Information on EC 1.1.1.307 - D-xylose reductase

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

EC NUMBER
COMMENTARY hide
1.1.1.307
-
RECOMMENDED NAME
GeneOntology No.
D-xylose reductase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xylitol + NAD(P)+ = D-xylose + NAD(P)H + H+
show the reaction diagram
xylitol + NAD+ = D-xylose + NADH + H+
show the reaction diagram
xylitol + NADP+ = D-xylose + NADPH + H+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
Pentose and glucuronate interconversions
-
-
SYSTEMATIC NAME
IUBMB Comments
xylitol:NAD(P)+ oxidoreductase
Xylose reductase catalyses the initial reaction in the xylose utilization pathway, the NAD(P)H dependent reduction of xylose to xylitol.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain F-3
-
-
Manually annotated by BRENDA team
strain F-3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
KFCC-10875
SwissProt
Manually annotated by BRENDA team
strain VGI-II
-
-
Manually annotated by BRENDA team
strain VGI-II
-
-
Manually annotated by BRENDA team
strain CBS 4435
SwissProt
Manually annotated by BRENDA team
IF0 0618
-
-
Manually annotated by BRENDA team
SCTCC 300249
UniProt
Manually annotated by BRENDA team
strain Y-456
-
-
Manually annotated by BRENDA team
gene XYL1
-
-
Manually annotated by BRENDA team
strain UFV-170 XR
-
-
Manually annotated by BRENDA team
strain UFV-170 XR
-
-
Manually annotated by BRENDA team
strain Y-1017
-
-
Manually annotated by BRENDA team
strain Y-1632
-
-
Manually annotated by BRENDA team
strain Y-2160
-
-
Manually annotated by BRENDA team
Torulopsis molishiama
strain 55
-
-
Manually annotated by BRENDA team
Torulopsis molishiama 55
strain 55
-
-
Manually annotated by BRENDA team
ssp. mobilis, and strain A3, an engineered strain ZM4 that is adapted to 5% D-xylose, gene ZMO0976
UniProt
Manually annotated by BRENDA team
ssp. mobilis, and strain A3, an engineered strain ZM4 that is adapted to 5% D-xylose, gene ZMO0976
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-galactose + NADH
?
show the reaction diagram
-
-
-
?
2-deoxy-D-galactose + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
2-deoxy-D-galactose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
2-deoxy-D-glucose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
2-deoxy-D-ribose + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
2-deoxy-D-ribose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
5-hydroxymethylfurfural + NADH + H+
(furan-2,5-diyl)dimethanol + NAD+
show the reaction diagram
9,10-phenanthrenequinone + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
show the reaction diagram
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
show the reaction diagram
butanal + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
butanal + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-arabinose + NADPH + H+
?
show the reaction diagram
D-arabinose + NADPH + H+
D-arabinitol + NADP+
show the reaction diagram
D-erythrose + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
D-erythrose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-erythrose + NADPH + H+
D-erythritol + NADP+
show the reaction diagram
D-erythrose + NADPH + H+
erythritol + NADP+
show the reaction diagram
-
catalytic efficiency is 100fold higher than the catalytic efficiency for D-xylose
-
-
?
D-fucose + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
D-fucose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-galactose + NADH
?
show the reaction diagram
-
-
-
?
D-galactose + NADH + H+
?
show the reaction diagram
D-galactose + NADPH + H+
?
show the reaction diagram
D-glucose + NADH
?
show the reaction diagram
-
-
-
?
D-glucose + NADH + H+
?
show the reaction diagram
D-glucose + NADPH + H+
?
show the reaction diagram
D-glucosone + NADPH + H+
D-fructose + NADP+
show the reaction diagram
-
catalytic efficiency is 22fold higher than the catalytic efficiency for D-xylose
-
-
?
D-glyceraldehyde + NADH
?
show the reaction diagram
-
-
-
?
D-lyxose + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
D-lyxose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
D-mannose + NADH + H+
?
show the reaction diagram
8% of the activity compared to D-xylose (with NADH as cofactor)
-
-
?
D-ribose + NADH + H+
?
show the reaction diagram
D-ribose + NADPH + H+
?
show the reaction diagram
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
show the reaction diagram
D-xylose + NADH + H+
xylitol + NAD+
show the reaction diagram
D-xylose + NADPH + H+
xylitol + NADP+
show the reaction diagram
DL-glyceraldehyde + NADH + H+
glycerol + NAD+
show the reaction diagram
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
show the reaction diagram
furfural + NADH + H+
(furan-2-yl)methanol + NAD+
show the reaction diagram
L-arabinose + NADH + H+
arabinitol + NAD+
show the reaction diagram
-
low activity in direction of arabinitol oxidation. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol
-
-
r
L-arabinose + NADH + H+
L-arabinitol + NAD+
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
L-arabinose + NADPH + H+
arabinitol + NADP+
show the reaction diagram
-
low activity in direction of arabinitol oxidation. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol
-
-
r
L-arabinose + NADPH + H+
L-arabinitol + NADP+
show the reaction diagram
L-arabinose + NADPH + H+
L-arabitol + NADP+
show the reaction diagram
-
-
-
-
?
