic study for elucidating the contribution of glutamine synthetase, glutamate dehydrogenase and other nitrogen-related physiological traits to the agronomic performance of common wheat is performed. A total of 148 quantitative trait loci are detected, 26 are detected for GDH activity spread over 13 chromosomes. A coincidence between a quantitative trait loci for GDH activity and a gene encoding GDH is also found on chromosome 2B
physiological function
-
complex regulatory behaviour in mammalian GDH, involving negative co-operativity in coenzyme binding. Main heterotropic regulators are ADP and GTP, and ADP is a fragment of the coenzyme. NAD(H) mediates homotropic interaction via heterotropic sites or conversely, ADP uses homotropic coenzyme sites
physiological function
-
CsGDH lacks the regulation by ADP and GTP seen in bovine GDH
physiological function
-
complex regulatory behaviour in mammalian GDH, involving negative co-operativity in coenzyme binding. Main heterotropic regulators are ADP and GTP, and ADP is a fragment of the coenzyme. NAD(H) mediates homotropic interaction via heterotropic sites or conversely, ADP uses homotropic coenzyme sites
physiological function
-
Gdh2p plays an evident role during aerobic glutamate metabolism
physiological function
-
isozyme GDH7 does not support net amination in vivo and the increase in GDH7 activity might be a response to oxidative stress during protoplast isolation
physiological function
-
the main physiological function of NADH-GDH is to provide 2-oxoglutarate for the tricarboxylic acid cycle. Differences in key metabolites of the tricarboxylic acid cycle in the triple mutant versus the wild-type indicate that, through metabolic processes operating mainly in roots, there is a strong impact on amino acid accumulation, in particular alanine, gamma-aminobutyrate, and aspartate in both roots and leaves, phenotypes, overview
metabolism
-
together with glutamine synthetase, the glutamate synthase, i.e. enzyme GOGAT, EC 1.4.1.14, offers the same net reaction as GDH, but with a much lower Km for ammonia, and driven by the splitting of ATP
additional information
-
Trp243 is located in the active-site cleft. Neither Trp64 nor Trp449 are strictly required for pH-dependent inactivation
additional information
-
structure-activity relationship, modeling, comparison to other hyperthermophilic enzymes from Pyrococcus furiosus and Thermococcus litoralis, overview
additional information
-
at position 242, P6 of the core fingerprint, where NAD+- and NADP+-dependent enzymes normally have Gly or Ala, respectively, clostridial GDH already has Ala. Replacement with Gly produced negligible shift in coenzyme specificity
additional information
-
the production of monoclonal antibodies against purified glutamate dehydrogenase from Sulfolobus solfataricus is performed with the aim to study the structure-function and evolutionary relationships between various types of glutamate dehydrogenases
additional information
-
the level of GDH alpha- and beta-subunits in tomato plants is regulated differently in each tomato organ
additional information
P282997
each polypeptide consists of an N-terminal substrate-binding (domain I) followed by a C-terminal cofactor-binding segment (domain II). The reaction takes place at the junction of the two domains, which move as rigid bodies and are presumed to narrow the cleft during catalysis. Critical glutamate at the P7 position of the core fingerprint with a role in NAD+ binding, mutational and isothermal titration calorimetry studies, overview
additional information
-
in clostridial GDH, which shows a remarkable discrimination (20000-80000fold) in favour of NAD+, the P6 residue, which should be Gly, is in fact Ala. Not only this, but the critical P7 residue is Gly instead of Asp or Glu
additional information
-
GDH from Peptoniphilus asaccharolyticus obeys the rules with Gly at P6 and Glu at P7
additional information
-
the isoenzyme profile in leaves changes on wounding, the change in GDH isoenzyme profile has no effect on ammonium assimilation. Protoplast isolation changes the redox state with NAD(P)H and oxidized glutathione levels increasing, and ascorbate, dehydroascorbate, NAD(P)+ and glutathione decreasing. ATP content in protoplasts declines to 2.6% of that in leaves, while that in wounded leaves increases by twofold
additional information
Solanum lycopersicum Micro-Tom
-
the level of GDH alpha- and beta-subunits in tomato plants is regulated differently in each tomato organ
-
additional information
Sulfolobus solfataricus MT-4
-
the production of monoclonal antibodies against purified glutamate dehydrogenase from Sulfolobus solfataricus is performed with the aim to study the structure-function and evolutionary relationships between various types of glutamate dehydrogenases
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxo-3-methylvalerate + NADPH + NH3
L-isoleucine + NADP+ + H2O
show the reaction diagram
-
very low specificity of wild-type
-
-
-
2-oxo-iso-caproate + NADPH + NH3
L-norleucine + NADP+ + H2O
show the reaction diagram
-
very low specificity of wild-type
-
-
-
2-oxo-iso-valerate + NADPH + NH3
L-leucine + NADP+ + H2O
show the reaction diagram
-
low specificity of wild-type
-
-
-
2-oxobutyrate + NADPH + NH3
2-aminobutyrate + NAD+ + H2O
show the reaction diagram
P39633
faint specificity
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
show the reaction diagram
P39633
-
-
-
r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
show the reaction diagram
-, Q9TVN3
-
-
-
r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
show the reaction diagram
-
2fold increase in NADH-dependent GDH aminating activity 28 days after flowering
-
-
r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
wild-type enzyme highly specific for 2-oxoglutarate
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
Clostridium difficile
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-, Q67C42, Q67C43
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-, Q977U6
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
in conjugation with glutamine synthase, the glutamate dehydrogenase plays a major role in controlling the translocation of organic carbon and nitrogen metabolites in both vegetative and reproductive organs. It is possible that the presence of glutamate dehydrogenase in multivesicular bodies within the flower receptacle is important for the recycling of carbon and nitrogen molecules in senescing tissues in which the enzyme is generally induced
-
-
?
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
no significant activity of deamination reaction
-
-
ir
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
Haloferax mediterranei R-4
Q977U6
-
-
-
r
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
P39633
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
Achlya sp.
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-, Q9TVN3
-
-
-
-
beta-phenylpyruvate + NADPH + NH3
L-phenylalanine + NADP+ + H2O
show the reaction diagram
-
low specificity of wild-type
-
-
-
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
show the reaction diagram
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
show the reaction diagram
Q50JE9
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
ir
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
-
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
-
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
Clostridium difficile
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
P24295
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
Apodachlya sp., Achlya sp.
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
P29051
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-, Q977U6
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
Q5BU42, Q5BU43, Q5BU44, Q5QDM6
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
B5AAK2
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
B5AAJ9
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
B5AAK3
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
B5AAK0
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
B5AAK1
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
A5LH94, -
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
P28997
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
P282997
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
strict substrate specificity
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
glutamate oxidation is favoured
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
control point for amino acid metabolism
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
primary role in squid mantle muscle is in regulating the catabolism of amino acids for energy production
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
the enzyme may be linked to oxygen through an electron-transport system
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
RocG is exclusively devoted to L-glutamate degradation rather than to its synthesis
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
A0R1C2
reaction cycle, specificities of forward and reverse reactions, overview, reaction cycle, overview
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
the amination reaction is preferred
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
Sulfolobus solfataricus MT-4
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
Solanum lycopersicum Micro-Tom
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
Clostridium botulinum 113B
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
Halobacterium salinarum NRC-36014
P29051
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
Aspergillus niger NCIM 565
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
Clostridium sp. SB4
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
Haloferax mediterranei R-4
Q977U6
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
show the reaction diagram
A5LH94, -
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
show the reaction diagram
Janthinobacterium lividum UTB1302
A5LH94
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
weak reaction
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
show the reaction diagram
-
-
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
show the reaction diagram
-, P29051
-
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
show the reaction diagram
P00366
-
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
show the reaction diagram
-
-
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
show the reaction diagram
-
progressive decrease in NAD-GDH deaminating activity from flowering to maturity
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
show the reaction diagram
-
at 40% the rate
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
show the reaction diagram
-
deamination at 5% the rate of L-glutamate deamination
-
-
?
L-norvaline + H2O + NAD+
oxopentanoate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
oxaloacetate + NADPH + NH3
L-aspartate + NADP+ + H2O
show the reaction diagram
P39633
faint specificity
-
-
?
oxaloacetate + NADPH + NH3
L-aspartate + NADP+ + H2O
show the reaction diagram
-
very low specificity of wild-type
-
-
-
p-hydroxyphenylpyruvate + NADPH + NH3
L-tyrosine + NADP+ + H2O
show the reaction diagram
-
very low specificity of wild-type
-
-
-
pyruvate + NADPH + NH3
L-alanine + NADP+ + H2O
show the reaction diagram
P39633
faint specificity
-
-
?
pyruvate + NADPH + NH3
L-alanine + NADP+ + H2O
show the reaction diagram
-
very low specificity of wild-type
-
-
-
L-serine + H2O + NAD+
3-hydroxy-2-oxopropanoate + NH3 + NADH
show the reaction diagram
-
deamination at 29% the rate of L-glutamate deamination
-
-
?
additional information
?
-
-
L-alpha-amino-gamma-nitroaminobutyrate deamination at 0.5% the rate of deamination of L-glutamate
-
-
?
additional information
?
-
P39633
no activity with L-aspartate, L-alanine, L-valine and L-serine
-
-
-
additional information
?
-
-
no specificity of wild-type for 2-ketohexonoate
-
-
-
additional information
?
-
-
RocG is able to bind to and concomitantly inactivate the activator protein GltC
-
-
-
additional information
?
-
A5LH94, -
inert reaction with L-glutamine, L-aspartate, L-alanine, L-leucine, L-valine, L-lysine, L-2-aminobutyrate, L-methionine, L-ornithine, L-phenylalanine, L-arginine, L-tryptophan, L-methionine, L-histidine, D-glutamate, and D-aspartate, the enzyme is not active with NADP+
-
-
-
additional information
?
-
-
in yeast, NADP+-dependent enzymes, EC 1.4.1.4, encoded by GDH1 and GDH3, are reported to synthesize glutamate from 2-oxtoglutarate, while an NAD+-dependent enzyme, EC 1.4.1.2, encoded by GDH2, catalyzes the reverse reaction. Gdh1p is the primary GDH enzyme and Gdh2p and Gdh3p play evident roles during aerobic glutamate metabolism
-
-
-
additional information
?
-
-
no or poor activity with NADP+/NADPH in both reaction directions. The enzyme also shows low activity with L-norvaline, L-2-aminobutyrate, L-valine, L-isoleucine, and L-leucine as substrates for oxidative deamination, and with 2-oxovalerate, 2-oxobutyrate, and 2-oxocaproate, for reducive amination, substrate specificity, overview. No activity with L-2-aminobutyrate, L-valine, L-isoleucine, L-leucine, L-glutamine, L-alanine, L-aspartate, L-cysteine, L-serine, L-lysine, L-phenylalanine, and L-tryptophan, or with 2-oxoisocaproate and pyruvate
-
-
-
additional information
?
-
Janthinobacterium lividum UTB1302
A5LH94
inert reaction with L-glutamine, L-aspartate, L-alanine, L-leucine, L-valine, L-lysine, L-2-aminobutyrate, L-methionine, L-ornithine, L-phenylalanine, L-arginine, L-tryptophan, L-methionine, L-histidine, D-glutamate, and D-aspartate, the enzyme is not active with NADP+
-
-
-
additional information
?
