Information on EC 1.4.1.4 - glutamate dehydrogenase (NADP+)

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

EC NUMBER
COMMENTARY hide
1.4.1.4
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RECOMMENDED NAME
GeneOntology No.
glutamate dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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oxidative deamination
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redox reaction
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reduction
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reductive amination
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-glutamate biosynthesis III
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nitrate reduction V (assimilatory)
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nitrate reduction VI (assimilatory)
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partial TCA cycle (obligate autotrophs)
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glutamate and glutamine metabolism
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Arginine biosynthesis
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Alanine, aspartate and glutamate metabolism
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Nitrogen metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NADP+ oxidoreductase (deaminating)
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CAS REGISTRY NUMBER
COMMENTARY hide
9029-11-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NADPH-GDH isozymes GDHI, GDHII, and GDHI'
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Aeropyrum pernix K1 JCM 9820
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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AKQ74236
GenBank
Manually annotated by BRENDA team
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AKQ74236
GenBank
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
hosts human adult and human infant
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Manually annotated by BRENDA team
strain breve a and parvolorum a
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Manually annotated by BRENDA team
hosts rat and calf
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Manually annotated by BRENDA team
strain infantis a and liberorum
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Manually annotated by BRENDA team
the hosts are pig and chicken
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Manually annotated by BRENDA team
host pig
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain DH5alpha
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
monokaryotic strain h1
Uniprot
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
CBS6556
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Manually annotated by BRENDA team
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Uniprot
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Amanita citrina
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Manually annotated by BRENDA team
no activity in Amanita muscaria
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Manually annotated by BRENDA team
no activity in Amanita muscaria MAN
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Manually annotated by BRENDA team
no activity in Boletus edulis
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Manually annotated by BRENDA team
no activity in Boletus edulis Hub 0
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Manually annotated by BRENDA team
no activity in Lactarius quietus
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Manually annotated by BRENDA team
no activity in Lactarius subdulcis
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Manually annotated by BRENDA team
no activity in Lactarius subdulcis BRI 2
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Manually annotated by BRENDA team
no activity in Paxillus involutus
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Manually annotated by BRENDA team
no activity in Pisolithus tinctorius
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Manually annotated by BRENDA team
no activity in Pisolithus tinctorius 441
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Manually annotated by BRENDA team
no activity in Rhizopogon luteolus
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Manually annotated by BRENDA team
no activity in Rhizopogon luteolus SERRE
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Manually annotated by BRENDA team
no activity in Scleroderma citrinum
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Manually annotated by BRENDA team
no activity in Scleroderma citrinum Foug A
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Manually annotated by BRENDA team
no activity in Suillus bovinus
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Manually annotated by BRENDA team
no activity in Suillus bovinus LED 1
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Manually annotated by BRENDA team
no activity in Thelephora terrestris
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Manually annotated by BRENDA team
no activity in Thelephora terrestris CHA
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Manually annotated by BRENDA team
no activity in Tricholoma populinum
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Manually annotated by BRENDA team
no activity in Tricholoma populinum BLAE
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Manually annotated by BRENDA team
no activity in Xerocomus chrysenteron
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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
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
NADPH-GDH isozymes GDHI, GDHII, and GDHI'
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Manually annotated by BRENDA team
strain DSM 3773
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Manually annotated by BRENDA team
two NADP+-dependent glutamate dehydrogenases encoded by GDH1 and GDH3
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Manually annotated by BRENDA team
strains 975h- and 972h+
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Manually annotated by BRENDA team
Sphaerostilbe repens
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
strain PCC 6803
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Manually annotated by BRENDA team
isolate AN1
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Manually annotated by BRENDA team
Thermophilic bacillus
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain ATCC 95640
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminopentanoate + H2O + NADP+
2-oxopentanoate + NH3 + NADPH + H+
show the reaction diagram
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activity with 2-oxovalerate amd 2-aminopentanoate is 25% and 17% compared to the activity with 2-oxoglutarate and L-glutamate
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r
2-oxoadipate + NADPH + NH3
L-2-aminoadipate + NADP+ + H2O
show the reaction diagram
2-oxobutanoate + NH3 + NADPH + H+
L-2-aminobutanoate + H2O + NADP+
show the reaction diagram
2-oxobutyrate + NADPH + NH3
L-2-aminobutyrate + NADP+ + H2O
show the reaction diagram
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
show the reaction diagram
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
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r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
show the reaction diagram
2-oxoglutarate + NH3 + NADPH
L-glutamate + H2O + NADP+
show the reaction diagram
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r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
show the reaction diagram
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
2-oxovalerate + NADPH + NH3
L-2-aminovalerate + NADP+ + H2O
show the reaction diagram
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15% of the activity with 2-oxoglutarate
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?
2-oxovalerate + NH3 + NADPH + H+
L-valine + H2O + NADP+
show the reaction diagram
L-2-oxoglutarate + NADPH + NH3
glutamate + NADP+ + H2O
show the reaction diagram
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?
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
L-glutamate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H + NH3
show the reaction diagram
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r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
L-homoserine + H2O + NAD+
4-hydroxy-2-oxobutanoate + NH3 + NADH
show the reaction diagram
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?
