Information on EC 1.1.1.14 - L-iditol 2-dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.1.1.14
-
RECOMMENDED NAME
GeneOntology No.
L-iditol 2-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-iditol + NAD+ = L-sorbose + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-sorbitol degradation I
-
-
degradation of sugar alcohols
-
-
Fructose and mannose metabolism
-
-
Metabolic pathways
-
-
Pentose and glucuronate interconversions
-
-
SYSTEMATIC NAME
IUBMB Comments
L-iditol:NAD+ 2-oxidoreductase
This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals. It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol. Enzymes from different organisms or tissues display different substrate specificity. The enzyme is specific to NAD+ and can not use NADP+.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-21-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
(Kloeckera sp.) No. 2201
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
guinea pig
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Gluconobacter oxydans G624 (FERM BP-4415)
strain G624 (FERM BP-4415)
UniProt
Manually annotated by BRENDA team
strain IFO 3255
-
-
Manually annotated by BRENDA team
strain IFO3257
-
-
Manually annotated by BRENDA team
Gluconobacter sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
japanese pear
-
-
Manually annotated by BRENDA team
strain Si4 (DSM8371)
-
-
Manually annotated by BRENDA team
MIll. cv. Momotaro
SwissProt
Manually annotated by BRENDA team
expression of isoform Sdh1 is elevated in high-sugar mutants, after sugar injections, and more pronounced when transfected tissues are incubated at low oxygen concentrations
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
-
sorbitol dehydrogenase can convert sorbitol to fructose, which can then be metabolized via the glycolytic pathway in sperm to make ATP. Sorbitol can serve as an alternative energy source for sperm motility and protein tyrosine phosphorylation
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-deoxy-D-sorbitol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
6-deoxy-D-sorbitol + NAD+
? + NADH
show the reaction diagram
-
nearly 2fold higher activity compared to D-sorbitol
-
-
?
6-fluoro-D-sorbitol + NAD+
? + NADH
show the reaction diagram
-
over 2fold higher activity compared to D-sorbitol, best substrate
-
-
?
D-adonitol + NAD+
D-ribulose + NADH
show the reaction diagram
-
-
-
-
?
D-arabinose + NADH
?
show the reaction diagram
D-arabitol + NAD(P)+
D-xylulose + NAD(P)H + H+
show the reaction diagram
D-arabitol + NAD+
?
show the reaction diagram
D-arabitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
D-fructose + NADH
?
show the reaction diagram
Gluconobacter sp.
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
show the reaction diagram
D-galactitol + NAD+
D-tagatose + NADH
show the reaction diagram
D-gluconate + NAD+
?
show the reaction diagram
-
low activity
-
-
?
D-glucose + NADH
?
show the reaction diagram
-
low activity
-
-
?
D-glycero-D-gluco-heptitol + NAD+
?
show the reaction diagram
-
-
-
-
?
D-mannitol + NAD(P)+
D-fructose + NAD(P)H + H+
show the reaction diagram
D-mannitol + NAD+
?
show the reaction diagram
D-mannitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-mannose + NADH
?
show the reaction diagram
-
low activity
-
-
?
D-psicose + NADH
?
show the reaction diagram
-
-
-
-
?
D-raffinose + NADH
?
show the reaction diagram
-
low activity
-
-
?
D-ribitol + NAD+
?
show the reaction diagram
D-ribose + NADH
?
show the reaction diagram
-
low activity
-
-
?
D-ribulose + NADH
?
show the reaction diagram
D-sorbitol + 2,6-dichlorophenolindophenol
L-sorbose + ?
show the reaction diagram
-
electron acceptor: i.e. DCIP
-
-
?
D-sorbitol + NAD(P)+
L-sorbose + NAD(P)H + H+
show the reaction diagram
D-sorbitol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-sorbitol + NAD+
L-sorbose + NADH + H+
show the reaction diagram
D-sorbose + NADH
?
show the reaction diagram
-
low activity
-
-
?
