1.4.1.2: glutamate dehydrogenase
This is an abbreviated version!
For detailed information about glutamate dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.2
-
1.4.1.2
-
ammonia
-
aminotransferase
-
giardia
-
deamination
-
dehydrogenases
-
malate
-
alpha-ketoglutarate
-
clostridium
-
difficile
-
assemblage
-
transaminase
-
succinate
-
duodenalis
-
adp
-
2-oxoglutarate
-
toxin
-
nitrate
-
stool
-
glutaminase
-
zoonotic
-
isocitrate
-
immunoassay
-
fecal
-
tpi
-
transamination
-
multilocus
-
toxigenic
-
neurospora
-
hyperinsulinism
-
triose
-
hypoglycemia
-
oxaloacetate
-
nadp-dependent
-
bilirubin
-
hexameric
-
hyperammonemia
-
giardiasis
-
triosephosphate
-
l-leucine
-
cryptosporidium
-
no3
-
aminooxyacetate
-
intestinalis
-
ribotype
-
quinoproteins
-
gamma-glutamyltransferase
-
glutaminolysis
-
diazoxide
-
degradation
-
agriculture
-
biotechnology
-
gaba-t
-
drug development
-
medicine
-
molecular biology
-
pancreatectomy
-
analysis
-
food industry
-
energy production
-
diagnostics
-
synthesis
- 1.4.1.2
- ammonia
- aminotransferase
- giardia
-
deamination
- dehydrogenases
- malate
- alpha-ketoglutarate
- clostridium
- difficile
-
assemblage
- transaminase
- succinate
- duodenalis
- adp
- 2-oxoglutarate
- toxin
- nitrate
-
stool
- glutaminase
-
zoonotic
- isocitrate
-
immunoassay
-
fecal
- tpi
-
transamination
-
multilocus
-
toxigenic
- neurospora
- hyperinsulinism
- triose
- hypoglycemia
- oxaloacetate
-
nadp-dependent
- bilirubin
-
hexameric
-
hyperammonemia
- giardiasis
-
triosephosphate
- l-leucine
- cryptosporidium
- no3
- aminooxyacetate
- intestinalis
-
ribotype
-
quinoproteins
- gamma-glutamyltransferase
-
glutaminolysis
- diazoxide
- degradation
- agriculture
- biotechnology
- gaba-t
- drug development
- medicine
- molecular biology
-
pancreatectomy
- analysis
- food industry
- energy production
- diagnostics
- synthesis
Reaction
Synonyms
At5g18170, AtGDH1, BpNADGDH, c, CCNA_00086, CsGDH, dehydrogenase, glutamate, GDH, GDH isoenzyme 1, GDH, NAD-dependent, gdh-1, gdh-2, GDH1, GDH2, Gdh2p, GDH3, GdhA, GDHB, GDHI, GdhZ, Glu dehydrogenase, GluD, GLUD1, GLUD2, GluDH, glutamate dehydrogenase, glutamate dehydrogenase (NAD), glutamate dehydrogenase 2, glutamate dehydrogenase alpha subunit, glutamate dehydrogenase beta subunit, glutamate dehydrogenase isoform 1, glutamate oxidoreductase, glutamic acid dehydrogenase, glutamic dehydrogenase, hGDH1, hGDH2-nerve-specific GDH, house-keeping GDH, L-glutamate dehydrogenase, L-glutamic acid dehydrogenase, More, NAD(+)-dependent glutamate dehydrogenase, NAD(H)-dependent glutamate dehydrogenase, NAD+-dependant glutamate dehydrogenase, NAD+-dependent GDH, NAD+-dependent GDHX, NAD+-dependent GluDH, NAD+-dependent glutamate dehydrogenase, NAD+-GDH, NAD+-glutamate dehydrogenase, NAD+-specific GDH, NAD+-specific glutamate dehydrogenase, NAD-dependent GDH, NAD-dependent glutamate dehydrogenase, NAD-dependent glutamic dehydrogenase, NAD-dependent L-glutamate dehydrogenase, NAD-GDH, NAD-glutamate dehydrogenase, NAD-linked glutamate dehydrogenase, NAD-linked glutamic dehydrogenase, NAD-specific glutamate dehydrogenase, NAD-specific glutamic dehydrogenase, NAD-ylGdh2p, NAD:glutamate oxidoreductase, NADH-dependent GDH, NADH-dependent glutamate dehydrogenase, NADH-GDH, NADH-glutamate dehydrogenase, NADH-linked glutamate dehydrogenase, OsGDH1, OsGDH2, OsGDH3, Pcal_1031, RocG, sco2999, Surface-associated protein PGAG1, t-GDH, type I GDH, YALI0E09603g, ylGDH2
ECTree
1.4.1.2 glutamate dehydrogenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.4.1.2 - glutamate dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G82K
-
dramatically switches to increased specificity for oxaloacetate, 280fold higher than those for 2-oxoglutarate
M101K
-
specific activity not drastically altered compared to the wild-type
M101S
-
dramatically switches to increased specificity for oxaloacetate, 495fold higher than those for 2-oxoglutarate
Y187M
-
no further stimulation of the mutated GDH isoenzymes by ADP in contrast to the wild-type
C1141T
D245K
E243D
E243K
E243R
-
the mutation shows reduced activity and almost no discrimination against NADPH compared to NADH
W244S
molecular biology
-
alpha-ketoglutarate dehydrogenase and GDH play a critical role in modulating alpha-ketoglutarate homeostasis
N97D/G376K
-
faster thermal inactivation, higher specific activity at 58°C
A242G
-
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
D165N
-
residual 2% of wild-type activity when purified after expression in Escherichia coli at 37°C, cells induced at 8°C are 1000fold less active than that produced at 37°C, spontaneous deamidation, which depends on the residual catalytic machinery of the mutated GDH active site
