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Information on EC 1.1.1.56 - ribitol 2-dehydrogenase for references in articles please use BRENDA:EC1.1.1.56
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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
adonitol dehydrogenase, NAD+-dependent ribitol dehydrogenase, RDH, ribitol dehydrogenase A, ribitol dehydrogenase B, ribitol dehydrogenase D, ribitol-specific dehydrogenase, ribitol: NAD+ 2-oxidoreductase,
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adonitol dehydrogenase
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NAD+-dependent ribitol dehydrogenase
ribitol dehydrogenase A
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wild type
ribitol dehydrogenase B
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mutant enzyme with different properties
ribitol dehydrogenase D
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mutant enzyme with different properties
ribitol-specific dehydrogenase
ribitol: NAD+ 2-oxidoreductase
NAD+-dependent ribitol dehydrogenase
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NAD+-dependent ribitol dehydrogenase
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RDH
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ribitol-specific dehydrogenase
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ribitol-specific dehydrogenase
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ribitol: NAD+ 2-oxidoreductase
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ribitol: NAD+ 2-oxidoreductase
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ribitol: NAD+ 2-oxidoreductase
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ribitol + NAD+ = D-ribulose + NADH + H+
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ribitol:NAD+ 2-oxidoreductase
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allitol + NAD+
D-psicose + NADH
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r
D-arabitol + NAD+
D-xylulose + NADH + H+
D-glucitol + NAD+
? + NADH
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?
D-psicose + NADH + H+
allitol + NAD+
D-sorbitol + NAD+
L-sorbose + NADH + H+
erythritol + NAD+
? + NADH
L-arabitol + NAD+
L-xylulose + NADH + H+
L-talitol + NAD+
L-tagatose + NADH
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r
ribitol + NAD+
D-ribulose + NADH
ribitol + NAD+
D-ribulose + NADH + H+
xylitol + NAD+
D-xylulose + NADH + H+
additional information
?
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D-arabitol + NAD+
D-xylulose + NADH + H+
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?
D-arabitol + NAD+
D-xylulose + NADH + H+
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?
D-arabitol + NAD+
D-xylulose + NADH + H+
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?
D-psicose + NADH + H+
allitol + NAD+
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?
D-psicose + NADH + H+
allitol + NAD+
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?
D-sorbitol + NAD+
L-sorbose + NADH + H+
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?
D-sorbitol + NAD+
L-sorbose + NADH + H+
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?
erythritol + NAD+
? + NADH
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?
erythritol + NAD+
? + NADH
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?
L-arabitol + NAD+
L-xylulose + NADH + H+
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L-arabitol + NAD+
L-xylulose + NADH + H+
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?
L-arabitol + NAD+
L-xylulose + NADH + H+
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r
L-arabitol + NAD+
L-xylulose + NADH + H+
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ribitol + NAD+
D-ribulose + NADH
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ribitol + NAD+
D-ribulose + NADH
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ribitol + NAD+
D-ribulose + NADH
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?
ribitol + NAD+
D-ribulose + NADH
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ribitol + NAD+
D-ribulose + NADH
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ribitol + NAD+
D-ribulose + NADH + H+
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?
ribitol + NAD+
D-ribulose + NADH + H+
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?
ribitol + NAD+
D-ribulose + NADH + H+
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85% yield
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?
ribitol + NAD+
D-ribulose + NADH + H+
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?
ribitol + NAD+
D-ribulose + NADH + H+
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high activity
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?
ribitol + NAD+
D-ribulose + NADH + H+
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high activity
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?
xylitol + NAD+
D-xylulose + NADH + H+
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?
xylitol + NAD+
D-xylulose + NADH + H+
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r
xylitol + NAD+
D-xylulose + NADH + H+
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mutants have increased xylitol activity
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?
xylitol + NAD+
D-xylulose + NADH + H+
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?
xylitol + NAD+
D-xylulose + NADH + H+
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?
additional information
?
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no activity with NADP+
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additional information
?
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no activity with NADP+
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additional information
?
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no activity with NADP+
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additional information
?
