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
1.4.1.2
-
RECOMMENDED NAME
GeneOntology No.
glutamate dehydrogenase
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reductive amination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
4-aminobutyrate degradation V
-
alanine degradation II (to D-lactate)
-
Alanine, aspartate and glutamate metabolism
-
Arginine and proline metabolism
-
ethylene biosynthesis IV
-
glutamate degradation I
-
glutamate degradation V (via hydroxyglutarate)
-
Metabolic pathways
-
methylaspartate cycle
-
Nitrogen metabolism
-
Taurine and hypotaurine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NAD+ oxidoreductase (deaminating)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dehydrogenase, glutamate
-
-
-
-
GDH
-
-
-
-
GDH
P00366
-
GDH isoenzyme 1
-
-
GDH isoenzyme 1
-
-
GDH, NAD-dependent
Q977U6
-
GDH, NAD-dependent
Haloferax mediterranei R-4
Q977U6
-
-
GDH1
-
beta subunit
GDH1
-
isozyme
GDH1
Q67C43
-
GDH1
Q852M0
-
GDH2
-
alpha subunit
GDH2
-
isozyme
GDH2
Q67C42
-
GDH2
Q852M0
-
GDH3
Q852M0
-
GdhA
-
alpha subunit
GDHB
-
beta subunit
Glu dehydrogenase
-
-
GLUD1
B5AAK2
isozyme
GLUD1
B5AAK3
isozyme
GLUD1
-
isozyme
GLUD1
B5AAJ9
isozyme
GLUD1
B5AAK0
isozyme
GLUD1
B5AAK1
isozyme
GLUD2
-
isozyme
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
P00366
-
glutamate dehydrogenase
Q50JE9
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
Q0E5H9, Q0E5I0
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
Q852M0
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase (NAD)
-
-
-
-
glutamate dehydrogenase alpha subunit
Q67C43
-
glutamate dehydrogenase beta subunit
Q67C42
-
glutamate oxidoreductase
-
-
-
-
glutamic acid dehydrogenase
-
-
-
-
glutamic dehydrogenase
-
-
-
-
hGDH1
-
-
hGDH2-nerve-specific GDH
-
-
house-keeping GDH
-
-
L-glutamate dehydrogenase
-
-
-
-
L-glutamate dehydrogenase
-
-
NAD(+)-dependent glutamate dehydrogenase
Q9TVN3
-
NAD(H)-dependent glutamate dehydrogenase
-
-
NAD(H)-dependent glutamate dehydrogenase
Q67C42, Q67C43
-
NAD(H)-dependent glutamate dehydrogenase
-
-
NAD+-dependant glutamate dehydrogenase
A0R1C2
-
NAD+-dependent GDH
-
-
NAD+-dependent GDH
-
-
NAD+-dependent GDH
-
-
NAD+-dependent GDH
-
-
NAD+-dependent GDH
-
-
-
NAD+-dependent GDHX
P29051
-
NAD+-dependent GDHX
Halobacterium salinarum NRC-36014
P29051
-
-
NAD+-dependent GluDH
-
-
NAD+-dependent glutamate dehydrogenase
-
-
NAD+-dependent glutamate dehydrogenase
-
-
NAD+-dependent glutamate dehydrogenase
P29051
-
NAD+-dependent glutamate dehydrogenase
Halobacterium salinarum NRC-36014
P29051
-
-
NAD+-dependent glutamate dehydrogenase
-
-
NAD+-GDH
A0R1C2
-
NAD+-glutamate dehydrogenase
-
-
NAD+-specific GDH
-
-
NAD+-specific glutamate dehydrogenase
P282997
-
NAD-dependent glutamate dehydrogenase
-
-
-
-
NAD-dependent glutamate dehydrogenase
-
-
NAD-dependent glutamate dehydrogenase
A5LH94
-
NAD-dependent glutamate dehydrogenase
-
-
NAD-dependent glutamic dehydrogenase
-
-
-
-
NAD-dependent L-glutamate dehydrogenase
A5LH94
-
NAD-dependent L-glutamate dehydrogenase
Janthinobacterium lividum UTB1302
A5LH94
-
-
NAD-GDH
-
-
-
-
NAD-GDH
Aspergillus niger NCIM 565
-
-
-
NAD-GDH
-
-
NAD-GDH
Q977U6
-
NAD-GDH
Haloferax mediterranei R-4
Q977U6
-
-
NAD-GDH
Janthinobacterium lividum UTB1302
A5LH94
-
-
NAD-glutamate dehydrogenase
-
-
-