L-norvaline + H2O + NADP+
2-oxopentanoate + NH3 + NADPH + H+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
show the reaction diagram
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
10 mM, 1.3fold increase in activity
K2SO4
enhances the activity by a maximum of about 280-300% at a concentration of 150-200 mM
MgSO4
10 mM, 1.3fold increase in activity
Na3PO4
enhances the activity by a maximum of about 280-300% at a concentration of 150-200 mM
Zn2+
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forward reaction of GDH from Aspergillus terreus is 80% inhibited by 5 mM ZnCl2
additional information
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Ca2+ has no effects on the aminating activity of NADP(H)-GDH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-pyridinedicarboxylate
2-hydroxyethyl disulfide
attenuation of reductive amination (forward) activity but a negligible effect on oxidative deamination (reverse) activity
2-Methyleneglutarate
2-oxoglutarate
4-chloromercuribenzoate
Ag2+
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at 1 mM, 60% inhibition
AgNO3
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1 mM, 30C, complete loss of aminating activity
AlCl3
BaCl2
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1 mM, 30C, 15% loss of aminating activity
CaCl2
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1 mM, 30C, 11% loss of aminating activity
CH2ICOOH
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1 mM, 30C, 15% loss of aminating activity
cystine
strongly and selectively inhibits the reductive amination reaction
dimethyl ester of isophthalic acid
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dimethyl ester of isophthalate (DMIP), but not isophthalate, inhibits Aspergillus niger growth on agar as well as in liquid culture. This is ascribed to the inability of isophthalate to enter fungal mycelia. Dimethyl ester of isophthalic acid is hydrolysed intracellularly to isophthalate. Subsequent to DMIP addition, intracellular isophthalate can be demonstrated. Addition of NH4+ to DMIP-treated Aspergillus niger mycelia results in intensive vacuolation, retraction of cytoplasm and autolysis
dithiothreitol
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1 mM, 30.7% residual activity
EDTA
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1 mM, 5.3% residual activity
FeSO3(NH4)2SO4
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1 mM, 30C, 14% loss of aminating activity
fumarate
glutamate
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competitive inhibitor of the amination reaction
Glutaric acid
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at 20 mM, 25% inhibition
glyoxylate
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at 20 mM, 30% inhibition
guanidine hydrochloride
Hexachlorophene
15% inhibition at 0.016 mM; 80% inhibition at 0.016 mM
HgCl2
hydroxylamine
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competitive inhibitor with ammonia and uncompetitive inhibitor with both 2-oxoglutarate and NADPH
iodoacetamide
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at 4 mM, complete inactivation
isocitrate
10 M, 64% of initial activity
Isophthalate
Isophthalic acid
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L-glutamate
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substrate inhibition above 15 mM
L-Glutamic acid
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at 20 mM 25% inhibition
L-homoserine
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competitive inhibitor with respect to both ammonia and glutamine
L-tryptophan
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at 20 mM, 15% inhibition
malate
MnCl2
N-ethylmaleimide
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at 0.8 mM, 44% inhibition
NAD+
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0.3 mM, 50.5% residual activity
NADH
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0.3 mM, 5.3% residual activity
NADP+
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inhibits at higher 2-oxoglutarate levels
NADPH
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0.3 mM, 3.8% residual activity
nitrogen assimilation control protein
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represses the transcription of the gene gdhA
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O2
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inactivation
oxaloacetate
p-Chloromercuriphenyl sulfonate
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inactivetes, can be reversed by addition of cysteine
p-hydroxymercuribenzoic acid
Pb(CH3COO)2
Pb2+
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5 mM, 19.8% residual activity
potassium phosphate
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over 0.1 M at oxidative deamination
pyridoxal 5'-phosphate
pyruvate
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at 10 mM slight inhibitory
sodium dodecylsulfate
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at 0.7% w/v after 1 h 5% activity
succinate
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competitive inhibitor with 2 oxoglutarate, uncompetitive with NADPH and non-competitive with ammonia
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,5-pyrazoledicarboxylate
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activates at lower 2-oxoglutarate concentration
3,5-pyridinedicarboxylate
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activates at lower 2-oxoglutarate concentration
acetonitrile
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activates
CaCl2
DL-2-hydroxyglutarate
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activates at lower 2-oxoglutarate concentration
ethanol
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activates up to 40% v/v
Glutarate
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activates at lower 2-oxoglutarate concentration
IDP
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at 1 mM five-fold Michaelis Menten constant of 2-oxoglutarate
Itaconate
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activates even in the presence of 10 mM 2-oxoglutarate
K2HPO4
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at 0.15 M three to fourfold stimulation of activity
K2SO4
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280-300% activity at 150-200 mM
K3PO4
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less effective than K2SO4 and Na3PO4
methanol
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activates
MgCl2
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at 5 mM, 104% activity, oxidative deamination
MnCl2
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at 5 mM, 250% activity, oxidative deamination
Na2SO4
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less effective than K2SO4 and Na3PO4
Na3PO4
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280-300% activity at 150-200 mM
oxalylglycine
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activates at lower 2-oxoglutarate concentration
potassium phosphate
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up to 0.1 M oxidative deamination
UTP
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activates up to 70%
Zn2+
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activates up to 0.1 mM
additional information
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exhibits 2.5-fold-higher GDH activity than cells are grown in milk, instead of glucose
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