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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ribitol degradation
-
-
degradation of sugar alcohols
-
-
Pentose and glucuronate interconversions
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
ribitol:NAD+ 2-oxidoreductase
-
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-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
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
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
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
0.02 M, requirement
Na+
-
slight increase
Sn2+
-
slight increase
Zn2+
-
activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
competitive to ribitol
Ag+
-
complete inhibition
Chelating agents
-
-
Cu2+
-
10-20% inhibition
diethyldithiocarbamate
-
50% inhibition at a concentration of 50 mM
dithiothreitol
-
-
Ni2+
-
10-20% inhibition
o-phenanthroline
-
50% inhibition at a concentration of 50 mM
p-chloromercuribenzoate
-
-
p-mercuribenzoate
-
reversible by L-cysteine
Zn2+
-
10-20% inhibition
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, 30C
0.8 - 1.1
D-ribulose
12.5
D-xylulose
-
pH 9, 30C
84.2 - 147
L-arabitol
233
L-mannitol
-
pH 9, 30C
1.5
L-ribulose
-
pH 9.5, 25C
178
L-sorbitol
-
pH 9, 30C
0.8
L-xylulose
-
pH 9.5, 25C
0.077 - 2.36
NAD+
0.02
NADH
-
pH 9.5, 25C
1.2 - 32.2
ribitol
77 - 1000
xylitol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
28
L-arabitol
Enterobacter aerogenes
-
-
299
ribitol
Enterobacter aerogenes
-
-
36
xylitol
Enterobacter aerogenes
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43.6
-
ribitol dehydrogenase B
50 - 150
-
for ribitol in crude extract
50 - 200
-
for L-arabitol in crude extract
83
-
wild type enzyme
270 - 280
-
for xylitol in crude extract
23000
-
after crystallization
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
-
sugar reduction
6.5
-
sugar reduction
7.4
-
sugar reduction
8
-
alcohol oxidation
8.5 - 9
-
alcohol oxidation
9 - 10
-
alcohol oxidation
9 - 10.3
-
alcohol oxidation
11
-
alcohol oxidation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
sugar reduction
8
-
50% of maximal activity
9.5 - 10.5
-
alcohol oxidation
10.7
-
50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
50% of maximal activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
gel filtration
92000
-
gel filtration
100000 - 110000
-
wild type, gel filtration
100000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
monomers of 27000, mutant B, SDS-PAGE
dimer
-
2 * 25000, SDS-PAGE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 11
-
-
287126
10 - 11
-
unstable at high pH values
287121
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 60
-
50% enzyme activity loss after 1 min to 15 days
37
-
extensive activity loss at pH 8 for 15 min
55
-
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
-
freezing and thawing causes 5-8% decrease of wild type enzyme activity
-
half life in crude extract at 55C mutant B: 6 min
-
half life in crude extract at 55C mutant D: 30 min
-
half life in crude extract at 55C wild type: 20 min
-
NAD+ improves stability and reverses inhibition
-
repeated freezing and thawing results in extensive activity loss
-
unstable in dilute solutions
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C wild type enzyme shows only slight loss of activity in phosphate buffer pH 7.0
-
2C presence of NAD+ several days
-
mutant B enzyme inactive after freezing for 2 months, half life of 10 days at 2C
-
stable at 3C in phosphate buffer, pH 7.4 for 1 month, unstable below pH 5.5 and at repeated freezing and thawing
-
wild type enzyme can be stored frozen for months without greater loss of activity , half life of 70 days at 2C
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ribitol dehydrogenase A and B
-
ribitol dehydrogenase B
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G196P
-
mutant D, increased activity towards xylitol
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