-
NAD-glutamate dehydrogenase
-
-
NAD-glutamate dehydrogenase
Aspergillus niger NCIM 565
-
-
-
NAD-glutamate dehydrogenase
-
-
NAD-glutamate dehydrogenase
Q977U6
-
NAD-glutamate dehydrogenase
Haloferax mediterranei R-4
Q977U6
-
-
NAD-linked glutamate dehydrogenase
-
-
-
-
NAD-linked glutamic dehydrogenase
-
-
-
-
NAD-specific glutamate dehydrogenase
-
-
-
-
NAD-specific glutamic dehydrogenase
-
-
-
-
NAD:glutamate oxidoreductase
-
-
-
-
NADH-dependent GDH
-
-
NADH-dependent glutamate dehydrogenase
-
-
-
-
NADH-dependent glutamate dehydrogenase
-
-
NADH-dependent glutamate dehydrogenase
-
-
NADH-GDH
-
-
NADH-GDH
Q5BU42, Q5BU43, Q5BU44, Q5QDM6
-
NADH-GDH
-
-
NADH-GDH
Solanum lycopersicum Micro-Tom
-
-
-
NADH-glutamate dehydrogenase
-
-
NADH-linked glutamate dehydrogenase
-
-
-
-
OsGDH1
-
-
OsGDH2
-
-
OsGDH3
-
-
Pcal_1031
-
gene name
Pcal_1031
-
gene name
-
Surface-associated protein PGAG1
-
-
-
-
L-glutamate dehydrogenase
-
-
-
additional information
A0R1C2
NAD+-specific glutamate dehydrogenases belongs to the L_180 class, that is affected by the binding of a small protein, GarA
CAS REGISTRY NUMBER
COMMENTARY
9001-46-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Achlya sp.
-
-
-
Manually annotated by BRENDA team
Apodachlya sp.
-
-
-
Manually annotated by BRENDA team
genes GDH1-3
-
-
Manually annotated by BRENDA team
three genes GDH1, GDH2, and GDH3 encoding the enzyme subunits
-
-
Manually annotated by BRENDA team
strain NCIM 565
-
-
Manually annotated by BRENDA team
Aspergillus niger NCIM 565
strain NCIM 565
-
-
Manually annotated by BRENDA team
strain DSM 31
-
-
Manually annotated by BRENDA team
strain ISW1214
Uniprot
Manually annotated by BRENDA team
Bacillus subtilis ISW1214
strain ISW1214
Uniprot
Manually annotated by BRENDA team
two enzymes GDHA and GDHB
-
-
Manually annotated by BRENDA team
cultivar Bronowski
-
-
Manually annotated by BRENDA team
GDH isoenzymes 1 and 7, genes GDH1 and GDH2 encoding subunits alpha and beta
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
Clostridium botulinum 113B
113B
-
-
Manually annotated by BRENDA team
Clostridium difficile
-
-
-
Manually annotated by BRENDA team
Clostridium sp. SB4
SB4
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
strain DSMZ 2266T
SwissProt
Manually annotated by BRENDA team
the sequence has errornously been assigned as NADP+-dependent glutamate dehydrogenase in Benachenhou, N., Baldacci, G.: Mol. Gen. Genet, 230, 345-352 (1991)
SwissProt
Manually annotated by BRENDA team
Halobacterium salinarum NRC-36014
-
SwissProt
Manually annotated by BRENDA team
strain R4 (ATCC 33500)
SwissProt
Manually annotated by BRENDA team
Haloferax mediterranei R-4
strain R4 (ATCC 33500)
SwissProt
Manually annotated by BRENDA team
fragment; strain UTB1302
UniProt
Manually annotated by BRENDA team
Janthinobacterium lividum UTB1302
fragment; strain UTB1302
UniProt
Manually annotated by BRENDA team
European yellow lupine
UniProt
Manually annotated by BRENDA team
fragment; European yellow lupine
UniProt
Manually annotated by BRENDA team
glutamate dehydrogenase 1, fragment; European yellow lupine
UniProt
Manually annotated by BRENDA team
glutamate dehydrogenase 2, fragment; European yellow lupine
UniProt
Manually annotated by BRENDA team
gene msmeg_4699
UniProt
Manually annotated by BRENDA team