D-tagatose + NADH
D-galactitol + NAD+
show the reaction diagram
D-xylitol + NAD+
?
show the reaction diagram
D-xylose + NADH
?
show the reaction diagram
D-xylulose + NADH
?
show the reaction diagram
erythritol + NAD+
?
show the reaction diagram
ethanol + NAD+
acetaldehyde + NADH
show the reaction diagram
glycerol + NAD+
?
show the reaction diagram
-
low activity
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
L-arabitol + NAD+
?
show the reaction diagram
L-erythrulose + NADH
?
show the reaction diagram
-
-
-
-
?
L-iditol + NAD+
?
show the reaction diagram
L-rhamnose + NADH
?
show the reaction diagram
-
low activity
-
-
?
L-sorbose + NADH
?
show the reaction diagram
L-threitol + NAD+
?
show the reaction diagram
meso-erythritol + NAD+
erythrulose + NADH
show the reaction diagram
-
high activity
-
-
?
ribitol + NAD+
?
show the reaction diagram
60% of the activity with D-sorbitol
-
-
?
sorbitol + NAD+
D-fructose + NADH
show the reaction diagram
Xylitol + NAD+
?
show the reaction diagram
29% of the activity with D-sorbitol
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
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-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-sorbitol + NAD+
L-sorbose + NADH + H+
show the reaction diagram
sorbitol + NAD+
D-fructose + NADH
show the reaction diagram
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
slightly activating
Fe3+
-
10 mM FeCl3 stimulates activity 2 fold
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S)-1-(3-thio-2-methylpropionyl)-L-proline
-
-
1,10-phenanthroline
1,2,3,4,5,6-cyclohexanehexolphosphoric acid
-
at pH 9.9
-
1,2-dithioethane
-
-
-
1,7-phenanthroline
-
-
1-thiobutane
-
-
1-thioglycol
-
-
1-thiosorbitol
-
-
2,2'-dipyridyl
-
-
2,3-Dimercaptopropanol
-
-
2,3-Dithiopropanol
-
-
2-hydroxybenzoic acid
-
at pH 9.9
2-hydroxymethyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
2-mercaptoethanol
-
-
2-methyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
i.e. SDI-157
2-methypropanoic acid amide
-
at pH 9.9
2-propylpentanoic acid
-
at pH 9.9
2-thiobutane
-
-
3,4-dihydroxyphenyl-1-hydroxyacetic acid
3,4-dihydroxyphenyl-ethanediol
-
at pH 7.4
3-hydroxy-4-methoxy-phenyl-1-hydroxy-acetic acid
-
at pH 7.4
4,4'-dipyridyl
-
-
4-hydroxy-3-methoxy-phenyl-1-hydroxy-acetic acid
-
at pH 7.4
4-hydroxy-3-methoxy-phenylacetic acid
-
at pH 7.4
4-hydroxy-3-methoxy-phenylethanediol
-
at pH 7.4
4-hydroxy-3-methoxy-phenylethyl alcohol
8-hydroxyquinoline
-
-
acetic acid amide
-
at pH 9.9
ADP
-
2 mM, 72% activity
Alrestatin
-
-
AMP
-
2 mM, 83% activity
ATP
-
2 mM, 54% activity
Ba(CH3COO)2
-
1 mM reduces activity to about 20%
Berberine
-
-
bis-diethylthiocarbamoyldisulfide
-
-
butanedioic acid
-
at pH 9.9
CdCl2
-
1 mM
Cibacron Blue 3G-A
-
-
CP-642,931
-
a potent and specific sorbitol dehydrogenase inhibitor, rmacokinetics, biomarker pharmacodynamics, and safety analysis, overview. The inhibitor is rapidly absorbed through the oral route and effectively inhibits SDH. However, the drug is not well tolerated due to adverse neuromuscular effects. The inhibitor alters the red blood cell sorbitol dehydrogenase activity after oral administration