L-lyxose + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
L-lyxose + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
methylglyoxal + NADPH + H+
?
show the reaction diagram
-
catalytic efficiency is 20fold higher than the catalytic efficiency for D-xylose
-
-
?
pentanal + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
pentanal + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
phenylglyoxal + NADPH + H+
?
show the reaction diagram
-
catalytic efficiency is 17fold higher than the catalytic efficiency for D-xylose
-
-
?
propionaldehyde + NADH + H+
?
show the reaction diagram
-
dual specific xylose reductase (dsXR)
-
-
?
propionaldehyde + NADPH + H+
?
show the reaction diagram
-
NADPH-dependent monospecific xylose reductase
-
-
?
pyridine-2-aldehyde + NADPH + H+
?
show the reaction diagram
-
catalytic efficiency is 7fold higher than the catalytic efficiency for D-xylose
-
-
?
valeraldehyde + NADPH + H+
?
show the reaction diagram
-
catalytic efficiency is 13fold higher than the catalytic efficiency for D-xylose
-
-
?
xylitol + NAD+
D-xylose + NADH + H+
show the reaction diagram
xylitol + NADP+
D-xylose + NADPH + H+
show the reaction diagram
xylosone + NADPH + H+
?
show the reaction diagram
-
catalytic efficiency is 20fold higher than the catalytic efficiency for D-xylose
-
-
?
xylulose + NADH + H+
? + NAD+
show the reaction diagram
-
-
-
r
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
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
show the reaction diagram
D-xylose + NADH + H+
xylitol + NAD+
show the reaction diagram
D-xylose + NADPH + H+
xylitol + NADP+
show the reaction diagram
xylitol + NAD+
D-xylose + NADH + H+
show the reaction diagram
xylitol + NADP+
D-xylose + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
NADP+
additional information
-
Kluyveromyces marxianus strains expressing Pichia stipitis Psxyl1 genes show reversed cofactor specificity, overview
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
1 mM, stimulates
CoCl2
1 mM, stimulates
FeCl2
1 mM, stimulates
Li+
Ca2+, Li+, Mg2+, Mn2+ and NH4+ at 10 mM decrease activity by 10-50%
Mg2+
Ca2+, Li+, Mg2+, Mn2+ and NH4+ at 10 mM decrease activity by 10-50%
MgCl2
1 mM, stimulates
Mn2+
Ca2+, Li+, Mg2+, Mn2+ and NH4+ at 10 mM decrease activity by 10-50%
MnCl2
1 mM, stimulates
NH4+
Ca2+, Li+, Mg2+, Mn2+ and NH4+ at 10 mM decrease activity by 10-50%
NiCl2
1 mM, stimulates
ZnCl2
1 mM, stimulates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
-
2 mM, completely abolishes D-xylose reduction
ATP
-
2 mM, completely abolishes D-xylose reduction, competitive
cholic acid
-
0.1% (w/v), 30% inhibition
Cu2+
activity is completely restored by addition of EDTA
deoxycholic acid
-
0.1% (w/v), 30% inhibition
dithiothreitol
DTT
1 mM, 35% inhibition
EDTA
-
1 mM, 30% inhibition
Hg2+
-
0.001 mM, 2 min, complete inhibition
Mn2+
-
25 mM, 95% inhibition
N-bromosuccinimide
-
NADPH protects
NaCl
-
50 mM, 25% inhibition
NADP+
NADPH
-
for monospecific xylose reductase (msXR) and dual specific xylose reductase (dsXR) NADPH behaves as a competitive inhibitor against NADP+. Competitive inhibition of is observed both at unsaturating and saturating concentrations of xylitol
p-chloromercuribenzoate
-
0.001 mM, 2 min, complete inhibition
pyridoxal 5'-phosphate
-
gradual inactivation. NADH, ATP or 2'-AMP protects. No protection by D-xylose
sodium phosphite
-
200 mM, 37% inhibition
xylitol
non-competitive against NADH and D-xylose
Zn2+
-
25 mM, 95% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
1 mM, increases activity by 13%
bovine serum albumin
-
cysteine
1 mM, increases activity by 29%
dithiothreitol
1 mM, increases activity by 43%
DTT
1 mM, 27% increase of activity
glutathione
1 mM, increases activity by 21%
Triton X-100
Tween 20
0.1%, the specific activity is increased by 20-30%
Tween 80
0.1%, the specific activity is increased by 20-30%
Tween-20
-
0.1% (w/v), 10-15% activation
Tween-80
-
0.1% (w/v), 10-15% activation
additional information
neither inhibited nor activated by EDTA at concentrations ranging from 1 to 10 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.126 - 0.221
2-deoxy-D-galactose
0.058
2-deoxy-D-glucose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.038