cv. Xanthi XHFD8 and cv. Xanthi G28
-
-
Manually annotated by BRENDA team
line A63-H
-
-
Manually annotated by BRENDA team
transgenic tobacco lines S4-H and S49-H, lines A63-NS and S49-NS as isogenic controls
-
-
Manually annotated by BRENDA team
var.Ti68, sense lines S4, S49 and S77 and antisense lines A44, A62, A63, A68 and A69
SwissProt
Manually annotated by BRENDA team
-
SwissProt
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
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
Scots pine
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
strain TAD1
-
-
Manually annotated by BRENDA team
TAD 1, two enzymes
-
-
Manually annotated by BRENDA team
strain TAD1
-
-
Manually annotated by BRENDA team
gene pcal_1031
-
-
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
-
-
Manually annotated by BRENDA team
Solanum lycopersicum Micro-Tom
three genes encoding the alpha-subunit, Slgdh-NAD;A1-3, and one additional gene encoding the beta-subunit of GDH, Slgdh-NAD;B1
-
-
Manually annotated by BRENDA team
Sulfolobus solfataricus MT-4
-
-
-
Manually annotated by BRENDA team
fragment; also named Symphalangus syndactylus
UniProt
Manually annotated by BRENDA team
PCC 6803
-
-
Manually annotated by BRENDA team
strain HB8
-
-
Manually annotated by BRENDA team
cultivar Yumai 34
-
-
Manually annotated by BRENDA team
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
16.5
-
2-oxoglutarate
P29051
pH 8.5, 40C, recombinant enzyme
2883
57.5
-
2-oxoglutarate
P29051
pH 8.5, 40C, recombinant enzyme in presence of DMSO
2883
71
-
2-oxoglutarate
-
pH 9.5, 50C, recombinant enzyme
2883
0.0018
-
L-glutamate
P29051
pH 9.0, 40C, recombinant enzyme in presence of DMSO
12211
0.0035
-
L-glutamate
P29051
pH 9.0, 40C, recombinant enzyme
12211
3.2
-
L-glutamate
-
pH 10.5, 50C, recombinant enzyme
12211
0.29
-
NAD+
-
mutant F232S/P262S/D263K , pH and temperature not specified in the publication
14330
0.72
-
NAD+
P29051
pH 9.0, 40C, recombinant enzyme
14330
0.75
-
NAD+
P29051
pH 9.0, 40C, recombinant enzyme in presence of DMSO
14330
149
-
NAD+
-
wild-type enzyme, pH and temperature not specified in the publication
14330
500
-
NAD+
-
pH 10.5, 50C, recombinant enzyme
14330
1.7
-
NADH
P29051
pH 8.5, 40C, recombinant enzyme
14331
1.9
-
NADH
P29051
pH 8.5, 40C, recombinant enzyme in presence of DMSO
14331
289
-
NADH
-
pH 6.0, 25C, mutant F238S/P262S
14331
329
-
NADH
-
pH 6.0, 25C, mutant A242G
14331
369
-
NADH
-
mutant F232S/P262S/D263K , pH and temperature not specified in the publication
14331
485
-
NADH
-
pH 6.0, 25C, mutant F238S
14331
553
-
NADH
-
pH 6.0, 25C, recombinant wild-type enzyme
14331
655
-
NADH
-
pH 8.0, 25C, mutant F238S/P262S
14331
663
-
NADH
-
pH 6.0, 25C, mutant D263K
14331
800
-
NADH
-
pH 6.0, 25C, mutant P262S
14331
1648
-
NADH
-
pH 8.0, 25C, mutant D263K
14331
1747
-
NADH
-
pH 8.0, 25C, mutant F238S
14331
2082
-
NADH
-
pH 8.0, 25C, mutant A242G
14331
2604
-
NADH
-
pH 7.0, 25C, mutant A242G
14331
2974
-
NADH
-
pH 8.0, 25C, recombinant wild-type enzyme
14331
3000
-
NADH
-
pH 7.0, 25C, mutant F238S/P262S
14331
3404
-
NADH
-
pH 7.0, 25C, mutant P262S
14331
3450
-
NADH
-
pH 8.0, 25C, mutant P262S
14331
3475
-
NADH
-
pH 7.0, 25C, mutant F238S
14331
3478
-
NADH
-
pH 7.0, 25C, mutant D263K
14331
5800
-
NADH
-
pH 9.5, 50C, recombinant enzyme
14331
6500
-
NADH
-