-
-
no or poor activity with NADP+/NADPH in both reaction directions. The enzyme also shows low activity with L-norvaline, L-2-aminobutyrate, L-valine, L-isoleucine, and L-leucine as substrates for oxidative deamination, and with 2-oxovalerate, 2-oxobutyrate, and 2-oxocaproate, for reducive amination, substrate specificity, overview. No activity with L-2-aminobutyrate, L-valine, L-isoleucine, L-leucine, L-glutamine, L-alanine, L-aspartate, L-cysteine, L-serine, L-lysine, L-phenylalanine, and L-tryptophan, or with 2-oxoisocaproate and pyruvate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
in conjugation with glutamine synthase, the glutamate dehydrogenase plays a major role in controlling the translocation of organic carbon and nitrogen metabolites in both vegetative and reproductive organs. It is possible that the presence of glutamate dehydrogenase in multivesicular bodies within the flower receptacle is important for the recycling of carbon and nitrogen molecules in senescing tissues in which the enzyme is generally induced
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
ir
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
P29051
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
A5LH94, -
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
P28997
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
P282997
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
control point for amino acid metabolism
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
primary role in squid mantle muscle is in regulating the catabolism of amino acids for energy production
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
the enzyme may be linked to oxygen through an electron-transport system
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
A0R1C2
reaction cycle, specificities of forward and reverse reactions, overview
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
Solanum lycopersicum Micro-Tom
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
Halobacterium salinarum NRC-36014
P29051
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
in yeast, NADP+-dependent enzymes, EC 1.4.1.4, encoded by GDH1 and GDH3, are reported to synthesize glutamate from 2-oxtoglutarate, while an NAD+-dependent enzyme, EC 1.4.1.2, encoded by GDH2, catalyzes the reverse reaction. Gdh1p is the primary GDH enzyme and Gdh2p and Gdh3p play evident roles during aerobic glutamate metabolism
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD(P)+
Q50JE9
-
NAD+
Clostridium difficile
-
-
NAD+
-
no activity with NADP+
NAD+
-
highly specific for. The ratio for turnover number to Km-value is 405 times greater than for NADP+
NAD+
-
protects against targeting the Cys320 in the active site by 5,5'-dithiobis(2-nitrobenzoate)
NAD+
A5LH94, -
dependent
NAD+
A0R1C2
specific for
NAD+
-
the core fingerprint for coenzyme binding is the conserved sequence Gly-X-Gly-X-X-Gly, which consists of residues that form a hydrophobic core between the beta-strands and the alpha-helix, and glycine residues that allow for a tight turn between the first beta-strand and the following alpha-helix. In all these enzymes, the last residue in helix alphaA has to be a Gly, the first Gly of the consensus, because any larger residue would interfere with the adenine ribose. Coenzyme binding structure, overview
NADH
-
no aminating activity either in presence of NADH or NADPH
NADH
-
no activity with NADPH
NADH
-
the ratio for turnover number to Km-value is 1000fold greater than for NADPH
NADH
P39633
does not prevent heat inactivation
NADH
-
gradual increase in enzyme activity with increasing concentrations of NADH in preparations with 0.1 mM Hg or without Hg
NADH
-
strong preference (1170fold) for NADH over NADPH
NADH
-
the wild-type enzyme displays negative NAD+ cooperativity at pH 7 and pH 9 values
NADH
-
OsGDH1 contains an NADH-specific motif; OsGDH2 gene contains an NADH-specific motif; OsGDH3 gene contains an NADH-specific motif
NADH
-
preferred coenzyme compared to NADP+
NADH
A0R1C2
specific for
NADH
-
the core fingerprint for coenzyme binding is the conserved sequence Gly-X-Gly-X-X-Gly, which consists of residues that form a hydrophobic core between the beta-strands and the alpha-helix, and glycine residues that allow for a tight turn between the first beta-strand and the following alpha-helix. In all these enzymes, the last residue in helix alphaA has to be a Gly, the first Gly of the consensus, because any larger residue would interfere with the adenine ribose. Coenzyme binding structure, overview
NADH
-
highly preferred cofactor
NADP+
-
less than 1% of the activity with NAD+
NADP+
-
about 4% of the activity with NAD+
NADP+
-
highly specific for NAD+. The ratio for turnover number to Km-value for NAD+ is 405 times greater than for NADP+
NADPH
-
can replace NADH only at pH 6, not at pH 7-10
NADPH
-
rate with NADPH is 300times lower than with NADH
NADPH
-
activity with NADH, NADPH and NAD+ in the ratio 126:2:1
NADPH
-
less than 1% of the activity with NADH
NADPH
-
with NADPH less than 10% of the activity with NADH
NADPH
-
about 4% of the activity with NADH
NADPH
-
the ratio for turnover number to Km-value for NADH is 1000fold greater than that for NADPH
acetyl-NAD+
-
-
additional information
-
no activity with NADPH and NADP+
-
additional information
-, Q977U6
no activity with NADPH
-
additional information
P28997
NADP+ and NADPH are poor cofactors. The presence of an acidic residue at the P7 position, adjacent to the 2'-OH group, typically discriminates against NADP+. PaGDH contains a P7 glutamate and has high specificity for NAD(H), with a kcat/Km for NAD+ that is approximately 1000fold greater than that for NADP+
-
additional information
-
in the wild-type enzyme there is a strong pH dependence in the level of discrimination between NADH and NADPH
-
additional information
P282997
cofactor recognition and differentiation method, three-dimensional cofactor binding structure, modelling, detailed overview
-
additional information
-
when NAD+ is replaced by NADP+, the GDH activity in the wild-type occurs only some specific homohexamer and heterohexamers with very low level
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Al3+
-
enhances increase in GDH activity due to Hg
betaine
P29051
high concentrations of salt may be substituted with 30% DMSO or betaine with good stability and activity
Ca2+
-
activation of reductive amination; slight inhibition of oxidative deamination
Ca2+
-
activation of amination, no effect on deamination
Ca2+
-
required
Ca2+
-
activation of partially purified enzyme
Ca2+
-
amination is stimulated, deamination not influenced
Ca2+
-
activation
Ca2+
-
activation
Ca2+
-
activation
Ca2+
-, Q852M0
a putative EF-hand loop motif, which binds Ca2+ in the GDH2 and GDH3 proteins, but absent in GDH1
Cd2+
-
increases both GDH aminating and deaminating activity, accumulating in roots and shoots of seedlings not only increases GDH activity, but also modifies its coenzymatic specificity
Hg2+
-
increases NADH-GDH activity substantially, however, specific activity of the enzyme decreases at lower concentration of Hg, and increases to lesser extent at higher concentration of Hg
KCl
-, Q977U6
activity with KCl slightly higher than with NaCl
Mg2+
-
stimulation
Na+
-
after 5 days of NaCl treatments, the leaf NADH-GDH activity shows 22.58% and 105.37% enhancements at 150 and 300 mM NaCl, respectively
NaCl
-, Q977U6
-
NaCl
-
22.58% and 105.37% enhancements of NADH-GDH activity at 150 and 300 mM NaCl, respectively
NH4+
-, Q9TVN3
transcriptional upregulation
Zn2+
-
activation of reductive amination
Zn2+
-
can replace Ca2+, requirement
Mn2+
-
activation of reductive amination
additional information
-, Q9TVN3
high K+ concentrations up to 0.45 M have no influence on activity
additional information
Q0E5H9, Q0E5I0
gdh-1 expression is not influenced by the salinity of the medium, no measurable glutamate dehydrogenase activity in cells grown in G10 mineral medium at various salinities; gdh-2 expression is very low at every salt concentration tested, no measurable glutamate dehydrogenase activity in cells grown in G10 mineral medium at various salinities
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-Methyleneglutarate
-
potent competitive inhibitor
2-oxoglutarate
A5LH94, -
substrate inhibition
3,3'-[(2-bromobenzene-1,4-diyl)di(E)ethene-2,1-diyl]bis(6-hydroxybenzoic acid)
-
i.e. BSB
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
P00366
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
-
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
ADP
Clostridium difficile
-
-
Al3+
-
inhibits the enzyme activity in the absence of Hg
Al3+
-
as increasing the Al3+ concentration, the activity of GDH is firstly inhibited (at less than 0.03 mM), then activated (0.03-0.08 mM), and finally inhibited (above 0.08 mM) in the Tris-HCl buffer solution at pH 6.5 and 7.5
alpha,gamma-Diethyl glutamate
-
-
alpha-ketoglutarate
-
-
AMP
Clostridium difficile
-
-
ATP/GTP-competitive inhibitor of casein kinase-2
-
-
-
aurintricarboxylic acid
-
-
Bithionol
-
-
Bithionol
P00366
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits
Bithionol
-
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits
Ca2+
-
activation of reductive amination; slight inhibition of oxidative deamination
Ca2+
-
activation of reductive amination; no effect on oxidative deamination
Calmidazolium
-
-
citrate
-
inhibition of amination, no effect on deamination
citrate
A5LH94, -
67% activity in the presence of 10 mM citrate
Co2+
A5LH94, -
82% activity in the presence of 1 mM Co2+
D-asparagine
A5LH94, -
93% activity in the presence of 10 mM D-asparagine
D-Aspartate
A5LH94, -
90% activity in the presence of 10 mM D-aspartate
D-glutamate
A5LH94, -
94% activity in the presence of 10 mM D-glutamate
D-glutamine
A5LH94, -
95% activity in the presence of 10 mM D-glutamine
Diethylstilbestrol
-
-
DTNB
-
inactivation via blocking of the only two Cys residues, Cys144 in helix alpha7a of domain I, the substrate-binding domain, and Cys320 in a loop that connects betak and alpha13 in domain II, the coenzyme-binding domain
epicatechin
-
-
epicatechin-3-monogallate
-
-
epicatechin-monogallate
-
-
epigallocatechin
-
-
epigallocatechin-3,5-digallate
-
-
epigallocatechin-3-gallate
-
-
erythrosin B
-
-
ethaverine hydrochloride
-
-
fumarate
-
amination
fumarate
A5LH94, -
32% activity in the presence of 10 mM fumarate
Gallic acid
-
-
glutamate
-
amination
glutamine
-
amination
glutamine
-
reduces increase in GDH activity due to Hg
glutathione
-
reduces increase in GDH activity due to Hg
glycogen accumulation regulator
A0R1C2
GarA, native or unphosphorylated GarA is able to interact with NAD+-GDH causing a reduction in NAD+-GDH activity by altering the affinity of the enzyme for its substrate. This binding is prevented by the phosphorylation of GarA by PknG
-
guanidine hydrochloride
-
72C, almost complete loss of activity by addition of more than 3 M
GW-5074
-
-
Hexachlorophene
-
-
Hexachlorophene
P00366
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that hexachlorophene forms a ring around the internal cavity in GDH through aromatic stacking interactions between the drug and GDH as well as between the drug molecules themselves
Hexachlorophene
-
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that hexachlorophene forms a ring around the internal cavity in GDH through aromatic stacking interactions between the drug and GDH as well as between the drug molecules themselves
Hg2+
A5LH94, -
no activity in the presence of 1 mM Hg2+
Isocitrate
A5LH94, -
49% activity in the presence of 10 mM isocitrate
Isophthalate
-
-
Isophthalate
-
potent in vitro inhibitor
Isophthalic acid
-
-
KCl
-
3 M, 75% inhibition
L-glutamate
A5LH94, -
substrate inhibition at L-glutamate concentrations above 20 mM
L-glutamine
A5LH94, -
89% activity in the presence of 10 mM L-glutamine
L-ornithine
A5LH94, -
83% activity in the presence of 10 mM L-ornithine
leoidin
-
-
malate
A5LH94, -
65% activity in the presence of 10 mM malate
metergoline
-
-
Mg2+
A5LH94, -
64% activity in the presence of 1 mM Mg2+
N-acetylglutamate
-
-
N-alpha-p-tosyl-L-lysine chloromethyl ketone
-
TLCK
N-carbamylglutamate
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-methylglutamate
-
-
NaCl
-
3 M, 89% inhibition
NADPH
-
the wrong cofactor, NADPH, without the correct binding pocket to receive its 2'-phosphate, finds an alternative and catalytically unproductive way of occupying the coenzyme site
Ni2+
A5LH94, -
77% activity in the presence of 1 mM Ni2+
oxaloacetate
-
amination
p-Aminomercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
phosphoenolpyruvate
-
weak
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
Pyruvic acid
-
-
succinate
A5LH94, -
36% activity in the presence of 10 mM succinate
suloctidil
-
-
thiol reagents
-
-