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the enzyme shows 8.6% activity with allitol, low activity with xylitol (1.8%) and no activity with D-sorbitol, L-arabitol, galactitol, D-mannitol, inositol and glycerol
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additional information
?
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the enzyme shows 8.6% activity with allitol, low activity with xylitol (1.8%) and no activity with D-sorbitol, L-arabitol, galactitol, D-mannitol, inositol and glycerol
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ribitol + NAD+
D-ribulose + NADH
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?
ribitol + NAD+
D-ribulose + NADH + H+
ribitol + NAD+
D-ribulose + NADH + H+
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?
ribitol + NAD+
D-ribulose + NADH + H+
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?
ribitol + NAD+
D-ribulose + NADH + H+
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?
ribitol + NAD+
D-ribulose + NADH + H+
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high activity
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?
ribitol + NAD+
D-ribulose + NADH + H+
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high activity
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?
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NAD+
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NADH
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Co2+
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about 111% activity at 1 mM
Ni2+
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about 108% activity at 1 mM
Ba2+
209% activity at 5 mM
Ba2+
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about 126.8% activity at 1 mM
Ca2+
245% activity at 5 mM
Ca2+
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about 113.5% activity at 1 mM
Mg2+
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0.02 M, requirement
Mg2+
162% activity at 5 mM
Mg2+
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about 114.8% activity at 1 mM
additional information
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bacterial enzyme has no requirement for Zn2+
additional information
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no requirement for metal ions
additional information
not affected by Mn2+ and Co2+
additional information
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not influenced by Mn2+
additional information
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2-mercaptoethanol
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competitive to ribitol
Ag+
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complete inhibition
diethyldithiocarbamate
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50% inhibition at a concentration of 50 mM
EDTA
the enzyme activity is mostly lost (about 97%) after EDTA treatment
Fe3+
27.2% residual activity at 5 mM
K+
73.6% residual activity at 5 mM
o-phenanthroline
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50% inhibition at a concentration of 50 mM
p-chloromercuribenzoate
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p-mercuribenzoate
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reversible by L-cysteine
Cu2+
50.5% residual activity at 5 mM
Cu2+
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about 20% residual activity at 1 mM
Hg2+
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protection by NAD+
Hg2+
complete inhibition at 1 mM
Zn2+
61.9% residual activity at 5 mM
Zn2+
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about 43% residual activity at 1 mM
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sulfhydryl compounds
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requirement
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12.5
D-xylulose
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pH 9, 30°C
233
L-mannitol
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pH 9, 30°C
1.5
L-ribulose
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pH 9.5, 25°C
178
L-sorbitol
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pH 9, 30°C
0.8
L-xylulose
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pH 9.5, 25°C
0.8
D-ribulose
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pH 9.5, 25°C
1.1
D-ribulose
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pH 9, 30°C
84.2
L-arabitol
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pH 9, 30°C
0.042
NAD+
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at pH 10.0 and 35°C
0.16
NAD+
at pH 11.0 and 25°C
1.2
ribitol
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pH 9.5, 25°C
10.3
ribitol
at pH 11.0 and 25°C
13.9
ribitol
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at pH 10.0 and 35°C
32.2
ribitol
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pH 9, 30°C
77
xylitol
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pH 9, 30°C
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10
ribitol
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at pH 10.0 and 35°C
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0.71
ribitol
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at pH 10.0 and 35°C
30.9
ribitol
at pH 11.0 and 25°C
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23000
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after crystallization
270 - 280
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for xylitol in crude extract
43.6
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ribitol dehydrogenase B
50 - 150
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for ribitol in crude extract
50 - 200
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for L-arabitol in crude extract
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6 - 6.5
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sugar reduction
8.5 - 9
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alcohol oxidation
9 - 10
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alcohol oxidation
9 - 10.3
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alcohol oxidation
11
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alcohol oxidation
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10.7
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50% of maximal activity
8
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50% of maximal activity
9 - 11
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the enzyme shows about 25% activity at pH 9.0, while at pH 10.5 and 11.0 the activity is 85.6 and 68.11% respectively of that at pH 10.0
9.5 - 10.5
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alcohol oxidation
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45
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25 - 45
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about 90% activity at 25°C, 100% activity at 35°C, about 80% activity at 40°C, about 55% activity at 45°C
50 - 60
the enzyme retains more than 90% of the maximum activity at 50°C, with more than 85% activity at 55°C, and more than 80% at 60°C
8
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50% of maximal activity
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brenda
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UniProt
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brenda
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brenda
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brenda
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brenda
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brenda
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UniProt
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inducible enzyme; mutants with constitutive enzyme
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brenda
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brenda
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100000 - 110000
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wild type, gel filtration
27000
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4 * 27000, wild type enzyme, SDS-PAGE
25000
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4 * 25000, wild type enzyme, SDS-PAGE
25000
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2 * 25000, SDS-PAGE
25000
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4 * 25000, SDS-PAGE
25000
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4 * 25000, SDS-PAGE
25000
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4 * 25000, SDS-PAGE
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?