pH 7.0, 25C, recombinant wild-type enzyme
14331
8110
-
NADH
-
wild-type enzyme, pH and temperature not specified in the publication
14331
5.9
-
NH3
-
pH 9.5, 50C, recombinant enzyme
14472
45
-
NH3
P29051
pH 8.5, 40C, recombinant enzyme
14472
115
-
NH3
P29051
pH 8.5, 40C, recombinant enzyme in presence of DMSO
14472
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
pseudo-first-order kinetic plots for inactivation of F238S GDH by DTNB, overview
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0064
-
3,3'-[(2-bromobenzene-1,4-diyl)di(E)ethene-2,1-diyl]bis(6-hydroxybenzoic acid)
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0015
-
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
P00366
pH 7.5
0.0026
-
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
-
pH 7.5
0.1
-
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
-
value above 100, pH 7.5
0.0158
-
ATP/GTP-competitive inhibitor of casein kinase-2
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
-
0.0012
-
aurintricarboxylic acid
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0037
-
BH3I-2
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0048
-
Bithionol
P00366
pH 7.5
0.0055
-
Bithionol
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0059
-
Bithionol
-
pH 7.5
0.017
-
Bithionol
-
pH 7.5
0.0077
-
Calmidazolium
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0017
-
Diethylstilbestrol
-
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
-
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
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.05
-
erythrosin B
-
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
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0015
-
GW-5074
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0017
-
Hexachlorophene
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0019
-
Hexachlorophene
-
pH 7.5
0.0039
-
Hexachlorophene
P00366
pH 7.5
0.012
-
Hexachlorophene
-
pH 7.5
0.0328
-
metergoline
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
0.0138
-
suloctidil
-
in 0.1 M sodium phosphate buffer, pH 8.0, using 50 mM sodium glutamate and 0.2 mM NAD+
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
37
-
decreasing temperature results in much lower enzyme activity
10
43
-
10C: about 45% of maximal activity, 43C: about 75% of maximal activity
40
80
-
40C: about 50% of maximal activity, 80C: about 40% of maximal activity
40
90
P29051
temperature profile, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
10.5
-
Pcal_1031 retains more than 80% of its activity after incubation for 30 min at pH 4.0-10.5 at 50C
4
-
-
15 min, 30C, inactivation
6.5
7.2
-
15 min, 30C, stable
7
-
-
the wild type enzyme shows pH-dependent inactivation and conformational change and loses 91% of its activity over a few min on transfer from pH 7.0 to pH 8.8
8
-
-
15 min, 30C, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
extremely unstable at 0C to 4C due to the dissociation of the holoenzyme into catalytically inactive subunits
-
the enzyme resists proteolysis by trypsin, chymotrypsin or endoproteinase Glu-C at 25C. Above 30C the enzyme became cleavable by chymotrypsin, at a single site. Proteolysis is accompanied by the loss of enzyme activity. Proteolysis is prevented by either of the substrates 2-oxoglutarate or L-glutamate but not by the coenzymes NAD+ or NADH