2-deoxy-D-ribose
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
1.8
benzaldehyde
pH 7.2, temperature not specified in the publication
2 - 33
Butanal
285.4
D-arabinose
pH 6.0
0.02 - 151.7
D-erythrose
0.007 - 0.01
D-fucose
0.015 - 180
D-galactose
0.006 - 360
D-glucose
0.068 - 302
D-ribose
0.01 - 722
D-xylose
1.14 - 2.43
DL-glyceraldehyde
4.2
furfural
pH 7.2, temperature not specified in the publication
0.02 - 93
L-arabinose
0.117 - 0.144
L-Lyxose
0.027 - 0.0587
NAD+
0.0033 - 40
NADH
0.0266
NADP+
-
pH 7, 25°C
0.0018 - 7.6
NADPH
3.9 - 14.7
pentanal
13.2 - 78
propionaldehyde
209 - 537
xylitol
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5 - 8.4
2-deoxy-D-galactose
6.8
2-deoxy-D-glucose
Candida intermedia
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
1.4
2-deoxy-D-ribose
Candida intermedia
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
0.027 - 12
9,10-phenanthrenequinone
5.4 - 21.2
Butanal
24.3 - 27.5
D-erythrose
10.2 - 20.7
D-fucose
9.4 - 1800
D-galactose
8.2 - 1320
D-glucose
4.9 - 3120
D-ribose
0.002 - 324000
D-xylose
14.1 - 24.3
DL-glyceraldehyde
13.5 - 1800
L-arabinose
5.6
L-idose
Candida intermedia
-
pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH
6.6 - 18.4
L-Lyxose
0.89 - 0.92
NAD+
4.7 - 25110
NADH
0.82
NADP+
Candida tenuis
-
pH 7, 25°C
2.6 - 324000
NADPH
5.9 - 20.7
pentanal
4.6 - 6.9
propionaldehyde
0.87 - 0.92
xylitol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.7 - 38
2-deoxy-D-galactose
2006
117
2-deoxy-D-glucose
Candida intermedia
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
531
36.8
2-deoxy-D-ribose
Candida intermedia
-
pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH
2811
20 - 2300
9,10-phenanthrenequinone
558
0.16 - 0.93
Butanal
540
0.028
D-arabinose
Candida parapsilosis
Q6Y0Z3
pH 6.0
565
0.089 - 1380
D-erythrose
1442
1457 - 2070
D-fucose
1256
0.16 - 627
D-galactose
71
0.05 - 1370
D-glucose
35
0.043 - 134
D-ribose
292
0.0009 - 27430
D-xylose
115
0.3 - 21.3
DL-glyceraldehyde
487
0.75 - 1230
L-arabinose
206
46 - 157
L-Lyxose
1647
15.2 - 34.1
NAD+
7
81.7 - 83750
NADH
8
30.9
NADP+
Candida tenuis
-
pH 7, 25°C
10
6.2 - 1466000
NADPH
5
0.4 - 5.31
pentanal
781
0.035 - 0.09
propionaldehyde
273
0.0034 - 0.031
xylitol
416
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0239
ATP
-
pH 7, 25°C, variable substrate: NADH
0.034
Cu2+
pH 6.0
0.074 - 0.65
NAD+
0.0019 - 0.02
NADH
0.0015 - 0.17
NADP+
0.014
NADPH
-
pH 7.0, 25°C, dual specific xylose reductase (dsXR)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.11
Torulopsis molishiama
-
-
0.16 - 0.4
-
recombinant enzyme in transgenic strains of Saccharomyces cerevisiae
0.48
-
cell extract
1.39 - 1.56
-
NADH-dependent activity
2
-
mutant enzyme Y49F
2.4
mutant K21A, substrate NADH, pH 6.5, 35°C
2.86
-
recombinant strain LNG2, pH 7.0, 25°C, xylose reduction with NADPH
3.4
-
NADPH-dependent activity
4.84
-
NADPH-dependent activity
4.93
-
NADH-dependent activity
5
mutant K21A, substrate NADPH, pH 6.5, 35°C
6.6
wild-type, substrate NADH, pH 6.5, 35°C
10.37
-
NADH-dependent activity
16.7
-
NADH-dependent activity
20.3
wild-type, substrate NADPH, pH 6.5, 35°C
22.1
-
NADPH-dependent activity
23.2
-
NADPH-dependent activity
47.8
-
D-xylose reductase 3
56.9
-
D-xylose reductase 1
81
-
D-xylose reductase 2
104
-
wild-type enzyme
251.5
cofactor: NADPH
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
assay at
8.9
-
xylitol oxidation
additional information
-
use of response surface analysis for the maximization of xylose reductase activity as a function of pH and temperature. This methodology also makes it possible to determine a desirable working region where a high xylose reductase to xylitol dehydrogenase ratio can be attained
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6.5
pH 4.0: about 55% of maximal activity, pH 6.5: about 60% of maximal activity
4 - 7
-
pH 4.0: about 40% of maximal activity, pH 7.0: about 50% of maximal activity
4.5 - 7.5
-
pH 4.5: about 55% of maximal activity, pH 7.5: about 50% of maximal activity
5 - 7
pH 5.0: 81% of maximal activity, pH 7.0: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
