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Information on EC 1.1.1.56 - ribitol 2-dehydrogenase
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1.1.1.56 ribitol 2-dehydrogenaseSpecify your search results
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ribitol 2-dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NAD+-dependent ribitol dehydrogenase
RDH
ribitol dehydrogenase B
-
mutant enzyme with different properties
ribitol-specific dehydrogenase
ribitol: NAD+ 2-oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ribitol + NAD+ = D-ribulose + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
ribitol:NAD+ 2-oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9014-23-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ribitol + NAD+
D-ribulose + NADH
-
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
-
high activity
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
mutants have increased xylitol activity
-
?
additional information
?
-
no activity with NADP+
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ribitol + NAD+
D-ribulose + NADH + H+
-
high activity
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Mg2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
the enzyme activity is mostly lost (about 97%) after EDTA treatment
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9 - 11
-
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
-
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
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (392 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
homotetramer
-
4 * 25928, calculated from amino acid sequence
homotetramer
-
4 * 26650, liquid chromatography/mass spectrometry
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 50
-
the enzyme retains 72, 72, 48 and 0% of its initial activity after 4 h at 25, 30, 40 and 50°C, respectively
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
-
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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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
-
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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
-
mutant B enzyme inactive after freezing for 2 months, half life of 10 days at 2°C
-
stable at 3°C 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 2°C
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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
-
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
brenda
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
-
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
brenda
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
-
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
-
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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