D263K
F232S/P262S/D263K
-
site-directed mutagenesis, the mutant shows switched cofactor spcificity compared to the wild-type enzyme, it has high activity with NADPH/NADP+
F238S
F238S/P262S
F238S/P262S/D263K/N290G
-
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
F238S/P262S/N290G
-
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
F238S?P262S?D263K
-
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
N290G
-
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
P262S
W243F
W310F
W393F
W449F
W64F
additional information
C1141T
residue C1141 is responsible for the inhibition of enzyme activity by HgCl2, and HgCl2 functions as an activating compound for mutant C1141T
D245K
-
the mutation shows reduced activity and 36.4fold discrimination against NADPH compared to NADH
D245K
-
site-directed mutagenesis, discrimination against NADPH by factor 32, compared to 1000 for the wild-type enzyme
E243D
-
the mutation shows reduced activity and 130fold discrimination against NADPH compared to NADH
E243D
-
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
E243D
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
E243K
-
the mutation shows reduced activity and almost no discrimination against NADPH compared to NADH
E243K
-
site-directed mutagenesis, discrimination against NADPH by a factor below 130, compared to 1000 for the wild-type enzyme
E243K
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
W244S
-
the mutation shows reduced activity and 205fold discrimination against NADPH compared to NADH
W244S
site-directed mutagenesis, reduced catalytic activity and altered cofactor specificity, importance of Trp244 is apparent from kinetic studies of W244S
D263K
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
-
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
-
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
F238S
site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants
F238S
-
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
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
-
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
F238S/P262S
-
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
P262S
site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants
P262S
-
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
-
decreased activity compared to the wild type enzyme, more thermostable than the wild type enzyme
W243F
-
site-directed mutagenesis, catalytically impaired enzyme due to hindered glutamate binding, the mutant shows Michaelis-Menten kinetics
W310F
-
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
W449F
-
decreased activity compared to the wild type enzyme, more thermostable than the wild type enzyme
W449F
-
site-directed mutagenesis, the mutation does not affect the allosteric behaviour of the enzyme
W64F
-
65% wild type enzyme activity, less thermostable than the wild type enzyme
W64F
-
site-directed mutagenesis, the mutation does not affect the allosteric behaviour of the enzyme
additional information
-
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
additional information
-
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
additional information
-
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
additional information
-
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
additional information
YALI0E09603g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
additional information
-
YALI0E09603g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
additional information
-
YALI0E09603g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
-
additional information
-
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
additional information
chimaeric protein consisting of domain I from NAD+-dependent GDH of Clostridium symbiosum, residues 1-200, domain II from NADP+-dependent GDH of Escherichia coli, residues 201-404 and the C-terminal helix again from Clostridium symbiosum, residues 405-448 which re-enters domain I. Domain II maintains its structural and functional integrity independent of the hinge and domain I. The enzyme is fully functional and retains the preference for NADP+ cofactor from the parent E. coli domain II
additional information
-
chimaeric protein consisting of domain I from NAD+-dependent GDH of Clostridium symbiosum, residues 1-200, domain II from NADP+-dependent GDH of Escherichia coli, residues 201-404 and the C-terminal helix again from Clostridium symbiosum, residues 405-448 which re-enters domain I. Domain II maintains its structural and functional integrity independent of the hinge and domain I. The enzyme is fully functional and retains the preference for NADP+ cofactor from the parent E. coli domain II
