Information on EC 1.1.1.56 - ribitol 2-dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.56
-
RECOMMENDED NAME
GeneOntology No.
ribitol 2-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ribitol + NAD+ = D-ribulose + NADH + H+
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
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reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
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Pentose and glucuronate interconversions
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ribitol degradation
-
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degradation of sugar alcohols
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-
SYSTEMATIC NAME
IUBMB Comments
ribitol:NAD+ 2-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9014-23-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
allitol + NAD+
D-psicose + NADH
show the reaction diagram
-
-
-
r
D-arabitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
D-glucitol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
D-psicose + NADH + H+
allitol + NAD+
show the reaction diagram
D-sorbitol + NAD+
L-sorbose + NADH + H+
show the reaction diagram
erythritol + NAD+
? + NADH
show the reaction diagram
L-arabitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
L-talitol + NAD+
L-tagatose + NADH
show the reaction diagram
-
-
-
r
ribitol + NAD+
D-ribulose + NADH
show the reaction diagram
ribitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
xylitol + NAD+
D-xylulose + NADH + H+
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
ribitol + NAD+
D-ribulose + NADH
show the reaction diagram
-
-
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
about 111% activity at 1 mM
Na+
-
slight increase
Ni2+
-
about 108% activity at 1 mM
Sn2+
-
slight increase
Zn2+
-
activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
competitive to ribitol
Ag+
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complete inhibition
Chelating agents
-
-
diethyldithiocarbamate
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50% inhibition at a concentration of 50 mM
dithiothreitol
-
-
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
Ni2+
-
10-20% inhibition
o-phenanthroline
-
50% inhibition at a concentration of 50 mM
p-chloromercuribenzoate
-
-
p-mercuribenzoate
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reversible by L-cysteine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sulfhydryl compounds
-
requirement
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
107
allitol
-
pH 9, 30°C
0.8 - 1.1
D-ribulose
12.5
D-xylulose
-
pH 9, 30°C
84.2 - 147
L-arabitol
233
L-mannitol
-
pH 9, 30°C
1.5
L-ribulose
-
pH 9.5, 25°C
178
L-sorbitol
-
pH 9, 30°C
0.8
L-xylulose
-
pH 9.5, 25°C
0.042 - 2.36
NAD+
0.02
NADH
-
pH 9.5, 25°C
1.2 - 32.2
ribitol
77 - 1000
xylitol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
28
L-arabitol
Enterobacter aerogenes
-
-
10 - 299
ribitol
36
xylitol
Enterobacter aerogenes
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.71 - 30.9
ribitol
1476
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43.6
-
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
83
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wild type enzyme
270 - 280
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for xylitol in crude extract
23000
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after crystallization
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
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sugar reduction
6.5
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sugar reduction
7.4
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sugar reduction
8
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alcohol oxidation
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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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sugar reduction
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
10.7
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50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
50% of maximal activity
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
4 * 27000, wild type enzyme, SDS-PAGE
50000
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gel filtration
92000
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gel filtration
100000 - 110000
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wild type, gel filtration
100000
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gel filtration
104000
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gel filtration
110000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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monomers of 27000, mutant B, SDS-PAGE
dimer
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2 * 25000, SDS-PAGE
homotetramer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 11
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-
287126
10 - 11
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unstable at high pH values
287121
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 60
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50% enzyme activity loss after 1 min to 15 days
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
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G196P
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mutant D, increased activity towards xylitol
Show AA Sequence (189 entries)
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