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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

Reaction

L-glutamate
+
H2O
+
NAD+
=
2-oxoglutarate
+
NH3
+
NADH
+
H+

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 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.1 With NAD+ or NADP+ as acceptor
                1.4.1.2 glutamate dehydrogenase

Inhibitors

Inhibitors on EC 1.4.1.2 - glutamate dehydrogenase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-methyl-2,4-pentanediol
8.5 mM, 94% residual activity. the sequence contains several binding sites for 2-methyl-2,4-pentanediol
2-Methyleneglutarate
-
potent competitive inhibitor
2-oxoglutarate
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
5,5'-dithiobis(2-nitrobenzoate)
alpha,gamma-Diethyl glutamate
-
-
alpha-ketoglutarate
-
-
ATP/GTP-competitive inhibitor of casein kinase-2
-
-
-
aurintricarboxylic acid
-
-
BH3I-2
-
-
bithionol
Calmidazolium
-
-
chlortetracyclin
-
-
citrate
D-asparagine
93% activity in the presence of 10 mM D-asparagine
D-Aspartate
90% activity in the presence of 10 mM D-aspartate
D-glutamate
D-glutamine
95% activity in the presence of 10 mM D-glutamine
diethyl dicarbonate
-
inactivation follows pseudo-first-order kinetics
diethylstilbestrol
-
-
DL-valine
-
-
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
-
-
ethyl acetimidate
-
inactivation with ethyl acetimidate shows pseudo-first-order kinetics
fumarate
gallic acid
-
-
glutamate
glutamine
Glutarate
glutathione
-
reduces increase in GDH activity due to Hg
glycogen accumulation regulator
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
-
72°C, almost complete loss of activity by addition of more than 3 M
GW-5074
-
-
Hexachlorophene
iodoacetamide
-
-
iodoacetate
-
weak
isocitrate
isophthalate
isophthalic acid
-
-
KCl
-
3 M, 75% inhibition
L-aspartate
L-glutamate
substrate inhibition at L-glutamate concentrations above 20 mM
L-glutamine
89% activity in the presence of 10 mM L-glutamine
L-Malic acid
-
-
L-ornithine
83% activity in the presence of 10 mM L-ornithine
leoidin
-
-
malate
metergoline
-
-
N-acetylglutamate
-
-
N-alpha-p-tosyl-L-lysine chloromethyl ketone
-
TLCK
N-carbamylglutamate
-
-
N-ethylmaleimide
N-methylglutamate
-
-
NaCl
-
3 M, 89% inhibition
NADP+
-
non-competitive versus L-glutamate, non-competitive versus NAD+
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
o-Iodobenzoate
-
-
oxaloacetate
p-Aminomercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
phosphoenolpyruvate
-
weak
pyridoxal 5'-phosphate
Pyruvic acid
succinate
suloctidil
-
-
Tetranitromethane
-
rapid loss of enzymatic activity versus time at various concentrations of modifier, showing pseudo-first-order kinetics
thiol reagents
-
-
additional information
-