Mn2+
A5LH94, -
52% activity in the presence of 1 mM Mn2+
additional information
-
strong inhibition by increasing ionic strength
-
additional information
-
no inhibition or activation in the presence of 500 mM AMP, ADP, ATP, cyclic-AMP, GMP, GDP or GTP
-
additional information
-
increase in GDH activity due to Hg remains unaffected by the supply of sucrose
-
additional information
-
Met sulfoximine and azaserine do not affect the aminating and deaminating activities of GDH
-
additional information
A5LH94, -
not inhibited by NAD+
-
additional information
-
no inhibition by GTP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetonitrile
-
activates
ADP
-
absolute requirement as cofactor
ADP
-
absolute requirement as cofactor; stimulation
ADP
-
activates in presence of 3 M NaCl or 3 M KCl. Inhibition in absence of salts
ADP
-
ADP can reverse inhibition
Al3+
-
GDH is activated at 0.03-0.08 mM in the Tris-HCl buffer solution at pH 6.5 and 7.5
alkalized extract
-
from the tuber of Corydalis ternata, activates the hGDH1 up to 3.2fold and hGDH2 up to 4.1fold, hGDH2 is more sensitively affected by 1 mM ADP than hGDH1 on the activation by alkalized extracts
-
alkalized extract
-
from the tuber of Corydalis ternata, increases GDH activity 2.4fold after one year of feeding
-
AMP
-
stimulation
asparagine
-
activates
aspartate
-
activates
ATP
-
activates in presence of 3 M NaCl or 3 M Kcl, slight activation in absence of salts
D-Arginine
A5LH94, -
212% activity in the presence of 10 mM D-arginine
DMSO
P29051
activates
ethylene
-
increase in the expression of GDH and the aminating GDH activity
ethylene
-
induces protein expression
glycerol
P29051
activates at 10%
guanidine hydrochloride
-
activates
H2O2
-
increase in the aminating GDH activity correlating with gene expression, in a dose-dependent manner
heating
-
at 90C the activity of the recombinant enzyme increases to a level comparable to that of the native enzyme
-
jasmonic acid
-
increase in the expression of GDH and the aminating GDH activity
jasmonic acid
-
5 mM, induces protein expression
jasmonic acid
-
-
L-arginine
A5LH94, -
936% activity in the presence of 10 mM L-arginine
L-asparagine
A5LH94, -
118% activity in the presence of 10 mM L-asparagine
L-aspartate
A5LH94, -
1735% activity in the presence of 10 mM L-aspartate
L-aspartate
A5LH94, -
catalytic activator, 2fold activation at 0.1 mM, effect on enzyme kinetics, overview
L-cysteine
-
stimulates deamination
L-His
-
activates in presence of 3 M NaCl, 3 M Kcl or in absence of salts
L-histidine
A5LH94, -
155% activity in the presence of 10 mM L-histidine
L-Leu
-
activates in presence of 3 M NaCl, 3 M Kcl or in absence of salts
L-lysine
A5LH94, -
161% activity in the presence of 10 mM L-lysine
L-methionine
A5LH94, -
206% activity in the presence of 10 mM L-methionine
L-tryptophan
A5LH94, -
235% activity in the presence of 10 mM L-tryptophan
NaCl
-
high NaCl induces the formation of reactive oxygen species, which in turn induces the synthesis of the alpha-subunit of GDH
NaNO3
-, Q852M0
GDH1 transcripts slightly and slowly increase by 2fold after N nutrition addition while GDH2 mRNA is not affected
NH3
-
GDH is activated by excess ammonia
NH4Cl
-, Q852M0
rapid and marked increase in the accumulation of mRNAs for GDH1 and GDH2 after supply
NH4NO3
-
increases the NADH-GDH activity in the presence of Hg
protopine
-
activates the human GDH isozymes, but to a less extent
protopine
-
increases GDH activity 1.6fold
salicylic acid
-
increase in the expression of GDH
salicylic acid
-
induces protein expression
salicylic acid
-
-
tetrahydrofuran
-
activates
Urea
-
72C, maximal enhancement at 2 mM
Urea
-
at 5 M the activity of the recombinant enzyme increases to a level comparable to that of the native enzyme, urea-induced activation of recombinant GDH is irreversible
Urea
-
activates the enzyme irreversibly at 5 M
Zn2+
A5LH94, -
224% activity in the presence of 1 mM Zn2+
leucine
-
stimulation
additional information
-
no inhibition or activation in the presence of 500 mM AMP, ADP, ATP, cyclic-AMP, GMP, GDP or GTP
-
additional information
-
cryptogein and Onozuka R10 induce GDH expression, GDH activity is correlated with GDH expression and the GDH enzyme preferentially catalyses the aminating reaction; GDH mRNA accumulates preferentially in plants inoculated with the avirulent Pseudomonas syringae pv. syringae CFBP3077 (hrp+) and the virulent Pseudomonas syringae pv. tabaci CFBP1503 strains, induction of GDH expression by bacterial infection dependeds on the hrp- genotype, but not on the virulence/avirulence genotype; leaf GDH aminating-activity increases, whereas deaminating-activity is not affected by infection with viruses CMV, TEV, and PVY
-
additional information
Q67C42, Q67C43
prolonged dark-stress increases GDH activity, more likely due to resistance of the GDH protein to stress-induced proteolysis, rather than to post-translational up-regulation; prolonged dark-stress increases GDH activity, more likely due to resistance of the GDH protein to stress-induced proteolysis, rather than to post-translational up-regulation
-
additional information
-
no activation by ADP
-
additional information
-
the enzyme is activated by heat above 70C, urea and organic solvents, but not by salts. Activation of recombinant enzyme by urea and heat, that is purified as inactive enzyme at 4C
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0008
-
2-oxoglutarate
P29051
pH 8.5, 40C, recombinant enzyme in presence of DMSO
0.00111
-
2-oxoglutarate
-
animals treated with alkalized extract from the tuber of Corydalis ternata
0.00131
-
2-oxoglutarate
-
animals treated with protopine
0.00138
-
2-oxoglutarate
-
control group
0.0034
-
2-oxoglutarate
P29051
pH 8.5, 40C, recombinant enzyme
0.041
-
2-oxoglutarate
A5LH94, -
pH 6.5, 25C, recombinant enzyme, in presence of 10 mM L-aspartate
0.066
-
2-oxoglutarate
-
-
0.0862
-
2-oxoglutarate
-
mutant D165N
0.103
-
2-oxoglutarate
-
pH 7, 25C
0.125
-
2-oxoglutarate
-
wild-type
0.2
-
2-oxoglutarate
-
-
0.56
-
2-oxoglutarate
-
-
0.65
-
2-oxoglutarate
-
wild-type
0.65
-
2-oxoglutarate
P39633
wild-type
0.71
-
2-oxoglutarate
-, Q9TVN3
-
0.75
-
2-oxoglutarate
-
activated NAD-GDH
0.92
-
2-oxoglutarate
-
pH 9.5, 50C, recombinant enzyme
0.93
-
2-oxoglutarate
P39633
mutant E27F
1.22
-
2-oxoglutarate
P39633
mutant Q144R
1.35
-
2-oxoglutarate
-
-
1.7
-
2-oxoglutarate
-
-
1.9
-
2-oxoglutarate
-
non-activated NAD-GDH
2.36
-
2-oxoglutarate
-
NAD+-dependent enzyme
2.36
-
2-oxoglutarate
-
pH 8.0, 20C
2.85
-
2-oxoglutarate
-
wild-type CsGDH, Vmax: 546 micromol/min/mg, pH 8.0, 25C
3.3
-
2-oxoglutarate
Achlya sp.
-
-
3.3
-
2-oxoglutarate
-
-
3.4
-
2-oxoglutarate
-
-
4.6
-
2-oxoglutarate
-
-
5.6
-
2-oxoglutarate
-
pH 8.0
100
-
2-oxoglutarate
-
mutant M101S
285
-
2-oxoglutarate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 781 mM NH4Cl, Vmax: 2260 micromol/min/mg, pH 8.0, 25C
606
-
2-oxoglutarate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 1800 mM NH4Cl, Vmax: 200 micromol/min/mg, pH 8.0, 25C
5.82
-
glutamate
-
pH 7, 25C
7.4
-
glutamate
-
-
0.000011
-
L-glutamate
P29051
pH 9.0, 40C, recombinant enzyme
0.000025
-
L-glutamate
P29051
pH 9.0, 40C, recombinant enzyme in presence of DMSO
0.00299
-
L-glutamate
-
animals treated with protopine
0.00302
-
L-glutamate
-
animals treated with alkalized extract from the tuber of Corydalis ternata
0.00321
-
L-glutamate
-
control group
0.16
-
L-glutamate
-
native enzyme; recombinant, heat-activated enzyme
0.17
-
L-glutamate
-
-
0.18
-
L-glutamate
-
recombinant, urea-activated enzyme
0.24
-
L-glutamate
-
-
0.34
-
L-glutamate
P39633
wild-type
0.39
-
L-glutamate
P00366
0.009 mM inhibitor biothionol, Vmax: 0.05, pH 7.5
1.06
-
L-glutamate
P00366
0.005 mM inhibitor biothionol, Vmax: 0.1, pH 7.5
1.17
-
L-glutamate
P00366
0.003 mM inhibitor biothionol, Vmax: 0.14, pH 7.5
1.27
-
L-glutamate
P00366
0.008 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.05, pH 7.5
1.38
-
L-glutamate
P00366
0.0015 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.13, pH 7.5; without inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.17, pH 7.5
1.39
-
L-glutamate
-
wild-type CsGDH, Vmax: 47.1 micromol/min/mg, pH 8.0, 25C
1.4
-
L-glutamate
-
-
1.53
-
L-glutamate
P00366
0.004 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.09, pH 7.5
1.62
-
L-glutamate
P00366
without inhibitor biothionol, Vmax: 0.18, pH 7.5
2.66
-
L-glutamate
-
mutant D165N
3.1
-
L-glutamate
Achlya sp.
-
-
3.25
-
L-glutamate
-
mutant enzyme W393F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25C; wild type enzyme, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25C
3.3
-
L-glutamate
-
mutant enzyme W449F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25C
3.41
-
L-glutamate
-
mutant enzyme W64F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25C
3.7
5
L-glutamate
-
mutant enzyme W310F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25C
3.97
-
L-glutamate
-
wild-type
4.3
-
L-glutamate
Clostridium difficile
-
-
5.3
-
L-glutamate
-
pH 10.5, 50C, recombinant enzyme
5.5
-
L-glutamate
-
-
7.1
-
L-glutamate
A5LH94, -
in the presence of 5 mM NAD+, in 100 mM glycine/NaOH (pH 9.5), at 25C
18.2
-
L-glutamate
-
mutant enzyme W243F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25C
28.6
-
L-glutamate
-
NAD+-dependent enzyme
28.6
-
L-glutamate
-
pH 8.0, 20C
32.2
-
L-glutamate
-
-
37.1
-
L-glutamate
-
-
49
-
L-glutamate
-
-
98
-
L-glutamate
-, Q9TVN3
-
0.018
-
NAD+
-
recombinant, urea-activated enzyme
0.019
-
NAD+
-
native enzyme
0.021
-
NAD+
-
recombinant, heat-activated enzyme
0.028
-
NAD+
-
pH 10.5, 50C, recombinant enzyme
0.046
-
NAD+
-
-
0.076
-
NAD+
-
mutant D165N
0.08
-
NAD+
P39633
wild-type
0.112
-
NAD+
P29051
pH 9.0, 40C, recombinant enzyme in presence of DMSO
0.118
-
NAD+
P29051
pH 9.0, 40C, recombinant enzyme
0.125
-
NAD+
-
wild type enzyme, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25C
0.138
-
NAD+
-
mutant enzyme W393F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25C
0.14
-
NAD+
-
wild-type
0.14
-
NAD+
P00366
0.008 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.04, pH 7.5
0.168
-
NAD+
-
wild-type CsGDH, Vmax: 40.6 micromol/min/mg, pH 8.0, 25C
0.22
-
NAD+
-
mutant enzyme W449F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25C
0.23
-
NAD+
-
mutant enzyme W64F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25C
0.23
-
NAD+
P00366
0.0015 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.13, pH 7.5
0.26
-
NAD+
P00366
0.004 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.09, pH 7.5; 0.009 mM inhibitor biothionol, Vmax: 0.05, pH 7.5
0.28
-
NAD+
-
-
0.31
-
NAD+
P00366
without inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.24, pH 7.5; without inhibitor biothionol, Vmax: 0.24, pH 7.5
0.35
-
NAD+
-
mutant enzyme W310F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25C
0.36
-
NAD+
P00366
0.005 mM inhibitor biothionol, Vmax: 0.13, pH 7.5
0.4
-
NAD+
-
mutant enzyme W243F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25C
0.43
-
NAD+
P00366
0.003 mM inhibitor biothionol, Vmax: 0.22, pH 7.5
0.5
-
NAD+
-
NAD+-dependent enzyme
0.5
-
NAD+
-
pH 8.0, 20C
0.56
-
NAD+
-
-
0.61
-
NAD+
Achlya sp.
-
-
0.8
-
NAD+
Clostridium difficile
-
-
2.1
-
NAD+
A5LH94, -
in the presence of 20 mM L-glutamate, in 100 mM glycine/NaOH (pH 9.5), at 25C
0.001
-
NADH
-
pH 9.5, 50C, recombinant enzyme
0.0044
-
NADH
-
pH 7, 25C
0.0044
-
NADH
-
wild type enzyme, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.0056
-
NADH
-
mutant D165N
0.0076
-
NADH
-
mutant enzyme W244S, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.009
-
NADH
P29051
pH 8.5, 40C, recombinant enzyme in presence of DMSO
0.0108
-
NADH
-
wild-type
0.0123
-
NADH
-
mutant enzyme E243D, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.014
-
NADH
P29051
pH 8.5, 40C, recombinant enzyme
0.018
-
NADH
-
mutant enzyme D245K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.018
-
NADH
-
pH 6.0, 25C, mutant P262S
0.02
-
NADH
-
pH 7.0, 25C, recombinant wild-type enzyme
0.022
-
NADH
-
pH 6.0, 25C, mutant D263K
0.023
-
NADH
-
pH 7.0, 25C, mutant D263K
0.025
-
NADH
-
pH 7.0, 25C, mutant A242G
0.028
-
NADH
-
pH 6.0, 25C, mutant F238S
0.034
-
NADH
-
pH 6.0, 25C, mutant A242G
0.035
-
NADH
-
pH 7.0, 25C, mutant F238S/P262S
0.036
-
NADH
-
mutant enzyme E243K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.036
-
NADH
-
pH 6.0, 25C, recombinant wild-type enzyme
0.03609
-
NADH
-
control group
0.037
-
NADH
-
non-activated NAD-GDH
0.03785
-
NADH
-
animals treated with protopine
0.03833
-
NADH
-
animals treated with alkalized extract from the tuber of Corydalis ternata
0.0385
-
NADH
-
mutant enzyme E243R, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.04
-
NADH
-
pH 7.0, 25C, mutant F238S
0.047
-
NADH
-
pH 7.0, 25C, mutant P262S
0.048
-
NADH
-
pH 6.0, 25C, mutant F238S/P262S
0.055
-
NADH
Achlya sp.