-
cyanamide
cyanide
-
-
cysteamine
-
significant only at pH 9.9
cysteine
D-fructose
D-sorbitol
-
above 49 mM, substrate inhibition
Decanoic acid
-
at pH 9.9
diethyldicarbonate
-
-
Diethylthiocarbamate
Disulfiram
-
-
dithioerythritol
-
protection at low concentration, inhibition at high concentration, 100 mM
dithiothreitol
DL-2-bromosuccinate
-
1 mM
DL-2-thiovaline
-
-
DTT
-
competitive and noncompetitive with respect to D-sorbitol and NAD+, respectively
Eriochrome Black T
-
-
ethanedioic acid
-
at pH 9.9
Fe2+
-
complete inhibition at 0.91 mM
FeSO4
-
1 mM
glutathione
-
-
ICI 171071
-
-
ICI 222155
-
-
imidazole
-
-
iodoacetamide
-
NADH 0.4 mM protects
iodoacetate
Isonicotinic acid hydrazide
-
-
KCl
-
0.1 M, inactivation
Mg2+
-
slightly inhibitory
MgSO4
-
1 mM
Mn2+
-
slightly inhibitory
monoiodoacetate
-
75% inhibition at 1.79 mM
N-bromosuccinimide
-
-
N-ethylmaleimide
-
1 mM
o-phenanthroline
-
-
p-chloromercuribenzoate
p-hydroxymercuribenzoate
-
-
Pb(CH3COO)2
-
-
Penicillamine
-
weak inhibition
Ponalrestat
-
-
propanedioic acid
-
at pH 9.9
pyrazole
quercetin
quinine x HCl
-
slightly inhibitory, 25% inhibition at 1.79 mM
Semicarbazide
-
10 mM
thioacetate
-
at pH 9.9
Thiocyanate
Thiourea
-
at pH 9.9
Tolrestat
-
-
Urea
-
at pH 9.9
Valproic acid
-
weak inhibition
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-(-)-2-octanol
-
at pH 9.9
(S)-(+)-2-octanol
-
at pH 9.9
1-Hexanol
-
-
1-Octanol
-
-
2,2,2-tribromoethanol
-
-
2,2,2-trichloroethanol
-
-
2,2,2-Trifluoroethanol
-
-
2-monobromoethanol
-
-
2-monochloroethanol
-
-
2-monofluoroethanol
-
-
cysteine
-
fructose reduction at pH 7.4, inhibits at pH 9.0
D-sorbitol
-
at high concentration
dithiothreitol
-
1 mM 24% stimulation
haloalcohols
-
at high concentration
-
NaBr
-
-
NaCl
-
-
NaI
-
-
SDS
-
-
Semicarbazide
-
1 mM
Sodium azide
-
10 mM stimulates 2fold
sodium taurodeoxycholate
-
-
additional information
-
enzyme needs product, i.e. SldB, of upstream gene sldB, encoding a hydrophobic polypeptide, for activity, the polypeptide might be a chaperone-like component that signals processing and folding of the enzyme to give the active enzyme form
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.5
2-deoxy-D-sorbitol
1.9
3-deoxy-D-sorbitol
-
-
15.5
3-fluoro-D-sorbitol
-
-
26.4
4-deoxy-D-sorbitol
-
-
11.7
4-fluoro-D-sorbitol
-
-
0.48
6-deoxy-D-sorbitol
-
-
0.74
6-fluoro-D-sorbitol
-
-
1 - 1500
D-fructose
1.5 - 500
D-galactitol
6.2 - 9.1
D-glucitol
16 - 555
D-mannitol
1.3 - 125
D-ribitol
34 - 260
D-ribulose
0.0032 - 785
D-sorbitol
10 - 13
D-tagatose
0.17 - 37
D-xylitol
1
D-xylulose
-
-
20
L-arabitol
-
-
25
L-erythrulose
-
-
9 - 20
L-Iditol
110 - 800
L-sorbose
268
L-Threitol
-
-
0.041 - 0.6
NAD+
0.007 - 0.28
NADH
additional information
additional information
-
kinetic mechanism
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
441
3-deoxy-D-sorbitol
Ovis aries
-
-
350
3-fluoro-D-sorbitol
Ovis aries
-
-
