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 hide
1.4.1.2
-
RECOMMENDED NAME
GeneOntology No.
glutamate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
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redox reaction
-
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reduction
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-
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reductive amination
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-aminobutanoate degradation V
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alanine metabolism
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Alanine, aspartate and glutamate metabolism
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Arginine biosynthesis
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ethylene biosynthesis IV (engineered)
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glutamate and glutamine metabolism
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L-alanine degradation II (to D-lactate)
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L-glutamate degradation I
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L-glutamate degradation V (via hydroxyglutarate)
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Metabolic pathways
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methylaspartate cycle
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Nitrogen metabolism
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Taurine and hypotaurine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NAD+ oxidoreductase (deaminating)
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CAS REGISTRY NUMBER
COMMENTARY hide
9001-46-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Achlya sp.
-
-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
-
-
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Manually annotated by BRENDA team
Apodachlya sp.
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-
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain NCIM 565
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-
Manually annotated by BRENDA team
strain ISW1214
Uniprot
Manually annotated by BRENDA team
two enzymes GDHA and GDHB
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-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
113B
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-
Manually annotated by BRENDA team
113B
-
-
Manually annotated by BRENDA team
SB4
-
-
Manually annotated by BRENDA team
SB4
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
strain DSMZ 2266T
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
strain R4 (ATCC 33500)
SwissProt
Manually annotated by BRENDA team
strain R4 (ATCC 33500)
SwissProt
Manually annotated by BRENDA team
fragment; strain UTB1302
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
gene msmeg_4699
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Scots pine
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-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
strain TAD1
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-
Manually annotated by BRENDA team
gene pcal_1031
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-
Manually annotated by BRENDA team
gene pcal_1031
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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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-
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
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-
Manually annotated by BRENDA team
DSM 320
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
fragment; also named Symphalangus syndactylus
UniProt
Manually annotated by BRENDA team
PCC 6803
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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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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-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 + NADH + NH3
2-aminobutyrate + NAD+ + H2O
show the reaction diagram
faint specificity
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + 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
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
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
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
show the reaction diagram
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
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 + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
show the reaction diagram
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-serine + H2O + NAD+
3-hydroxy-2-oxopropanoate + NH3 + NADH
show the reaction diagram
-
deamination at 29% the rate of L-glutamate deamination
-
-
?
oxaloacetate + NADPH + NH3
L-aspartate + NADP+ + H2O
show the reaction diagram
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
additional information
?
-
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 + 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
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-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
additional information
?
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-NAD+
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-
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Al3+
-
enhances increase in GDH activity due to Hg
betaine
high concentrations of salt may be substituted with 30% DMSO or betaine with good stability and activity
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+
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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
activity with KCl slightly higher than with NaCl
Mg2+
-
stimulation
Mn2+
-
activation of reductive amination
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
NH4+
transcriptional upregulation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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alpha-ketoglutarate
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ATP/GTP-competitive inhibitor of casein kinase-2
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aurintricarboxylic acid
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BH3I-2
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-
Bithionol
Calmidazolium
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-
chlortetracyclin
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-
citrate
Co2+
82% activity in the presence of 1 mM Co2+
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
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-
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
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-
epicatechin-3-monogallate
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-
epicatechin-monogallate
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epigallocatechin
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-
epigallocatechin-3,5-digallate
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-
epigallocatechin-3-gallate
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-
erythrosin B
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ethaverine hydrochloride
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-
ethyl acetimidate
-
inactivation with ethyl acetimidate shows pseudo-first-order kinetics
fumarate
gallic acid
-
-
glutamate
glutamine
Glutarate
glutathione
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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
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guanidine hydrochloride
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72C, almost complete loss of activity by addition of more than 3 M
GW-5074
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-
Hexachlorophene
iodoacetamide
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-
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
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-
N-acetylglutamate
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-
N-alpha-p-tosyl-L-lysine chloromethyl ketone
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TLCK
N-carbamylglutamate
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N-ethylmaleimide
N-methylglutamate
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-
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
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p-hydroxymercuribenzoate
phosphoenolpyruvate
-
weak
pyridoxal 5'-phosphate
Pyruvic acid
succinate
suloctidil
-
-
Tetranitromethane
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rapid loss of enzymatic activity versus time at various concentrations of modifier, showing pseudo-first-order kinetics
thiol reagents
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-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetonitrile
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activates
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
asparagine
-
activates
aspartate
-
activates
ATP
-
activates in presence of 3 M NaCl or 3 M Kcl, slight activation in absence of salts
D-arginine
212% activity in the presence of 10 mM D-arginine
dAMP
-
stimulation
ethylene
glycerol
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
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jasmonic acid
L-arginine
L-asparagine
L-aspartate
L-aspartic acid
-
-
L-cysteine
L-His
-
activates in presence of 3 M NaCl, 3 M Kcl or in absence of salts
L-histidine
L-isoleucine
-
-
L-Leu
-
activates in presence of 3 M NaCl, 3 M Kcl or in absence of salts
L-lysine
L-methionine
L-phenylalanine
-
-
L-tryptophan
leucine
-
stimulation
NaCl
-
high NaCl induces the formation of reactive oxygen species, which in turn induces the synthesis of the alpha-subunit of GDH
NaNO3
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
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
salicylic acid
tetrahydrofuran
-
activates
Zn2+
224% activity in the presence of 1 mM Zn2+
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008 - 606
2-oxoglutarate
5.82 - 7.4
glutamate
0.000011 - 1349
L-glutamate
0.018 - 2.1
NAD+
0.001 - 42.5
NADH
0.163 - 3.7
NADP+
0.0384 - 1.64
NADPH
0.00013 - 300
NH3
0.00528 - 304
NH4+
2.27 - 4.16
oxaloacetate
additional information
additional information