-
-
0.055
-
NADH
-
wild-type CsGDH, Vmax: 285 micromol/min/mg, pH 8.0, 25C
0.07
-
NADH
-
wild-type
0.07
-
NADH
P39633
wild-type
0.078
-
NADH
-
pH 8.0, 25C, recombinant wild-type enzyme
0.085
-
NADH
-
pH 8.0, 25C, mutant A242G
0.089
-
NADH
-
-
0.09
-
NADH
-
activated NAD-GDH
0.091
-
NADH
-
mutant M101S
0.091
-
NADH
-
pH 8.0, 25C, mutant D263K
0.095
-
NADH
-
mutant G82K
0.14
-
NADH
-
-
0.142
-
NADH
-
pH 8.0, 25C, mutant P262S
0.16
-
NADH
P39633
mutant E27F
0.19
-
NADH
-
pH 8.0
0.204
-
NADH
-
pH 8.0, 25C, mutant F238S/P262S
0.23
-
NADH
-
pH 8.0, 25C, mutant F238S
0.41
-
NADH
P39633
mutant Q144R
42.5
-
NADH
-
-
0.163
-
NADP+
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 80.8 micromol/min/mg, pH 8.0, 25C
0.0384
-
NADPH
-
mutant enzyme E243R, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.053
-
NADPH
-
mutant enzyme E243K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.065
-
NADPH
-
-
0.238
-
NADPH
-
mutant enzyme D245K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.431
-
NADPH
-
mutant enzyme W244S, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.476
-
NADPH
-
mutant enzyme E243D, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.51
-
NADPH
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 2180 micromol/min/mg, pH 8.0, 25C
1.64
-
NADPH
-
wild type enzyme, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.00013
-
NH3
P29051
pH 8.5, 40C, recombinant enzyme in presence of DMSO
0.00035
-
NH3
P29051
pH 8.5, 40C, recombinant enzyme
9.8
-
NH3
-
pH 9.5, 50C, recombinant enzyme
24.6
-
NH3
-
pH 8.0, 20C
33.9
-
NH3
A5LH94, -
as NH4+, pH 6.5, 25C, recombinant enzyme, in absence of L-aspartate
300
-
NH3
-
pH 8.0
0.00528
-
NH4+
-
animals treated with alkalized extract from the tuber of Corydalis ternata
0.0054
-
NH4+
-
animals treated with protopine
0.00613
-
NH4+
-
control group
0.033
-
NH4+
-
for 200 mM NH4+
0.98
-
NH4+
-
-
2.33
-
NH4+
-, Q9TVN3
-
12.9
-
NH4+
-
wild-type CsGDH, Vmax: 307 micromol/min/mg, pH 8.0, 25C
22.8
-
NH4+
-
non-activated NAD-GDH
24.6
-
NH4+
-
NAD+-dependent enzyme
25.6
-
NH4+
-
activated NAD-GDH
26
-
NH4+
Achlya sp.
-
-
33.3
-
NH4+
-
-
49.4
-
NH4+
-
mutant D165N
52.3
-
NH4+
P39633
mutant E27F
55.6
-
NH4+
P39633
wild-type
56.8
-
NH4+
P39633
mutant Q144R
62.8
-
NH4+
-
wild-type
96
-
NH4+
-
from double-reciprocal plots for concentrations between 5 mM and 200 mM
304
-
NH4+
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 1960 micromol/min/mg, pH 8.0, 25C
2.27
-
oxaloacetate
-
mutant M101S
4.16
-
oxaloacetate
-
mutant G82K
1349
-
L-glutamate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 121.9 micromol/min/mg, pH 8.0, 25C
additional information
-
additional information
-
no significant changes in Km values between groups treated with alkalized extract from the tuber of Corydalis ternata or protopine and control groups
-
additional information
-
additional information
-
wild-type Vmax: 23.71 (pH 7), 35.16 (pH 9)
-
additional information
-
additional information
A5LH94, -
the enzyme shows positive cooperativity towards 2-oxoglutarate and NADH, and Michaelis-Menten type kinetics with ammonium chloride in the absence of catalytic activator L-aspartate. L-aspartate effect on enzyme kinetics, overview
-
additional information
-
additional information
-
dissociation constants of wild-type and mutant enzymes for different coenzymes, overview
-
additional information
-
additional information
-
cofactor kinetics, overview
-
additional information
-
additional information
-
cofactor kinetics, overview. Even without the heterotropic antenna responsible for allosteric regulation in mammalian enzymes, the GDH is emphatically still allosteric. The Eadie-Hofstee plot for NAD+ is strongly non-linear.Att pH 9.0 there is almost total positive co-operativity with glutamate, with a Hill coefficient close to the theoretical maximum of 6 for a hexamer
-
additional information
-
additional information
-
cofactor kinetics, overview
-
additional information
-
additional information
-
enzyme kinetics of wild-tyype and mutant enzymes with NADPH, overview
-
additional information
-
additional information
-
kinetics of recombinant wild-type and mutant enzymes with NADH/NAD+ and NADPH/NADP+, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.012
-
2-oxoglutarate
-
mutant M101S
0.013
-
2-oxoglutarate
-
mutant G82K
20.3
-
2-oxoglutarate
-
pH 7, 25C
46
-
2-oxoglutarate
P29051
pH 8.5, 40C, recombinant enzyme in presence of DMSO
56
-
2-oxoglutarate
P29051
pH 8.5, 40C, recombinant enzyme
65
-
2-oxoglutarate
-
pH 9.5, 50C, recombinant enzyme
342
-
2-oxoglutarate
P39633
wild-type
344
-
2-oxoglutarate
-
wild-type
344
-
2-oxoglutarate
P39633
mutant E27F
435
-
2-oxoglutarate
P39633
mutant Q144R, 1.3 times higher than that of the wild-type
6.7
-
glutamate
-
pH 7, 25C
17
-
L-glutamate
P29051
pH 9.0, 40C, recombinant enzyme in presence of DMSO
17
-
L-glutamate
-
pH 10.5, 50C, recombinant enzyme
18.1
-
L-glutamate
P39633
wild-type
24
-
L-glutamate
P29051
pH 9.0, 40C, recombinant enzyme
14
-
NAD+
-
pH 10.5, 50C, recombinant enzyme
15
-
NAD+
P29051
pH 9.0, 40C, recombinant enzyme in presence of DMSO
16
-
NAD+
P29051
pH 9.0, 40C, recombinant enzyme
1.71
-
NADH
-
mutant enzyme E243R, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
10.6
-
NADH
-
mutant enzyme E243K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
10.9
-
NADH
-
mutant enzyme W244S, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
11.2
-
NADH
-
pH 6.0, 25C, mutant A242G
13.6
-
NADH
-
pH 6.0, 25C, mutant F238S
13.9
-
NADH
-
pH 6.0, 25C, mutant F238S/P262S
14.4
-
NADH
-
pH 6.0, 25C, mutant P262S
14.6
-
NADH
-
pH 6.0, 25C, mutant D263K
16.4
-
NADH
-
mutant enzyme D245K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
16.9
-
NADH
-
mutant enzyme E243D, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
19.9
-
NADH
-
pH 6.0, 25C, recombinant wild-type enzyme
31.3
-
NADH
-
wild type enzyme, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
39
-
NADH
P29051
pH 8.5, 40C, recombinant enzyme
47
-
NADH
P29051
pH 8.5, 40C, recombinant enzyme in presence of DMSO
58
-
NADH
-
pH 9.5, 50C, recombinant enzyme
65.1
-
NADH
-
pH 7.0, 25C, mutant A242G
80
-
NADH
-
pH 7.0, 25C, mutant D263K
105
-
NADH
-
pH 7.0, 25C, mutant F238S/P262S
130.2
-
NADH
-
pH 7.0, 25C, recombinant wild-type enzyme
133
-
NADH
-
pH 8.0, 25C, mutant F238S/P262S
139
-
NADH
-
pH 7.0, 25C, mutant F238S
150
-
NADH
-
pH 8.0, 25C, mutant D263K
160
-
NADH
-
pH 7.0, 25C, mutant P262S
177
-
NADH
-
pH 8.0, 25C, mutant A242G
232
-
NADH
-
pH 8.0, 25C, recombinant wild-type enzyme
402
-
NADH
-
pH 8.0, 25C, mutant F238S
490
-
NADH
-
pH 8.0, 25C, mutant P262S
1.67
-
NADPH
-
mutant enzyme E243R, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
3
-
NADPH
-
mutant enzyme W244S, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
5.06
-
NADPH
-
mutant enzyme E243D, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
6
-
NADPH
-
mutant enzyme D245K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
10
-
NADPH
-
wild type enzyme, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
14.8
-
NADPH
-
mutant enzyme E243K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
58
-
NH3
-
pH 9.5, 50C, recombinant enzyme
84
-
NH3
P29051
pH 8.5, 40C, recombinant enzyme in presence of DMSO
85
-
NH3
P29051
pH 8.5, 40C, recombinant enzyme
3.45
-
oxaloacetate
-
mutant G82K
5.68
-
oxaloacetate
-
mutant M101S
additional information
-
oxaloacetate
-
mutant M101S
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
16.5
-
2-oxoglutarate
P29051
pH 8.5, 40C, recombinant enzyme
2883
57.5
-
2-oxoglutarate
P29051
pH 8.5, 40C, recombinant enzyme in presence of DMSO
2883
71
-
2-oxoglutarate
-
pH 9.5, 50C, recombinant enzyme
2883
0.0018
-
L-glutamate
P29051
pH 9.0, 40C, recombinant enzyme in presence of DMSO
12211
0.0035
-
L-glutamate
P29051
pH 9.0, 40C, recombinant enzyme
12211
3.2
-
L-glutamate
-
pH 10.5, 50C, recombinant enzyme
12211
0.29
-
NAD+
-
mutant F232S/P262S/D263K , pH and temperature not specified in the publication
14330
0.72
-
NAD+
P29051
pH 9.0, 40C, recombinant enzyme
14330
0.75
-
NAD+
P29051
pH 9.0, 40C, recombinant enzyme in presence of DMSO
14330
149
-
NAD+
-
wild-type enzyme, pH and temperature not specified in the publication
14330
500
-
NAD+
-
pH 10.5, 50C, recombinant enzyme
14330
1.7
-
NADH
P29051
pH 8.5, 40C, recombinant enzyme
14331
1.9
-
NADH
P29051
pH 8.5, 40C, recombinant enzyme in presence of DMSO
14331
289
-
NADH
-
pH 6.0, 25C, mutant F238S/P262S
14331
329
-
NADH
-
pH 6.0, 25C, mutant A242G
14331
369
-
NADH
-
mutant F232S/P262S/D263K , pH and temperature not specified in the publication
14331
485
-
NADH
-
pH 6.0, 25C, mutant F238S
14331
553
-
NADH
-
pH 6.0, 25C, recombinant wild-type enzyme
14331
655
-
NADH
-
pH 8.0, 25C, mutant F238S/P262S
14331
663
-
NADH
-
pH 6.0, 25C, mutant D263K
14331
800
-
NADH
-
pH 6.0, 25C, mutant P262S
14331
1648
-
NADH
-
pH 8.0, 25C, mutant D263K
14331
1747
-
NADH
-
pH 8.0, 25C, mutant F238S
14331
2082
-
NADH
-
pH 8.0, 25C, mutant A242G
14331
2604
-
NADH
-
pH 7.0, 25C, mutant A242G
14331
2974
-
NADH
-
pH 8.0, 25C, recombinant wild-type enzyme
14331
3000
-
NADH
-
pH 7.0, 25C, mutant F238S/P262S
14331
3404
-
NADH
-
pH 7.0, 25C, mutant P262S
14331
3450
-
NADH
-
pH 8.0, 25C, mutant P262S
14331
3475
-
NADH
-
pH 7.0, 25C, mutant F238S
14331
3478
-
NADH
-
pH 7.0, 25C, mutant D263K
14331
5800
-
NADH
-
pH 9.5, 50C, recombinant enzyme
14331
6500
-
NADH
-
pH 7.0, 25C, recombinant wild-type enzyme
14331
8110
-
NADH
-
wild-type enzyme, pH and temperature not specified in the publication
14331
5.9
-
NH3
-
pH 9.5, 50C, recombinant enzyme
14472
45
-
NH3
P29051
pH 8.5, 40C, recombinant enzyme
14472
115
-
NH3
P29051
pH 8.5, 40C, recombinant enzyme in presence of DMSO
14472
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
pseudo-first-order kinetic plots for inactivation of F238S GDH by DTNB, overview
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0064
-
3,3'-[(2-bromobenzene-1,4-diyl)di(E)ethene-2,1-diyl]bis(6-hydroxybenzoic acid)
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0015
-
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
P00366
pH 7.5
0.0026
-
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
-
pH 7.5
0.1
-
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
-
value above 100, pH 7.5
0.0158
-
ATP/GTP-competitive inhibitor of casein kinase-2
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
-
0.0012
-
aurintricarboxylic acid
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0037
-
BH3I-2
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0048
-
Bithionol
P00366
pH 7.5
0.0055
-
Bithionol
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0059
-
Bithionol
-
pH 7.5
0.017
-
Bithionol
-
pH 7.5
0.0077
-
Calmidazolium
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0017
-
Diethylstilbestrol
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0005
-
epicatechin-3-monogallate
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0005
-
epigallocatechin-3-monogallate
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.05
-
erythrosin B
-
IC50 above 0.05 mM, in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.08
-
Gallic acid
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0015
-
GW-5074
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0017
-
Hexachlorophene
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0019
-
Hexachlorophene
-
pH 7.5
0.0039
-
Hexachlorophene
P00366
pH 7.5
0.012
-
Hexachlorophene
-
pH 7.5
0.0328
-
metergoline
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0138
-
suloctidil
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0003
-
-
mutant D165N overexpressed at 8C
0.012
-
-
2-oxoglutarate, mutant M101K
0.014
-
-
2-oxoglutarate, mutant K80R
0.019
-
-
2-oxoglutarate, mutant G82R and M101S
0.026
-
-
2-oxoglutarate, mutant G82K
0.034
-
-
mutant D165N overexpressed at 37C
0.047
-
-
mutant D165N overexpressed at 23C
0.077
-
-, Q9TVN3
NADP-linked GDH activity
0.21
-
-
on L-aspartate, mutant M101S
0.29
-
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
0.32
-
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.33
-
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0; wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
0.34
-
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.35
-
-
control group
0.39
-
-
on L-aspartate, mutant G82K
0.49
-
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH using NAD+
0.5
-
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
0.51
-
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
0.55
-
-, Q9TVN3
-
0.57
-
-
with protopine
0.62
-
A5LH94, -
recombinant enzyme from crude cell extract, at 25C
0.73
-
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
0.77
-
-, Q9TVN3
NAD-linked GDH activity
0.84
-
-
with alkalized extract from the tuber of Corydalis ternata
0.87
-
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.9
-
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
0.97
-
-, Q9TVN3
in the presence of antibiotics and ammonia
1.12
-
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
1.14
-
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
1.23
-
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
1.32
-
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
1.47
-
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5; mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
1.53
-
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
1.83
-