129
4-deoxy-D-sorbitol
Ovis aries
-
-
354
4-fluoro-D-sorbitol
Ovis aries
-
-
274
6-deoxy-D-sorbitol
Ovis aries
-
-
559
6-fluoro-D-sorbitol
Ovis aries
-
-
0.71 - 506
D-sorbitol
0.63
D-xylitol
Rattus norvegicus
-
wild-type, pH 10.0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
1,2-dithioethane
-
pH 9.9
-
0.34
1-thiosorbitol
-
pH 9.9
0.007
2,3-Dithiopropanol
-
pH 9.9
0.00023 - 0.00025
2-hydroxymethyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
35
3,4-dihydroxyphenyl-1-hydroxyacetic acid
-
pH 9.9
1.7
4-hydroxy-3-methoxy-phenylethyl alcohol
-
pH 9.9
0.025
Berberine
-
pH 9.9
0.022
Cibacron Blue 3G-A
-
pH 9.9
10
cyanamide
-
pH 9.9
11
Diethylthiocarbamate
-
pH 9.9
0.0075
Disulfiram
-
pH 9.9
0.029
Eriochrome Black T
-
pH 9.9
0.22
NAD+
-
-
0.01
NADH
-
-
13
Penicillamine
-
pH 9.9
28
pyrazole
-
pH 9.9
0.072
quercetin
-
pH 9.9
22
Thiocyanate
-
pH 9.9
4.5
Valproic acid
-
pH 9.9
additional information
additional information
-
inhibition kinetics at different pH
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.62
-
purified recombinant enzyme
14.4
-
-
30.94
-
partially purified
45.3
-
purified enzyme
additional information
-
activity at growth in media with different pH values
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
native enzyme
5.6
-
D-fructose reduction
5.7 - 7
-
D-fructose reduction
5.9
-
D-fructose reduction
6 - 7.2
-
D-fructose reduction
6.1
-
D-fructose reduction
6.7
-
D-fructose reduction
7.4 - 8
-
D-fructose reduction
7.5
fructose reduction
8.1 - 8.5
-
sorbitol oxidation
8.8
-
D-fructose reduction
9
-
sorbitol oxidation
9 - 10.5
-
sorbitol oxidation
9 - 10
9
-
sorbitol oxidation
9.5
-
sorbitol oxidation
9.5 - 10.5
Gluconobacter sp.
-
assay at
9.5
-
assay at
10
-
sorbitol oxidation
10.1
recombinant enzyme
10.5
sorbitol oxidation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7 - 8
-
at pH 4.7 and 8 about 50% of activity maximum, D-fructose reduction
5 - 7
-
30% of maximal activity at pH 5.0 and 60% of maximal activity at pH 7.0, fructose reduction
5 - 7.5
-
less than 20% of maximal activity below pH 5, less than 80% above pH 7.5, fructose reduction
5 - 7
-
at pH 5.0 and pH 7.0 about 60% of maximal activity, fructose reduction
6 - 9
-
at pH 6 about 70% of maximal activity, at pH 9 about 40%, fructose reduction
6 - 7.2
-
less than 50% of maximal activity above and below, sugar reduction
7 - 10
-
40% of maximal activity at 7 and 70% of maximal activity at 10, sorbitol oxidation
7.5 - 9
-
less than 20% of maximal activity below pH 7.5, 100% at pH 9.0, sorbitol oxidation
7.5 - 10
-
at pH 7.5 about 70% of maximal activity, at pH 10 about 100%, sorbitol oxidation
7.5 - 9.5
-
at pH 7.5 and pH 9.5 about 70% of maximal activity, sorbitol oxidation
8 - 11
-
at pH 8 and 11 about 50% of activity maximum, sorbitol oxidation
9 - 10.5
-
less than 70% of maximal activity above and below, sorbitol oxidation
9.2 - 11.6
-
less than 50% of maximal activity above and below, sorbitol oxidation
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
40
Gluconobacter sp.