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monomers of 27000, mutant B, SDS-PAGE
dimer
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2 * 25000, SDS-PAGE
homotetramer
4 * 25800, calculated from amino acid sequence
homotetramer
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4 * 25800, calculated from amino acid sequence
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homotetramer
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4 * 25000, SDS-PAGE; 4 * 25928, calculated from amino acid sequence; 4 * 26650, liquid chromatography/mass spectrometry
homotetramer
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4 * 25000, SDS-PAGE; 4 * 25928, calculated from amino acid sequence; 4 * 26650, liquid chromatography/mass spectrometry
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tetramer
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4 * 25000, SDS-PAGE
tetramer
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4 * 25000, wild type enzyme, SDS-PAGE
tetramer
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4 * 27000, wild type enzyme, SDS-PAGE
tetramer
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4 * 25000, SDS-PAGE
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G196P
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mutant D, increased activity towards xylitol
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10 - 11
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unstable at high pH values
287121
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25 - 50
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the enzyme retains 72, 72, 48 and 0% of its initial activity after 4 h at 25, 30, 40 and 50°C, respectively
37
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extensive activity loss at pH 8 for 15 min
4 - 60
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50% enzyme activity loss after 1 min to 15 days
40 - 60
the enzyme shows half-lives of 25.7, 15.3, 7.5, 3.1, and 0.45 h at 40°C, 45°C, 50°C, 55°C, and 60°C, respectively
55
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half-life of mutant B is 6 min, half-life of mutant D is 30 min, half-life of wild-type enzyme is 20 min
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freezing and thawing causes 30-40% decrease of mutant B enzyme activity
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freezing and thawing causes 5-8% decrease of wild type enzyme activity
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half life in crude extract at 55°C mutant B: 6 min
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half life in crude extract at 55°C mutant D: 30 min
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half life in crude extract at 55°C wild type: 20 min
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NAD+ improves stability and reverses inhibition
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repeated freezing and thawing results in extensive activity loss
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unstable in dilute solutions
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-20°C wild type enzyme shows only slight loss of activity in phosphate buffer pH 7.0
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2°C presence of NAD+ several days
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mutant B enzyme inactive after freezing for 2 months, half life of 10 days at 2°C
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stable at 3°C in phosphate buffer, pH 7.4 for 1 month, unstable below pH 5.5 and at repeated freezing and thawing
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wild type enzyme can be stored frozen for months without greater loss of activity , half life of 70 days at 2°C
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Ni-NTA column chromatography
nickel-charged Sepharose resin column chromatography
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ribitol dehydrogenase A and B
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ribitol dehydrogenase B
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
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Dothie, J.M.; Giglio, J.R.; Moore, C.B.; Tayler, S.S.; Hartley, B.S.
Ribitol dehydrogenase of Klebsiella aerogenes. Sequence and properties of wild-type and mutant strains
Biochem. J.
230
569-578
1985
Klebsiella aerogenes
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Loviny, T.; Norton, P.M.; Hartley, B.S.
Ribitol dehydrogenase of Klebsiella aerogenes. Sequence of the structural gene
Biochem. J.
230
579-585
1985
Klebsiella aerogenes
brenda
Szumiko, T.; Byra, A.
