Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.4.1.2 - glutamate dehydrogenase and Organism(s) Bos taurus and UniProt Accession P00366

for references in articles please use BRENDA:EC1.4.1.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Bos taurus
UNIPROT: P00366 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide
L-glutamate
+
H2O
+
NAD+
=
2-oxoglutarate
+
NH3
+
NADH
+
H+
+
+
=
+
+
+
Synonyms
glutamate dehydrogenase, gdh, glud1, hgdh1, glutamic dehydrogenase, nad-gdh, l-glutamate dehydrogenase, nad-dependent glutamate dehydrogenase, nadh-gdh, glutamic acid dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutamate dehydrogenase
-
dehydrogenase, glutamate
-
-
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase (NAD)
-
-
-
-
glutamate oxidoreductase
-
-
-
-
glutamic acid dehydrogenase
-
-
-
-
glutamic dehydrogenase
-
-
-
-
L-glutamate dehydrogenase
-
-
-
-
NAD-dependent glutamate dehydrogenase
-
-
-
-
NAD-dependent glutamic dehydrogenase
-
-
-
-
NAD-GDH
-
-
-
-
NAD-glutamate dehydrogenase
-
-
-
-
NAD-linked glutamate dehydrogenase
-
-
-
-
NAD-linked glutamic dehydrogenase
-
-
-
-
NAD-specific glutamate dehydrogenase
-
-
-
-
NAD-specific glutamic dehydrogenase
-
-
-
-
NAD:glutamate oxidoreductase
-
-
-
-
NADH-dependent glutamate dehydrogenase
-
-
-
-
NADH-linked glutamate dehydrogenase
-
-
-
-
Surface-associated protein PGAG1
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
reductive amination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NAD+ oxidoreductase (deaminating)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9001-46-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
show the reaction diagram
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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
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
3,3'-[(2-bromobenzene-1,4-diyl)di(E)ethene-2,1-diyl]bis(6-hydroxybenzoic acid)
-
i.e. BSB
ATP/GTP-competitive inhibitor of casein kinase-2
-
-
-
aurintricarboxylic acid
-
-
BH3I-2
-
-
bithionol
-
-
Calmidazolium
-
-
diethylstilbestrol
-
-
epicatechin
-
-
epicatechin-3-monogallate
-
-
epicatechin-monogallate
-
-
epigallocatechin
-
-
epigallocatechin-3,5-digallate
-
-
epigallocatechin-3-gallate
-
-
erythrosin B
-
-
ethaverine hydrochloride
-
-
gallic acid
-
-
GTP
-
-
GW-5074
-
-
Hexachlorophene
-
-
leoidin
-
-
metergoline
-
-
suloctidil
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.39 - 1.62
L-glutamate
0.14 - 0.43
NAD+
additional information
additional information
-
cofactor kinetics, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0015
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
Bos taurus
pH 7.5
0.0048
bithionol
Bos taurus
pH 7.5
0.0039
Hexachlorophene
Bos taurus
pH 7.5
0.0064
3,3'-[(2-bromobenzene-1,4-diyl)di(E)ethene-2,1-diyl]bis(6-hydroxybenzoic acid)
Bos taurus
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0158
ATP/GTP-competitive inhibitor of casein kinase-2
Bos taurus
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
-
0.0012
aurintricarboxylic acid
Bos taurus
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0037
BH3I-2
Bos taurus
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0055
bithionol
Bos taurus
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0077
Calmidazolium
Bos taurus
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0017
diethylstilbestrol
Bos taurus
-
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
Bos taurus
-
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
Bos taurus
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.05
erythrosin B
Bos taurus
-
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
Bos taurus
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0015
GW-5074
Bos taurus
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0017
Hexachlorophene
Bos taurus
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0328
metergoline
Bos taurus
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0138
suloctidil
Bos taurus
-
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]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
104
-
GDH II
167
-
GDH I
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to the family of amino acid dehydrogenases
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHE3_BOVIN
558
0
61512
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
330000
-
non-denaturing PAGE
57500
-
6 * 57500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
6 * 57500, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GDH I and II
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cho, S.W.; Lee, J.; Choi, S.Y.
Two soluble forms of glutamate dehydrogenase isoproteins from bovine brain
Eur. J. Biochem.
233
340-346
1995
Bos taurus
Manually annotated by BRENDA team
Li, M.; Allen, A.; Smith, T.J.
High throughput screening reveals several new classes of glutamate dehydrogenase inhibitors
Biochemistry
46
15089-15102
2007
Bos taurus
Manually annotated by BRENDA team
Zhang, Y.; Lu, N.; Gao, Z.
Hemin-H2O2-NO2(-) induced protein oxidation and tyrosine nitration are different from those of SIN-1: a study on glutamate dehydrogenase nitrative/oxidative modification
Int. J. Biochem. Cell Biol.
41
907-915
2009
Bos taurus
Manually annotated by BRENDA team
Li, M.; Smith, C.J.; Walker, M.T.; Smith, T.J.
Novel inhibitors complexed with glutamate dehydrogenase: allosteric regulation by control of protein dynamics
J. Biol. Chem.
284
22988-23000
2009
Escherichia coli, Tetrahymena, Bos taurus (P00366)
Manually annotated by BRENDA team
Engel, P.C.
Making biochemistry count: life among the amino acid dehydrogenases
Biochem. Soc. Trans.
39
425-429
2011
[Clostridium] symbiosum, Bos taurus, Homo sapiens
Manually annotated by BRENDA team