-
D-sorbitol oxidation
50
Gluconobacter sp.
-
D-fructose reduction
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 50
-
50% of maximal activity at 15C, 40% of maximal activity at 50C
30 - 50
-
maximal activity at 30C, 40% activity at 45C, 30% activity at 50C, no activity at 60C
35 - 65
-
35C: about 50% of activity maximum, 65C: about 95% of activity maximum
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
-
isoelectric focusing, pI value isoform present in seed
4.8
-
isoelectric focusing, pI value isoform present in seed
5.5
-
isoelectric focusing, pI value isoform present in seed and cortex
6.1
-
calculated
6.3
-
isoelectric focusing, pI value isoform present in seed and cortex
7.3
-
isoelectric focusing, pI value isoform present in cortex
8.3
-
isoelectric focusing, pI value isoform present in cortex
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isoform Sdh1, specific for kernel and endosperm
Manually annotated by BRENDA team
-
cell culture derived from the kidney inner medulla
Manually annotated by BRENDA team
-
isoform Sdh1, specific for kernel and endosperm. Maximaml expression at both mRNA and enzyme activity level during early kernel development
Manually annotated by BRENDA team
-
tissue culture
Manually annotated by BRENDA team
-
ventral and dorsal
Manually annotated by BRENDA team
-
enzyme activity is higher in seed than in cortex per mg and fresh weight. Isoforms SDH1 and SDH3 are expressed in both seed and cortex tissue, isoform SDH2 expression is limited to cortex
Manually annotated by BRENDA team
-
activity is higher than in cortex per mg and fresh weight, and contributes significantly to whole fruit activity during weeks 2-5 after bloom. Isoforms SDH1 and SDH3 are expressed in both seed and cortex tissue. Isoforms SDH6 and SDH9 are expressed in seed tissues only
Manually annotated by BRENDA team
-
shoot tip
Manually annotated by BRENDA team
-
SORD is present along the entire length of sperm flagellum, but does not show the same distribution pattern as alpha-tubulin. Sord mRNA and SORD protein expression is up-regulated during late spermiogenesis
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
plus 80000, 160000 and 300000, mutant Y110F
53640
calculated from amino acid sequence
61000
-
Stokes' radius, sedimentation coefficient
63000
-
gel filtration
65800
-
Stokes' radius, sedimentation coefficient
80000
-
plus 160000, 40000 and 300000, mutant Y110F
95000
-
gel filtration
97000
-
disc gel electrophoresis
106000
-
gel filtration
110000
-
gel filtration
115000
-
ultracentrifugal analysis
120000
-
gel filtration
140000
-
gel filtration
153000
-
gel filtration
155000
156000
-
gel filtration
160000
-
plus 80000, 40000 and 300000, mutant Y110F
300000
-
above 300000, wild-type and part of mutant Y110F
800000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
monomer
tetramer
trimer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified enzyme alone, and in complex with NAD+, or with NADH and inhibitor SDI-158, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution, modelling
purified recombinant enyme, hanging drop vapour diffusion method, 22C, enzyme is complexed with cofactor NAD+ in a molar ratio 1:6, 0.0025 ml protein solution mixed with 0.002 ml well solution containing 0.1 M Tris, pH 8.6, 0.2 M sodium acetate, 10% PEG 3350, and with 0.0005 ml 30% v/v 2-methyl-2,4-pentanediol, 1 week, X-ray diffraction structure determination and analysis at 2.75 A resolution
-
sitting drop vapour-diffusion method. Sorbitol dehydrogenase is crystallized in the absence of the cofactor NAD(H) and its structure is determined to 2.4 A resolution using molecular replacement
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 11
-
several days at 4C
285897
4.5
-
at lower pH denaturation occurs
285874
5 - 9
-
30 min at 30C
285896
6
-
loses zinc at lower pH
285892
7 - 8
-
12 h at 4C
285901
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
50% loss of activity after 4 days
18
-
50% loss of activity after 40 min, alpha-crystallin protects fully against activity loss
21
-
50% loss of activity after 2 days, non-purified enzyme in serum
22