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
2.16
-
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
2.26
-
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
2.3
-
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
2.98
-
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
3
-
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
3.05
-
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
3.1
-
A5LH94, -
purified recombinant enzyme, at 25C
3.27
-
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
3.41
-
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
3.51
-
-
native enzyme
3.54
-
-
recombinant, urea-activated enzyme
3.65
-
-
recombinant, heat-activated enzyme
3.82
-
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
4.1
-
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
4.93
-
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
5
-
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
5.2
-
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
5.8
-
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
6.52
-
P29051
recombinant enzyme in Haloferax volcanii, pH 8.5, 40C
6.78
-
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
7.2
-
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
9.01
-
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
9.6
-
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
9.8
-
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
11
-
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
12
-
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
12.5
-
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
15
-
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
17.6
-
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
19
-
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
19.7
-
-
in the absence of Hg and in the presence of 0.1 mM AlCl3
20
-
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
20.1
-
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
20.6
-
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
25
-
-
in the presence of 0.001 mM Hg and in the presence of NH4NO3
25.3
-
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
26.7
-
-
in the presence of 0.001 mM Hg
30
-
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
31.4
-
-
-
34
-
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
34.2
-
-
in the absence of Hg
35
-
P29051
recombinant enzyme purified from Haloferax volcanii, pH 8.5, 40C
38
-
-
GDH-I
50
-
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
52.9
-
-
in the absence of Hg and in the presence of 5 mM sucrose
54
-
-
GDH-II
54
-
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
54.6
-
-
in the presence of 0.01 mM Hg
56
-
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
56.5
-
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
58
-
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH using NADP+
58.6
-
-
in the absence of Hg and in the presence of 5 mM glutathione
59.4
-
-
in the absence of Hg and in the presence of 5 mM glutamine
62
-
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
65.8
-
-
in the absence of Hg and in the presence of NH4NO3
68
-
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
70.94
-
-
in the presence of 0.1 mM Hg and in the presence of 5 mM glutathione
72
-
-
in the presence of 0.01 mM Hg and in the presence of NH4NO3
89.3
-
-, Q977U6
purified recombinant enzyme
90
-
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
101.8
-
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
102
-
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
104
-
-
GDH II
104
-
-, Q977U6
purified native enzyme
119.5
-
-
in the presence of 0.1 mM Hg
146
-
Clostridium difficile
-
-
155
-
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
167
-
-
GDH I
170.6
-
-
in the presence of 0.1 mM Hg and in the presence of 5 mM glutamine
171.4
-
-
in the presence of 0.1 mM Hg and in the presence of 0.1 mM AlCl3
174
-
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
243.4
-
-
in the presence of 0.1 mM Hg and in the presence of NH4NO3
248
-
-
NAD+-dependent enzyme
286.4
-
-
-
328.2
-
-
in the presence of 0.1 mM Hg and in the presence of 5 mM sucrose
401
-
-
-
440
-
-
2-oxoglutarate, wild-type
540
-
-
-
1092
-
-
above
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
glucose withdrawal stimulates GDH activity
additional information
-
-
GDH activity is markedly increased in Pseudomonas fluorescens cultures exposed to menadione-containing media containing Arg, Glu and Pro. When NH4+ is utilized as the nitrogen source, both alpha-ketoglutarate dehydrogenase and GDH levels are diminished. These enzymatic profiles are reversed when control cells are incubated in menadione media
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
lowly activated anionic exchangers-epoxy-GDH is stable at pH 4 and 25C
6
8
-
assay at
6.5
-
A5LH94, -
reductive amination assay at
7
-
-, Q9TVN3
-
7
-
-
assay at, the wild-type enzyme displays negative NAD+ cooperativity at pH 7 and pH 9 values
7.3
7.5
-
reductive amination
7.3
-
P39633
optimal for 2-oxoglutarate amination
7.4
7.5
-
reductive amination
7.4
8.2
-
reductive amination
7.4
-
-
amination
7.5
-
P00366
assay at
7.7
-
-
reductive amination of 2-oxoglutarate
7.7
-
P39633
optimal for L-glutamate deamination
7.8
-
-
reductive amination
7.8
-
-
assay at
7.9
-
-
reductive amination
8
8.3
-
reductive amination
8
8.5
-
reductive amination
8
8.5
-, Q977U6
-
8
-
-
reductive amination
8
-
-
reductive amination
8
-
-
reductive amination
8
-
-
reductive amination
8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8.2
-
Apodachlya sp.
-
reductive amination
8.2
-
-
glutamate oxidation
8.2
-
-
reductive amination
8.4
-
-
reductive amination
8.4
-
-
forward reaction
8.5
9
-
reductive amination
8.5
-
Clostridium difficile
-
-
8.5
-
-
amination
8.5
-
P29051
amination
8.8
-
-
glutamate oxidation
8.8
-
-
oxidative deamination
8.8
-
-
deamination
8.8
-
-
reductive amination
9
-
Apodachlya sp.
-
glutamate oxidation
9
-
-
oxidative deamination
9
-
-
oxidative deamination
9
-
-
oxidative deamination
9
-
-
reverse reaction
9
-
A5LH94, -
in glycine-NaOH buffer at 40C
9
-
-
assay at, the wild-type enzyme displays negative NAD+ cooperativity at pH 7 and pH 9 values
9
-
P29051
deamination
9.2
-
-
oxidative deamination
9.2
-
-
oxidative deamination
9.2
-
-
oxidative deamination
9.3
-
-
oxidative deamination
9.4
-
-
glutamate oxidation
9.4
-
-
oxidative deamination of glutamate
9.5
10
-
oxidative deamination
9.5
-
-
oxidative deamination
9.5
-
-
reductive deamination
9.7
-
-
deamination
10.5
-
-
oxidative deamination
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.3
9.5
-, Q977U6
-
6.5
10.5
P29051
pH profile, overvew
6.9
8
P39633
-
7
8.8
-
about 50% of activity maximum at pH 7.0 and 8.8, reductive amination
7.5
10.5
-
-
7.5
9
-
about 65% of activity maximum at pH 7.5 and 9.0, reductive amination
7.9
8.5
-
about 90% of activity maximum at pH 7.9 and 8.5, reductive amination
8.4
10.1
-
50% of activity maximum at pH 8.4 and 10.1, oxidative deamination
8.4
9.2
-
about 90% of activity maximum at pH 8.4 and 9.2, oxidative deamination
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
NAD+-dependent enzyme
25
-
-
lowly activated anionic exchangers-epoxy-GDH is stable at pH 4 and 25C
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
A5LH94, -
reductive amination assay at
28
-
-
assay at
40
-
A5LH94, -
in glycine-NaOH buffer at pH 9.0
40
-
P29051
assay at
60
-
-, Q977U6
-
66
-
-
assay at
85
90
-
deamination
90
-
-
at pH 9.7
100
-
-
Pcal_1031 activity appreciably increases by incubating at temperatures up to 100C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
37
-
decreasing temperature results in much lower enzyme activity
10
43
-
10C: about 45% of maximal activity, 43C: about 75% of maximal activity
40
80
-
40C: about 50% of maximal activity, 80C: about 40% of maximal activity
40
90
P29051
temperature profile, overview
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
all GDH genes are expressed in the mitochondria of the root companion cells
Manually annotated by BRENDA team
Q50JE9
GDH, in both amination and deamination activities, gradually increases in the floret portion as storage progresses
Manually annotated by BRENDA team
-
phloem companion cells
Manually annotated by BRENDA team
-
GDH activity increases during the fruit ripening along with the content of free glutamate, the most abundant amino acid of ripe fruit involved in conferring the genuine tomato flavour. Only the active homohexamer of GDH beta-subunits is detected in roots while heterohexamers of GDH alpha- and beta-subunits are found in fruits. alpha-Subunit Slgdh-NAD;A1-3 transcripts are detected in all tomato tissues examined, showing the highest levels in mature green fruits, contrasting with beta-subunit Slgdh-NAD;B1 transcripts which are detected mainly in roots or in mature fruits when treated with glutamate, NaCl or salicylic acid
Manually annotated by BRENDA team
Solanum lycopersicum Micro-Tom
-
GDH activity increases during the fruit ripening along with the content of free glutamate, the most abundant amino acid of ripe fruit involved in conferring the genuine tomato flavour. Only the active homohexamer of GDH beta-subunits is detected in roots while heterohexamers of GDH alpha- and beta-subunits are found in fruits. alpha-Subunit Slgdh-NAD;A1-3 transcripts are detected in all tomato tissues examined, showing the highest levels in mature green fruits, contrasting with beta-subunit Slgdh-NAD;B1 transcripts which are detected mainly in roots or in mature fruits when treated with glutamate, NaCl or salicylic acid
-
Manually annotated by BRENDA team
-
specificly expressed
Manually annotated by BRENDA team
-
medulla, cortex
Manually annotated by BRENDA team
-
phloem companion cells
Manually annotated by BRENDA team
-
both GDH aminating activity and protein content are strongly induced in senescing flag leaves
Manually annotated by BRENDA team
Q67C42, Q67C43
; GDH activity is increased in homozygotes of sense lines and reduced in antisense line A63-H
Manually annotated by BRENDA team
-
the isoenzyme profile in leaves changes on wounding
Manually annotated by BRENDA team
Solanum lycopersicum Micro-Tom
-
-
-
Manually annotated by BRENDA team
Q5BU42, Q5BU43, Q5BU44, Q5QDM6
-
Manually annotated by BRENDA team
-, Q852M0
GDH detected in the region of the apical meristem and cortical cells in the tip region and elongation zone of the roots in both untreated and NH4Cl-treated plants, GDH3 barely detectable in leaf blades, leaf sheaths, spikelets and roots
Manually annotated by BRENDA team
Q67C42, Q67C43
GDH activity is increased in homozygotes of sense lines and reduced in antisense line A63-H; in A63-H lines the alpha-subunit level is unaffected as compared to controls
Manually annotated by BRENDA team
-
only the active homohexamer of GDH beta-subunits is detected in roots while heterohexamers of GDH alpha- and beta-subunits are found in fruits. alpha-Subunit Slgdh-NAD;A1-3 transcripts are detected in all tomato tissues examined, showing the highest levels in mature green fruits, contrasting with beta-subunit Slgdh-NAD;B1 transcripts which are detected mainly in roots or in mature fruits when treated with glutamate, NaCl or salicylic acid
Manually annotated by BRENDA team
-
DH3 is only active in roots
Manually annotated by BRENDA team
-
three root isoenzymes
Manually annotated by BRENDA team
Solanum lycopersicum Micro-Tom
-
only the active homohexamer of GDH beta-subunits is detected in roots while heterohexamers of GDH alpha- and beta-subunits are found in fruits. alpha-Subunit Slgdh-NAD;A1-3 transcripts are detected in all tomato tissues examined, showing the highest levels in mature green fruits, contrasting with beta-subunit Slgdh-NAD;B1 transcripts which are detected mainly in roots or in mature fruits when treated with glutamate, NaCl or salicylic acid
-
Manually annotated by BRENDA team
Q5BU42, Q5BU43, Q5BU44, Q5QDM6
-
Manually annotated by BRENDA team
-
specificly expressed
Manually annotated by BRENDA team
additional information
-
absent from mesophyll section
Manually annotated by BRENDA team
additional information
Q50JE9
branchlet, GDH, in both amination and deamination activities, decreases in the branchlets as storage progresses
Manually annotated by BRENDA team
additional information
-
ubiquitously expressed in various tissues
Manually annotated by BRENDA team
additional information
-
subunit distributin and expression patterns in tissues of tomato, overview. The level of GDH alpha- and beta-subunits in tomato plants is regulated differently in each tomato organ
Manually annotated by BRENDA team
additional information
-
in the wild-type, the specific activity of NADH-GDH is over 10times higher in the roots compared with that measured in the leaves
Manually annotated by BRENDA team
additional information
-
GDH3 is expressed only in the root companion cells, whereas the two others GDH1 and GDH2 are expressed in the same companion cells in both roots and shoots, tissue GDH isoenzyme composition, overview. The alpha, beta, and gamma polypeptides, that comprise the enzyme, can be assembled into a complex combination of heterohexamers in roots
Manually annotated by BRENDA team
additional information
Solanum lycopersicum Micro-Tom
-
subunit distributin and expression patterns in tissues of tomato, overview. The level of GDH alpha- and beta-subunits in tomato plants is regulated differently in each tomato organ