use of response surface analysis for the maximization of xylose reductase activity as a function of pH and temperature. This methodology also makes it possible to determine a desirable working region where a high xylose reductase to xylitol dehydrogenase ratio can be attained
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 40
-
activity increases linearly from 25°C to 50°C
25 - 65
-
25°C: about 55% of maximal activity, 65°C: about 65% of maximal activity
30 - 60
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.1
-
D-xylose reductase 2, isoelectric focusing, pH-range: 2.5-5.0
4.15
-
D-xylose reductase 1, isoelectric focusing, pH-range: 2.5-5.0
4.7
-
isoelectric focusing
5.19
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
the organism grows on rice straw hemicellulosic hydrolysate, as the only source of nutrient, optimization of culture conditions for production of xylitol from D-xylose, xylitol dehydrogenase remains constant, whereas the level of xylose reductase decreases when the initial xylose concentration is increased from 30 to 70 g/l, development of enzyme activities, overview
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
2 * 29000, SDS-PAGE
34000
-
2 * 34000, SDS-PAGE
36400
2 * 36400, SDS-PAGE
36600
x * 36600, calculated
36629
2 * 36629, calculated from sequence
37100
x * 37100, SDS-PAGE
38400
-
2 * 38400, SDS-PAGE
40000
x * 36000, calculated, x * 40000, SDS-PAGE; x * 40000, wild-type and double-mutant (K271R/N273D) histidine-tagged protein, SDS-PAGE
43000
-
1 * 43000, SDS-PAGE
48000
-
gel filtration
53000
-
gel filtration
58000
-
D-xylose reductase 1, D-xylose reductase 2, D-xylose reductase 3, gel filtration
60000
-
gel filtration
63000 - 65000
-
gel filtration
69000
gel filtration
364978
-
2 * 364978, D-xylose reductase 1, ion-spray mass spectrometry
365540
-
2 * 365540, D-xylose reductase 2, ion-spray mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 43000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the purified N309D mutant is crystallized by the hanging-drop vapour-diffusion method at 25°C. The best-diffracting crystals are grown using a well solution consisting of 2.1 M (NH4)2SO4, 100 mM sodium acetate and 100 mM sodium citrate, pH 6.4. Comparison of the 2.4 A X-ray crystal structure of mutant N309D bound to NAD+ with the previous structure of the wild-type holoenzyme reveals no major structural perturbations
-
hanging-drop vapour diffusion method, to 2.91 A resolution. Unit cell belongs to space group P31 or P32, presence of four XR molecules in the asymmetric unit, with 68.0% solvent content; hanging-drop vapour-diffusion method. X-ray diffraction data from xylose reductase crystals at 2.91 A resolution, the unit cell belongs to space group P3(1) or P3(2). Preliminary analysis indicates the presence of four xylose reductase molecules in the asymmetric unit, with 68.0% solvent content
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
below pH 5 and above pH 8.0 the enzyme is inactivated within 3-6 days
286260
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
60 days, 50% loss of activity
20
8 days, 50% loss of activity
21
-
at room temperature stable for more than 1 month
25
-
half-life: more than 2 months
30
3 days, 50% loss of activity
30 - 35
-
48 h, stability starts to decrease above 30-35°C
40
-
half-life: 94 min
45
4.5 h, 50% loss of activity
50
2 min, 50% loss of activity
additional information
-
non-ionic detergents and bovine serum albumin stabilize the enzyme to a significant extent during long-term incubation at 25°C, 30°C or 38°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable enzyme at 25°C in phosphate and Tris buffer of various ionic strengths between pH 6.0 and 7.0
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme undergoes thiol oxidation during storage or purification
-
286260
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 4 months, activity in cell extract remains stable
-
-20°C, pure enzyme preparation is stable for more than 4 months
-
38°C, 3 h, activity in cell extract remains stable
-
4°C, 3 h, activity in cell extract remains stable
-
4°C, enzyme retains activity for several months
4°C, pure enzyme preparation is stable for more than 4 months
-
4°C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant enzyme