The possible occurrence of zinc in ribitol and sorbitol dehydrogenases from Mycobacterium sp. 279
Acta Biochim. Pol.
31
401-408
1984
Mycobacterium sp.
brenda
Fromm, H.J.
D-Ribulose
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
6
432-437
1984
Klebsiella aerogenes
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brenda
Jörnvall, H.; v.Bahr-Lindström, H.; Jany, K.D.; Ulmer, W.; Fröschle, M.
Extended superfamily of short alcohol-polyol-sugar dehydrogenases: structural similarities between glucose and ribitol dehydrogenases
FEBS Lett.
165
190-196
1984
Klebsiella aerogenes
brenda
Burleigh, B.D.; Rigby, P.W.J.; Hartley, B.S.
A comparison of wild-type and mutant ribitol dehydrogenases from Klebsiella aerogenes
Biochem. J.
143
341-352
1974
Klebsiella aerogenes
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Taylor, S.S.; Rigby, P.W.J.; Hartley, B.S.
Ribitol dehydrogenase from Klebsiella aerogenes. Purification and subunit structure
Biochem. J.
141
693-700
1974
Klebsiella aerogenes
brenda
Charnetzky, W.T.; Mortlock, R.P.
Ribitol catabolic pathway in Klebsiella aerogenes
J. Bacteriol.
119
162-169
1974
Klebsiella aerogenes
brenda
Fossitt, D.D.; Wood, W.A.
Pentitol dehydrogenases of Aerobacter aerogenes
Methods Enzymol.
9
180-184
1966
Klebsiella aerogenes
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brenda
Nordlie, R.C.; Fromm, H.J.
Ribitol dehydrogenase. II. Studies on the reaction mechanism
J. Biol. Chem.
234
2523-2531
1959
Klebsiella aerogenes
brenda
Kahle, C.; Schneider, K.H.; Giffhorn, F.
Pentitol metabolism of Rodobacter sphaeroides Si4: purification and characterization of a ribitol dehydrogenase
J. Gen. Microbiol.
138
1277-1281
1992
Rhodobacter sphaeroides
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Muniruzzaman, S.; Kunisha, Y.; Ichiraku K.; Izumori, K.
Purification and characterization of a ribitol dehydrogenase from Enterobacter agglomerans strain 221e
J. Ferment. Bioeng.
79
496-498
1995
Pantoea agglomerans
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brenda
Adachi, O.; Fuji, Y.; Ano, Y.; Moonmangmee, D.; Toyama, H.; Shinagawa, E.; Theeragool, G.; Lotong, N.; Matsushita, K.
Membrane-bound sugar alcohol dehydrogenase in acetic acid bacteria catalyzes L-ribulose formation and NAD-dependent ribitol dehydrogenase is independent of the oxidative fermentation
Biosci. Biotechnol. Biochem.
65
115-125
2001
Gluconobacter oxydans
brenda
Singh, R.; Singh, R.; Kim, S.; Sigdel, S.; Park, J.; Choi, J.; Kim, I.; Lee, J.
D-Ribulose production by a ribitol dehydrogenase from Enterobacter aerogenes coupled with an NADH regeneration system
Biochem. Eng. J.
109
189-196
2016
Klebsiella aerogenes
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brenda
Singh, R.; Singh, R.; Kim, I.W.; Sigdel, S.; Kalia, V.C.; Kang, Y.C.; Lee, J.K.
An efficient ribitol-specific dehydrogenase from Enterobacter aerogenes
Enzyme Microb. Technol.
72
56-64
2015
Klebsiella aerogenes (A0A0H3FYM1), Klebsiella aerogenes, Klebsiella aerogenes KCTC 2190 (A0A0H3FYM1), Klebsiella aerogenes KCTC 2190
brenda
Hassanin, H.A.; Wang, X.; Mu, W.; Zhang, T.; Jiang, B.
Cloning and characterization of a new ribitol dehydrogenase from Providencia alcalifaciens RIMD 1656011
J. Sci. Food Agric.
96
2917-2924
2016
Providencia alcalifaciens, Providencia alcalifaciens RIMD 1656011
brenda
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