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
some labelling in the cytosol of the phloem companion cells of senescing flag leaves
Manually annotated by BRENDA team
-
bound to cytoplasmic membrane
Manually annotated by BRENDA team
-
preferentially localized in the mitochondria of phloem companion cells in both leaves and flowers
Manually annotated by BRENDA team
-
in mature flag leaves, GDH is localized in the mitochondria of the phloem companion cells, increases in senescensing flag leaves
Manually annotated by BRENDA team
-
GLUD2 is specifically targeted to mitochondria, whereas GLUD1 is localized in mitochondria and cytoplasm
Manually annotated by BRENDA team
-
four GDH deduced amino acid sequences possess the predicted mitochondrial target peptides, 18 amino acid residues at the N-terminus
Manually annotated by BRENDA team
Solanum lycopersicum Micro-Tom
-
four GDH deduced amino acid sequences possess the predicted mitochondrial target peptides, 18 amino acid residues at the N-terminus
-
Manually annotated by BRENDA team
-
within the flower receptacle, significant amounts of enzyme
Manually annotated by BRENDA team
-
isozyme GDH7 predominates
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45000
-
-
SDS-PAGE
46000
-
-
SDS-PAGE
48000
-
-, Q9TVN3
sequence analysis
87000
-
-
F187D mutant, gel filtration
98000
-
-
gel filtration
110000
130000
-
sucrose density gradient sedimentation
165000
175000
-
GDHA, gel filtration
180000
-
-
gel filtration
210000
250000
-
sucrose density gradient sedimentation
210000
-
-
gel filtration
220000
-
-
gel filtration
225000
-
Achlya sp., Pythium debaryanum
-
sucrose density gradient sedimentation
226000
-
-
gel filtration
230000
-
-
gel filtration
230000
-
-
sedimentation equilibrium analysis
240000
250000
-
GDH B, gel filtration
250000
-
-
gel filtration
250800
-
-
gel filtration
252000
-
-
gel filtration
260000
-
-
gel filtration
266000
-
-
gel filtration
268000
282000
-
sedimentation equilibrium
270000
-
-
gel filtration
270000
-
-
gel filtration
270000
-
-
gel filtration
270000
-
P39633
gel filtration
280000
-
-
recombinant enzyme, gel filtration
284000
-
-
gel filtration
286000
-
-
gel filtration, tagged recombinant enzyme
289000
-
-
gel filtration
290000
-
-
gel filtration
290000
-
-, Q977U6
recombinant NAD-GDH
295000
-
-
gel filtration
299000
-
-
recombinant, heat-activated enzyme, gel filtration
300000
-
Clostridium difficile
-
gel filtration
300000
-
-
NAD+-dependent enzyme, gel filtration
300000
-
-
gel filtration
310000
-
-
gel filtration
310000
-
-, Q977U6
wild-type NAD-GDH
330000
-
-
amino acid data
330000
-
-
non-denaturing PAGE
337000
-
-
recombinant, urea-activated enzyme, gel filtration
350000
390000
-
gel filtration
356000
-
-
gel filtration
380000
-
-
gel filtration
460000
-
-
sedimentation equilibrium
470000
-
-
gel filtration
474000
-
-
gel filtration
480000
-
-
sedimentation equilibrium analysis
670000
-
-
gel filtration
1100000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q977U6
x * 54000, SDS-PAGE, x * 47950, sequence analysis
?
Haloferax mediterranei R-4
-
x * 54000, SDS-PAGE, x * 47950, sequence analysis
-
dimer
-
2 * 54000, SDS-PAGE
dimer
-
F187D mutant, 2 * 47000
dimer
-
NAD+-dependent enzyme, 2 * 160000, SDS-PAGE
dimer
-
2 * 160000, SDS-PAGE
dimer
-
2 * 160000, SDS-PAGE
-
heterohexamer
-
the alpha, beta, and gamma polypeptides, that comprise the enzyme, can be assembled into a complex combination of heterohexamers in roots
hexamer
-
6 * 48500, SDS-PAGE
hexamer
-
6 * 45000, SDS-PAGE
hexamer
-
6 * 54000, SDS-PAGE
hexamer
-
6 * 51500, SDS-PAGE
hexamer
-
6 * 42500, SDS-PAGE
hexamer
-
6 * 42500, SDS-PAGE
hexamer
Clostridium difficile
-
6 * 45000, SDS-PAGE
hexamer
-
6 * 48000, SDS-PAGE
hexamer
-
6 * 42000, SDS-PAGE
hexamer
-
6 * 43000, SDS-PAGE
hexamer
-
6 * 48000, SDS-PAGE
hexamer
-
6 * 183000, SDS-PAGE
hexamer
-
6 * 45000, SDS-PAGE
hexamer
-
6 * 36000, SDS-PAGE
hexamer
-
6 * 57500, SDS-PAGE
hexamer
-
6 * 40000, SDS-PAGE
hexamer
P39633
6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis
hexamer
-
x-ray crystallography
hexamer
-
native PAGE
hexamer
-
6 * 47000, SDS-PAGE
hexamer
-
6 * 48200, tagged recombinant enzyme, SDS-PAGE
hexamer
P282997
each polypeptide consists of an N-terminal domain I that adopts an alpha/beta fold with 5 (mixed) beta-strands sandwiched between alpha-helices on both sides. The C-terminal NAD(P)+ binding domain II consists of a modified Rossmann fold with one of the beta-strands in the reverse orientation
hexamer
-
4 * 48000, about, SDS-PAGE
hexamer
-
(alphabeta)3
hexamer
Clostridium botulinum 113B
-
6 * 42500, SDS-PAGE
-
hexamer
-
6 * 48200, tagged recombinant enzyme, SDS-PAGE
-
hexamer or pentamer
-
5 * or 6 * 49000, SDS-PAGE
homohexamer
A5LH94, -
6 * 169360, deduced from amino acid sequence; 6 * 170000, SDS-PAGE
homohexamer
Janthinobacterium lividum UTB1302
-
6 * 169360, deduced from amino acid sequence; 6 * 170000, SDS-PAGE
-
tetramer
-
4 * 45000, SDS-PAGE
tetramer
-
4 * 116000, sedimentation equilibrium analysis after treatment with 6 M guanidine HCl and 0.5% mercaptoethanol
tetramer
-
4 * 58500, SDS-PAGE
tetramer
-
4 * 116000, SDS-PAGE
tetramer
-
4 * 116000, SDS-PAGE
tetramer
-
4 * 116000, SDS-PAGE
homotrimer
-
method not specified
additional information
-
-
additional information
-
three-dimensional structure and structure-activity relationship, modeling, comparison to other hyperthermophilic enzymes from Pyrococcus furiosus and Thermococcus litoralis, overview
additional information
-
structure modelling of cofactor-bound enzyme, overview
additional information
-
GDH1 gene encodes a polypeptide subunit termed beta and GDH2 gene encodes alpha and the polypeptides can be assembled as homo- or heterohexamers composed of different ratios of alpha and beta, leading to the formation of seven active isoenzymes, complex pattern of isoenzymes, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nitrosylation
-
results reveal both hemin-H2O2-NO2 and 3-morpholinosydnonimine hydrochloride can cause inactivation of GDH through protein oxidation and tyrosine nitration, the impact of the effect of protein oxidation (not thiol oxidation) on enzyme activity is stronger than that of protein tyrosine nitration. Mass spectrometric analysis indicate that nitrated tyrosine residues by hemin-H2O2-NO2 are Tyr262 and Tyr471 while by 3-morpholinosydnonimine hydrochloride are Tyr401 and Tyr493
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
co-crystallization of GDH with hexachlorophene and 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one is performed using the hanging drop, vapor-diffusion method at room temperature. In both cases, the drops are formed using a 1:1 mix of protein and reservoir solutions
P00366
crystal structure determination and analysis
-
native apo-enzyme, poor quality of native crystals is resolved by derivatization with selenomethionine, X-ray diffraction structure determination and analysis at 2.94 A resolution, single-wavelength anomalous diffraction methods
P282997
purified recombinant wild-type and SeMet-labeled GDHs, hanging drop vapour diffusion method, at 20C, protein in 10 mM Tris-HCl, pH 7.0, mixing of 0.002 ml of protein solution with 0.001 ml of reservoir solution containing 2.0 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.5, 200 mM NaCl, and equilibration with 0.5 ml reservoir solution, X-ray diffraction structure determination and analysis at 3.5 A resolution
P28997
3D structure determined by X-ray diffraction method, refined at a resolution of 2.9 A with a crystallographic R-factor of 19.9%. Crystals belonging to the space group P2(1)2(1)2(1) are grown in hanging drops in which 0.005 ml NAD+ is equilibrated against a reservoir containing 24% v/v polyethylene glycol monomethylether 550, 100 mM NaCl and 100 mM Tris-HCl
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
10.5
-
Pcal_1031 retains more than 80% of its activity after incubation for 30 min at pH 4.0-10.5 at 50C
4
-
-
15 min, 30C, inactivation
6.5
7.2
-
15 min, 30C, stable
7
-
-
the wild type enzyme shows pH-dependent inactivation and conformational change and loses 91% of its activity over a few min on transfer from pH 7.0 to pH 8.8
8
-
-
15 min, 30C, inactivation
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
4
-
complete inactivation
20
25
-
no activity in cell extracts prepared at 0 to 4C, high activities between 20C and 25C, 70% activity is retained after 2 h at 0C in the presence of 20% glycerol
30
-
-
about 45% loss of activity after 15 min, about 60% loss of activity after 30 min
40
50
A5LH94, -
the enzyme is stable for 10 min at temperatures up to 40C but is completely inactivated by incubation for 10 min at 50C
40
70
P29051
recombinant purified enzyme, fully stable at 40C
40
-
-
about 60% loss of activity after 5 min, about 80% loss of activity after 15 min
41
-
P39633
50% of its activity remains after incubation of the wild-type enzyme for 20 min
50
-
-
6 min, complete loss of activity
50
-
-
the wild-type GDH retains only approximately 48% of starting activity after incubation at 50C for 30 min in potassium phosphate (pH 7.0), mutant enzymes W243F and W449F show slightly enhanced stability, retaining approximately 5% more activity over the 30 min period, mutants W310F and W393F show greater stabilization retaining 78% and 82% of their activities, respectively, W64F retains only 37% activity after 30 min
55
-
-
half-life: 60 min
65
-
-
20 min, 50% loss of activity
70
-
-
10 min, 40% loss of activity
72
-
-
half-life: 410 min
75
-
-
15 min, complete inactivation
78
-
-
half-life: 50 min
80
-
-
10 min, complete inactivation
80
-
P29051
recombinant purified enzyme, 30 min, 88% remaining
82
-
-
half-life: 30 min
85
-
-
120 min, 50% activity loss
90
-
P29051
recombinant purified enzyme, 30 min, 56% remaining
100
-
-
no loss of activity after 2 h
100
-
-
pH 7.2, 120 min, stable
105
-
-
Pcal_1031retains full activity after incubation for 10 min at temperatures up to 105C
additional information
-
-
the enzyme shows extremely high temperature stability, molecular mechanism and comparison to other hyperthermophilic enzymes from Pyrococcus furiosus and Thermococcus litoralis, overview
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
extremely unstable at 0C to 4C due to the dissociation of the holoenzyme into catalytically inactive subunits
-
the enzyme resists proteolysis by trypsin, chymotrypsin or endoproteinase Glu-C at 25C. Above 30C the enzyme became cleavable by chymotrypsin, at a single site. Proteolysis is accompanied by the loss of enzyme activity. Proteolysis is prevented by either of the substrates 2-oxoglutarate or L-glutamate but not by the coenzymes NAD+ or NADH
-
the enzyme resists proteolysis by trypsin, chymotrypsin or endoproteinase Glu-C at 25C. Above 30C the enzyme becomes cleavable by chymotrypsin, at a single site. Proteolysis is accompanied by the loss of enzyme activity. Proteolysis is prevented by either of the substrates 2-oxoglutarate or L-glutamate but not by the coenzymes NAD+ or NADH
-
guanidine hydrochloride, 1.0 M, complete denaturation
-
ammonium sulfate improves stability
-
2-oxoglutarate stabilizes
-
ADP stabilizes
-
NADH stabilizes
-
DTT stabilizes
-
isophthalate stabilizes
-
NaCl, 0.1 M, stabilizes
-
potassium phosphate buffer, high concentration, stabilizes
-
presence of sulfhydryl groups in the environment stabilizes
-
strong dependence on high salt concentrations for stability
-
repeated freezing and thawing: loss of activity
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-propanol
P29051
GDHX retains 33% activity in 10% after 72 h, pH 8.5, room temperature. GDHX loses 94% of activity within 3 days in 10% solution
Acetone
P29051
GDHX retains 38% activity in 10% after 72 h, pH 8.5, room temperature
Acetone
Halobacterium salinarum NRC-36014
-
GDHX retains 38% activity in 10% after 72 h, pH 8.5, room temperature
-
acetonitrile
P29051
GDHX retains 30% activity in 10% after 72 h, pH 8.5, room temperature
acetonitrile
Halobacterium salinarum NRC-36014
-
GDHX retains 30% activity in 10% after 72 h, pH 8.5, room temperature
-
dimethylformamide
P29051
51% activity remaining after 72 h, pH 8.5, room temperature; GDHX retains 73% activity in 10% DMF after 30 min at pH 8.5, 40C, and 51% after 72 h, pH 8.5, room temperature
DMSO
P29051
GDHX retains 100% activity in the aqueous DMSO mixtures, high concentrations of salt may be substituted with 30% DMSO or betaine with good stability and activity
Ethanol
P29051
GDHX retains 34% activity in 10% after 72 h, pH 8.5, room temperature
Ethanol
Halobacterium salinarum NRC-36014
-
GDHX retains 34% activity in 10% after 72 h, pH 8.5, room temperature
-
Glycerol
P29051
GDHX retains 73% activity in 10% glycerol after 72 h, pH 8.5, room temperature
Glycerol
Halobacterium salinarum NRC-36014
-
GDHX retains 73% activity in 10% glycerol after 72 h, pH 8.5, room temperature
-
Methanol
P29051
GDHX retains more than 73% activity in 10% after 72 h, pH 8.5, room temperature
Methanol
Halobacterium salinarum NRC-36014
-
GDHX retains more than 73% activity in 10% after 72 h, pH 8.5, room temperature
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4-5C, 0.066 M phosphate buffer, pH 7.4 or 0.01 M arginine buffer, pH 9.5, 20 days, stable
-
-20C, loss of activity overnight
-
4C, 3 days, stable
-