-
5 h, stable
35
-
stable up to
45
-
50% loss of activity after 20 min, alpha-crystallin protects fully against activity loss
55
-
50% loss of activity after 10 min, alpha-crystallin protects fully against activity loss
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.1 mg/ml bovine serum albumin stabilizes at -20C
-
0.1 mg/ml bovine serum albumin stabilizes at 4C
-
0.1 mg/ml bovine serum albumin stabilizes at room temperature
-
1 mM dithiothreitol reduces stability
-
278 mM maltose stabilizes at 4C
-
30% sucrose stabilizes
6.8 M glycerol stabilizes at 4C
-
alpha-crystallin stabilizes
-
bovine serum albumin stabilizes
-
bovine serum albumin stabilizes at 4C
-
complete renaturation, alpha-crystallin has the ability to elicit protein refolding. This action of alpha-crystallin appears not to be dependent on ATP as energy donor, but essentially associated with intrinsic structural features of this chaperone molecule
-
dithioerythritol protects at 1 mM, inhibits at 100 mM
-
dithiothreitol protects at 1 mM at 4C
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freezing to -20C, loss of activity
-
freezing, loss of activity
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Triton X-100, 1%, and D-sorbitol stabilize the enzyme during solubilization and purification, while n-octyl-beta-D-glucopyranoside does not
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, 2 days, non-purified enzyme in serum
-
-20C, 70% loss of activity after 1 week, 0.1 mg/ml bovine serum albumin stabilizes
-
-20C, purified recombinant enzyme, 3d, almost complete loss of activity
-20C, stable for 4 months
-
-60C, 5 mM 2-mercaptoethanol, several months
-
-85C, good preservation
-
4C several days
-
4C, 2 mM dithiothreitol, 0.1 mM NADH, 15 days
-
4C, 20 mM potassium phosphate buffer, pH 7.0, 3 months
-
immobilized enzyme loses 20% of activity after 10 days at room temperature
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by solubilization with Triton X-100, DEAE-cellulose and -Sepharose, hydroxylapatite, and size exclusion chromatography, efficiency of different solubilization methods, overview
-
cobalt-based resin affinity chromatography
further purification from commercial preparation
-
recombinant from Escherichia coli by ammonium sulfate precipitation, anion-exchange and dye affinity cromatography, 23fold
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, co-expression with gene sldB in Escherichia coli strain JM109, sldB and PQQ are required for recombinant activity in Escherichia coli, co-expression of sldB is also required for enzyme activity in vivo
expressed in Pseudomonas putida strain IFO3738 fused to 6 x His-tag
expression in Escherichia coli
-
expression in Escherichia coli strain BL21
-
expression of wild-type and mutant enzymes in Escherichia coli
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gene MdSDH5, DNA and amino acid sequence determination and analysis, transient expression of MdSDH5-GFP and MdSDH6-GFP in the mesophyll protoplast of Arabidopsis thaliana; gene MdSDH6, DNA and amino acid sequence determination and analysis, phylogenetic tree, transient expression of MdSDH5-GFP and MdSDH6-GFP in the mesophyll protoplast of Arabidopsis thaliana
multiple genes, DNA sequence determination and analysis, a cDNA is expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
zinc-finger protein ZAC1 is up-regulated under hypertonic stress and negatively regulates expression of SDH
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E154C
-
purified preparations of mutant contain 0.1-0.4 atoms of Zn2+ per subunit and exhibit a constant catalytic Zn2+ centre activity of 1.19 per s, mutant does not require exogenous Zn2+ for stability. Mutant retains less than 1% of wild-type catalytic efficiency and displays similar primary and solvent deuterium effects as wild-type
Y110F
-
mutation in hydrogen onding network, complete loss of activity and destabilization of protein into tetramers, dimers and monomers compared to only tetramers for wild-type
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
synthesis
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