-
the enzyme resists proteolysis by trypsin, chymotrypsin or endoproteinase Glu-C at 25C. Above 30C the enzyme becomes cleavable by chymotrypsin, at a single site. Proteolysis is accompanied by the loss of enzyme activity. Proteolysis is prevented by either of the substrates 2-oxoglutarate or L-glutamate but not by the coenzymes NAD+ or NADH
-
guanidine hydrochloride, 1.0 M, complete denaturation
-
ammonium sulfate improves stability
-
2-oxoglutarate stabilizes
-
ADP stabilizes
-
NADH stabilizes
-
DTT stabilizes
-
isophthalate stabilizes
-
NaCl, 0.1 M, stabilizes
-
potassium phosphate buffer, high concentration, stabilizes
-
presence of sulfhydryl groups in the environment stabilizes
-
strong dependence on high salt concentrations for stability
-
repeated freezing and thawing: loss of activity
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-propanol
P29051
GDHX retains 33% activity in 10% after 72 h, pH 8.5, room temperature. GDHX loses 94% of activity within 3 days in 10% solution
Acetone
P29051
GDHX retains 38% activity in 10% after 72 h, pH 8.5, room temperature
Acetone
Halobacterium salinarum NRC-36014
-
GDHX retains 38% activity in 10% after 72 h, pH 8.5, room temperature
-
acetonitrile
P29051
GDHX retains 30% activity in 10% after 72 h, pH 8.5, room temperature
acetonitrile
Halobacterium salinarum NRC-36014
-
GDHX retains 30% activity in 10% after 72 h, pH 8.5, room temperature
-
dimethylformamide
P29051
51% activity remaining after 72 h, pH 8.5, room temperature; GDHX retains 73% activity in 10% DMF after 30 min at pH 8.5, 40C, and 51% after 72 h, pH 8.5, room temperature
DMSO
P29051
GDHX retains 100% activity in the aqueous DMSO mixtures, high concentrations of salt may be substituted with 30% DMSO or betaine with good stability and activity
Ethanol
P29051
GDHX retains 34% activity in 10% after 72 h, pH 8.5, room temperature
Ethanol
Halobacterium salinarum NRC-36014
-
GDHX retains 34% activity in 10% after 72 h, pH 8.5, room temperature
-
Glycerol
P29051
GDHX retains 73% activity in 10% glycerol after 72 h, pH 8.5, room temperature
Glycerol
Halobacterium salinarum NRC-36014
-
GDHX retains 73% activity in 10% glycerol after 72 h, pH 8.5, room temperature
-
Methanol
P29051
GDHX retains more than 73% activity in 10% after 72 h, pH 8.5, room temperature
Methanol
Halobacterium salinarum NRC-36014
-
GDHX retains more than 73% activity in 10% after 72 h, pH 8.5, room temperature
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4-5C, 0.066 M phosphate buffer, pH 7.4 or 0.01 M arginine buffer, pH 9.5, 20 days, stable
-
-20C, loss of activity overnight
-
4C, 3 days, stable
-
-15C, 50 mM Tris-HCl, pH 7.5, 0.1 M KCl, stable for several months
Clostridium difficile
-
-20C, up to 1 year, stable
-
-20C, gradual loss of activity
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4C, suspension of 50% saturated ammonium sulfate, 0.1 mM DTT, 25 mM glutamate, stable for months
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4C, more than 90% of original activity retained after 20 days
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-20C, several months
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-5C, 20% loss of activity after 3 months
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