-15C, 50 mM Tris-HCl, pH 7.5, 0.1 M KCl, stable for several months
Clostridium difficile
-
-20C, up to 1 year, stable
-
-20C, gradual loss of activity
-
4C, suspension of 50% saturated ammonium sulfate, 0.1 mM DTT, 25 mM glutamate, stable for months
-
4C, more than 90% of original activity retained after 20 days
-
-20C, several months
-
-5C, 20% loss of activity after 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DEAE-Sephacel column chromatography
-
NAD-GDH is best obtained from proline grown Aspergillus niger mycelia
-
18-22C, 20% glycerol, heat treatment, ammonium sulfate, gel filtration, ion-exchange chromatography
-
2 isoenzymes GDHA, GDHB
-
Ni2+ HiTrap chelating column chromatography
-
to homogeneity
-
to homogeneity, about 39fold
P39633
overexpression of GDHB in Escherichia coli
-
GDH I and II
-
DEAE-cellulose column chromatography and Super-Q Toyopearl column chromatography
-
overexpression in Escherichia coli
Clostridium difficile
-
gel filtration
-
overexpression of F187D mutant in Escherichia coli
-
recombinant wild-type and mutant enzymes by affinity chromatography purification, followed by gel filtration
-
recombinant wild-type and mutant enzymes from Escherichia coli strain XL1-Blue
-
Remazol-Red column chromatography
-
to homogeneity
-
using dye-affintiy chromatography and anion-exchange chromatography
-
activated and non-activated form
-
recombinant soluble enzyme 11.3fold from Haloferax volcanii strain DS70, by hydrophobic interaction and anion exchange chromatography, method optimization
P29051
gel filtration, native enzyme 232fold purified, recombinant enzyme 5.4fold purified
-, Q977U6
to homogeneity
-
DEAE-Toyopearl column chromatography, butyl-Toyopearl column chromatography, and Superdex 200 gel filtration
A5LH94, -
recombinant enzyme from Escherichia coli TOP10 cells by hydrophobic interaction chromatography
A5LH94, -
4 isoenzymes
-
2 isoenzymes: GDH-I and GDH-II
-
by sonication and centrifugation
-, Q852M0
Q sepharose column chromatography
-
recombinant enzyme
-
NAD+-dependent and NADP+-dependent GDH
-
recombinant N-terminally Met-Ala-Ser-tagged and C-terminally His6-tagged enzyme from Eschericia coli strain Rosetta(DE3) by affinity chromatography and gel filtration
-
inactivate recombinant enzyme expressed from Escherichia coli by affinity and anion exchange chromatography, followed by gel filtrration, activation by 5 M urea and 70c
-
overexpression in Escherichia coli
-
overexpression of mutants in Escherichia coli
-
GDH is readily adsorbed on highly activated anionic exchangers (HAAE), but hardly adsorbed on lowly activated supports (LAAE) or on highly activated epoxy supports. Using amino-epoxy supports, GDH immobilizes on HAAE-epoxy and more slowly on LAAE-epoxy supports. Both immobilized biocatalysts are incubated at pH 10 for different times to increase the multipoint covalent attachment. Lowly activated anionic exchangers-epoxy-GDH is stable at pH 4 and 25C, the enzyme stability does not depend on the enzyme concentration and does not release any subunit to the supernatant, in opposition to the results obtained using HAAE-epoxy supports
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7 isoenzymes
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
genes gdh1, gdh2 and gdh3, GDH1 gene encodes a polypeptide subunit termed beta and GDH2 gene encodes alpha and the polypeptides can be assembled as homo- or heterohexamers composed of different ratios of alpha and beta, leading to the formation of seven active isoenzymes
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expressed in Escherichia coli BL21(DE3)/pLysS cells
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expression in Escherichia coli
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expression in Escherichia coli MV1184
P39633
ligated to plasmid pT7Blue vector and cloned into Escherichia coli DH5a
Q50JE9
cloning and expression of soluble wild-type and mutant enzymes in Escherichia coli strain XL1-Blue
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expressed in Escherichia coli
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expression in Escherichia coli TG1
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expression in Escherichia coli TG1 cells
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recombinant expression of wild-type and mutant enzymes
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expressed in Escherichia coli XLOLR
-, Q9TVN3
expression in Escherichia coli
-, P29051
overexpression in halophilic host Haloferax volcanii strain DS70 of soluble, active enzyme with NAD+-GDH activity about 800times higher in the induced sample as compared to controls, expression in inclusion bodies in mesophilic Escherichia coli
P29051
ligated to NdeI/BamHI digested pET3a, expression in Escherichia coli BL21 (DE3)
-, Q977U6
expression of isoenzymes in Escherichia coli as soluble proteins
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expressed in Escherichia coli Top10 cells
A5LH94, -
recombinant expression in Escherichia coli TOP10 cells
A5LH94, -
gene msmeg_4699, semi-quantitative real-time PCR expression analysis
A0R1C2
tobacco transformed with either an antisense or sense copy of a beta-subunit gene of tomato GDH, transgenic plants recover with between 0.5- and 34-times normal leaf GDH activity; tobacco transformed with either an antisense or sense copy of a beta-subunit gene of tomato GDH, transgenic plants recover with between 0.5- and 34-times normal leaf GDH activity
Q67C42, Q67C43
expression in Escherichia coli BL21 cells
-, Q852M0
expressed in Escherichia coli strain TG1
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expression of wild-type GDH in Escherichia coli strain BL21(DE3), and of the SeMet-labeled enzyme in Escherichia coli strain B834 (DE3)
P28997
overexpression in Escherichia coli
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gene pcal_1031, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of N-terminally Met-Ala-Ser-tagged and C-terminally His6-tagged enzyme in Eschericia coli strain Rosetta(DE3)
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expressed in Escherichia coli (DE3)-codon plus-RIL cells
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expression of inactive enzyme in Escherichia coli
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expressed in Solanum lycopersicum line S77-H
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three genes encoding the alpha-subunit, Slgdh-NAD;A1-3, and one additional gene encoding the beta-subunit of GDH, Slgdh-NAD;B1, Slgdh-NAD;A1-3 show conserved structures, whereas Slgdh-NAD;B1 includes a novel 5'-untranslated exon, DNA and amino acid sequence determination and analysis, quantitative real-time PCR expresssion analysis
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overexpressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
transcription of GDH2, which encodes the GDH alpha subunit, is activated and translation of the GDH2 mRNA is also activated to synthesize a subunit polypeptides, when protoplasts are isolated. When detached leaves absorb either acidic 5 mM jasmonic acid or salicylic acid solutions via petioles, GDH7 isoenzyme is activated and the GDH isoenzyme expression pattern is similar to that of protoplasts
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enzyme expression is upregulated under N2-starvation, overview
A0R1C2
under nitrogen- and phosphorus-deficient conditions, respectively: OsGDH2 expression is largely reduced by both nitrogen- and phosphorus-deprivation after 1 h
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under nitrogen- and phosphorus-deficient conditions, respectively: In shoots, OsGDH2 is dramatically induced after nitorgen-deprivation for 1 day, with 5.4fold increase, respectively. Its expression increases greatly after 7 days of phosphorus-deprivation; under nitrogen- and phosphorus-deficient conditions, respectively: In shoots, OsGDH3 is dramatically induced after nitorgen-deprivation for 1 day, with 9.7fold increase, respectively. OsGDH3 expression is also up-regulated by 3.1fold after phosphorus-deprivation for 7 days. OsGDH3 transcript is undetectable under the normal conditions in roots, and increases by 7.6fold after phosphorus-deprivation for 1 day
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E27F
P39633
improved thermostability as compared to wild-type
E27K
P39633
slightly improved thermostability as compared to wild-type
E27V
P39633
slightly improved thermostability as compared to wild-type
G255A
P39633
no significant thermostability
G82K
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dramatically switches to increased specificity for oxaloacetate, 280fold higher than those for 2-oxoglutarate
G82R
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specific activity not drastically altered compared to the wild-type
K80R
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specific activity not drastically altered compared to the wild-type
M101K
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specific activity not drastically altered compared to the wild-type
M101S
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dramatically switches to increased specificity for oxaloacetate, 495fold higher than those for 2-oxoglutarate
Q144C
P39633
improved thermostability as compared to wild-type
Q144D
P39633
slightly improved thermostability as compared to wild-type
Q144K
P39633
no improved thermostability as compared to wild-type
Q144R
P39633
highly improved thermostability as compared to wild-type
A242G
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site-directed mutagenesis, the mutant shows A242G showed a decreased overall catalytic efficiency for NADH at all pH values of pH 6.0-8.0 after Ala replacement with Gly compared to the wild-type enzyme, the mutation had a severe effect on the overall catalytic efficiency with NADPH as coenzyme
D165H
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site-directed mutagenesis, catalytically inactive mutant
D165N
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residual 2% of wild-type activity when purified after expression in Escherichia coli at 37C, cells induced at 8C are 1000fold less active than that produced at 37C, spontaneous deamidation, which depends on the residual catalytic machinery of the mutated GDH active site
D165N/K125A
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correctly folded, no significant deamidation
D263K
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site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants for NAD+, NADH, and NADPH, but decreased for DTNB leading to inactivation by the inhibitor
D263K
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site-directed mutagenesis, the D263K mutation produces remarkably little change in the kinetic parameters for NADH at pH 6.0-8.0 compared to the wild-type enzyme, with NADPH at all three pH values the kcat for the mutant is much higher than for wild-type GDH, and this factor increases from pH 6.0 to pH 7.0 and pH 8.0
D263K
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site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
F187D
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dimeric form of enzyme
F232S/P262S/D263K
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site-directed mutagenesis, the mutant shows switched cofactor spcificity compared to the wild-type enzyme, it has high activity with NADPH/NADP+
F238S
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site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants
F238S
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site-directed mutagenesis, the mutant shows markedly increased catalytic efficiency with NADPH, especially at pH 8.0 in the range of pH 6.0-8.0
F238S/P262S
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site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants
F238S/P262S
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site-directed mutagenesis, the mutant shows markedly increased catalytic efficiency with NADPH, especially at pH 8.0 in the range of pH 6.0-8.0
F238S/P262S
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site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
F238S/P262S/D263K/N290G
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site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
F238S/P262S/N290G
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site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
N290G
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site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
P262S
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site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants
P262S
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site-directed mutagenesis, the mutant shows markedly increased catalytic efficiency with NADPH, especially at pH 8.0 in the range of pH 6.0-8.0
W243F
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decreased activity compared to the wild type enzyme, more thermostable than the wild type enzyme
W243F
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site-directed mutagenesis, catalytically impaired enzyme due to hindered glutamate binding, the mutant shows Michaelis-Menten kinetics
W310F
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more thermostable than the wild type enzyme
W310F
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site-directed mutagenesis, the mutant shows Michaelis-Menten kinetics
W393F
-
increased activity compared to the wild type enzyme, more thermostable than the wild type enzyme
W393F
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site-directed mutagenesis
W449F
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decreased activity compared to the wild type enzyme, more thermostable than the wild type enzyme
W449F
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site-directed mutagenesis, the mutation does not affect the allosteric behaviour of the enzyme
W64F
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65% wild type enzyme activity, less thermostable than the wild type enzyme
Y187M
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no further stimulation of the mutated GDH isoenzymes by ADP in contrast to the wild-type
D245K
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the mutation shows reduced activity and 36.4fold discrimination against NADPH compared to NADH
D245K
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site-directed mutagenesis, discrimination against NADPH by factor 32, compared to 1000 for the wild-type enzyme
E243D
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the mutation shows reduced activity and 130fold discrimination against NADPH compared to NADH
E243D
P282997
site-directed mutagenesis, the enzyme shows impaired NADH binding and catalytic activity due to the disruption of hydrogen bonds with 2'-OH and 3'-OH groups of ribose
E243D
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site-directed mutagenesis, substitution of Asp for Glu in E243D produces a shift in favour of NADPH by virtue of a threefold increase in the Km for NAD+ and a threefold decrease in that for NADP+, resulting in a 9fold shift in the overall discrimination factor, discrimination against NADPH by factor 130, compared to 1000 for the wild-type enzyme
E243K
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the mutation shows reduced activity and almost no discrimination against NADPH compared to NADH
E243K
P282997
site-directed mutagenesis, the enzyme shows highly impaired NADH binding, inability of E243K to effectively switch to NADPH, which may be explained by the position of the P7 side chain, which is not be ideal for binding to the 2'-phosphate
E243K
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site-directed mutagenesis, discrimination against NADPH by a factor below 130, compared to 1000 for the wild-type enzyme
E243R
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the mutation shows reduced activity and almost no discrimination against NADPH compared to NADH
W244S
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the mutation shows reduced activity and 205fold discrimination against NADPH compared to NADH
W244S
P282997
site-directed mutagenesis, reduced catalytic activity and altered cofactor specificity, importance of Trp244 is apparent from kinetic studies of W244S
G376K
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faster thermal inactivation, higher specific activity at 58C
N97D
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faster thermal inactivation
N97D/G376K
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faster thermal inactivation, higher specific activity at 58C
additional information
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construction of backcrossed homozygous gdh1, gdh2, gdh3, gdh1-2, and gdh1-2-3 mutants. Enzyme activity in the roots of the gdh1 single mutant is similar to the wild-type, NADH-GDH activity in the roots of the gdh2 mutant is about 25% lower than the wild type, whereas in the roots of the gdh3 mutant, the enzyme activity is 30% higher. In the leaves, there is a 60% reduction in NADH-GDH activity in the gdh1 single mutant but not in the other two single mutants. By contrast, both in the roots and in the leaves of the gdh1-2 double mutant, a dramatic decrease in NADH-GDH activity occurs, butin the gdh1-2 double mutant, some remaining enzyme activity is still detected in the roots. No NADH-GDH enzyme activity is detected in either of the organs of the gdh1-2-3 triple mutant. No NADPH-GDH enzyme activity is detected in the wild type or in the gdh single, double, or triple mutants. Metabolic profiling of the gdh1-2-3 triple mutant, e.g. placed under continuous darkness, overview
W100R
P39633
no significant thermostability
additional information
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site-directed mutagenesis to alter substrate specificity in phenylalanine dehydrogenase and varying strengths of binding of the wrong enantiomer in engineered mutant enzyme and implications for resolution of racemates, overview
F238S?P262S?D263K
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site-directed mutagenesis, the mutant shows complete reversal in coenzyme selectivity from NAD(H) to NADP(H) with retention of high levels of catalytic activity for the second coenzyme
additional information
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an active chimera (CEC) consisting of the substrate-binding domain (domain I) of CsGDH and the coenzyme-binding domain (domain II) of Escherichia coli GDH is generated. Kinetic constants of chimeric protein: Km values for substrates L-glutamate, 2-oxoglutarate, NH4Cl highly increased compared to wild-type, Vmax values also highly increased compared to wild-type. The CEC chimera, like Escherichia coli GDH, has a marked preference for NADP(H) as coenzyme. selectivity for the phosphorylated coenzyme does indeed reside solely in domain II. Positive cooperativity toward L-glutamate, characteristic of wild-type CsGDH, retains with domain I. Although glutamate cooperativity occurs only at higher pH values in the wild-tpye CsGDH, the chimeric protein shows it over the full pH range explored. The chimera is capable of catalyzing severalfold higher reaction rates (Vmax) in both directions than either of the parent enzymes from which it is constructed
W64F
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site-directed mutagenesis, the mutation does not affect the allosteric behaviour of the enzyme
additional information
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site-directed mutagenesis to alter substrate specificity in phenylalanine dehydrogenase and varying strengths of binding of the wrong enantiomer in engineered mutant enzyme and implications for resolution of racemates, overview
molecular biology
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alpha-ketoglutarate dehydrogenase and GDH play a critical role in modulating alpha-ketoglutarate homeostasis
additional information
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construction of an enzyme deletion DELTAgdh2 mutant, the mutant shows less than 15-20% of wild-type activity, but DELTAgdh3 shows 20fold increased NAD+-dependent GDH activity, EC 1.4.1.2, genotypes and phenotypes, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme solubulization from inclusion bodies after expressionin Escherichia coli in 50 mM HEPES-NaOH, pH 7.5, containing 8 M urea and 25 mM DTT, and renaturation of protein using both rapid dilution and gradual dialysis methods
P29051
after 10fold dilution of the enzyme denatured with 3 M guanidine hydrochloride, the enzyme does not recover its activity, whereas after dialysis, the protein recovers 10% of the original activity value
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
a strategy to control flocculation is investigated using dimorphic yeast, Benjaminiella poitrasii as a model. Parent form of this yeast (Y) exhibit faster flocculation (11.1 min) than the monomorphic yeast form mutant Y-5 (12.6 min). Flocculation of both Y and Y-5 can be altered by supplementing either substrates or inhibitor of NAD-glutamate dehydrogenase (NAD-GDH) in the growth media. The rate of flocculation is promoted by alpha-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. This opens up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing; the rate of flocculation is promoted by a-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. These interesting findings open up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing
diagnostics
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GLDH, gama-glutamyltransferase, aspartate-aminotransferase, alanine-aminotransferase and erythrocyte mean cell volume are assessed in 238 alcoholics admitted to hospital: on admission, after 24 h and after 7 days. All the values are significantly higher than those in healthy persons. The fastest activity decrease is seen in GLDH. The kinetics of GLDH and aspartate-aminotranferase are more applicable than gama-glutamyltransferase kinetics after a week, but GLDH kinetics are most reliable. GLDH is the most specific laboratory marker with almost 90% specificity. The sensitivity of combination erythrocyte mean cell volume and GLDH kinetics after 1 week of abstinence is pathognomonic by 97.2%. GLDH is an equally accurate marker of alcoholism in comparison to others
medicine
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the findings emphasize the integration of glucose metabolism, glutamine metabolism, and oncogenic signaling in glioblastoma cells and suggest that exploiting compensatory pathways of glutamine metabolism can improve the efficacy of cancer treatments that impair glucose utilization
molecular biology
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GDH is essential for the full development of the secretory response in beta-cells
agriculture
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GDH genes involved in leaf senescence are also a component of the plant defence response during plantpathogen interaction, GDH behaves like a non-specific stress-related gene
degradation
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clarification of the in vivo direction of the reaction catalyzed by GDH isoenzyme 1, the enzyme catabolizes L-glutamate in roots, and does not assimilate NH4+ in source leaves
medicine
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prolonged exposure to Corydalis ternata may be one of the ways to regulate glutamate concentration in brain through the activation of GDH
diagnostics
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GDH electrophoretic type (ETs) and sequence types may serve as useful markers in predicting the pathogenic behavior of strains of this serotype and that the molecular basis for the observed differences in the ETs is amino acid substitutions and not deletion, insertion, or processing uniqueness
biotechnology
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method describes immobilization of enzymes by the maximum amount of subunits and rigidification of the enzyme subunits involved in the immobilization
agriculture
-
plays some role in triticale plants defence against effects of different types of environmental stresses
additional information
P39633
Q144R can be used as a template gene to modify the substrate specificity of Bacillus subtilis GluDH for industrial use
food industry
Q50JE9
plays an essential role during postharvest senescence, its expression most likely is controlled by multigenes and regulated either transcriptionally or posttranscriptionally
additional information
-
reactivation of D165N is a consequence of the catalytic chemistry of the enzymes active site
additional information
-, Q9TVN3
high sequence similarity to GDH genes from the Bacteroides, GDH is an anabolic enzyme catalysing the assimilation of ammonia by Entodinium caudatum in the rumen, the gene is probably acquired by lateral gene transfer from a ruminal bacterium
molecular biology
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GDH, in conjunction with NADH-glutamte synthase, contributes to the control of leaf glutamate homeostasis, an amino acid that plays a central signaling and metabolic role at the interface of the carbon and nitrogen assimilatory pathways
additional information
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glutamine synthetase-GOGAT pathway and GDH play distinct roles in the source-sink nitrogen cycle of tobacco leaves, regardless of leaf age, [15N]ammonium does not depend on GDH
additional information
Q67C42, Q67C43
GDH gene expression and translation are apparently subject to complex regulation; large modulation of GDH beta-subunit titre does not affect plant viability under ideal growing conditions, GDH gene expression and translation are apparently subject to complex regulation
additional information
-, Q852M0
induction of GDH1 and GDH2 transcripts along the root do not coincide with that of NADH-GOGAT expression
additional information
-
possible role of enzyme under Hg-stress
additional information
-
subunit rearrangement, i.e., a change in the quaternary structure of the hexameric recombinant GDH, is essential for activation of the enzyme
degradation
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at high salinity glutamate seems to be preferentially produced through the process catalyzed by NADH-GDH, whereas GS-catalysis might be the main glutamate synthesis pathway under low salinity
additional information
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shift in GDH cellular compartmentation is important during leaf nitrogen remobilization