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Information on EC 1.1.1.289 - sorbose reductase
for references in articles please use BRENDA:EC1.1.1.289
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.289 sorbose reductase
IUBMB Comments
The reaction occurs predominantly in the reverse direction. This enzyme can also convert D-fructose into D-mannitol, but more slowly. Belongs in the short-chain dehydrogenase family.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.289
-
gluconobacter
- albicans
- frateurii
-
s-4-chloro-3-hydroxybutanoate
- mannitol
- 4-chloro-3-oxobutanoate
- xylitol
-
biocatalytic
- suboxydans
-
substrate-coupled
- d-fructose
-
s-chbe
-
co-substrates
-
nadp-dependent
-
enantiomeric
- synthesis
showSynonyms
nadph-dependent l-sorbose reductase, nadph-dependent sorbose reductase, fad-dependent d-sorbitol dehydrogenase, nadph-sr, l-sorbose reductase, sorbose reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FAD-dependent D-sorbitol dehydrogenase
flavin adenine dinucleotide-dependent D-sorbitol dehydrogenase
L-sorbose reductase
NADPH-dependent L-sorbose reductase
SboA
SLDH
SOU1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucitol + NADP+ = L-sorbose + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
D-glucitol:NADP+ oxidoreductase
The reaction occurs predominantly in the reverse direction. This enzyme can also convert D-fructose into D-mannitol, but more slowly. Belongs in the short-chain dehydrogenase family.
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CAS REGISTRY NUMBER
COMMENTARY
138440-90-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-chloro-3-oxobutanoate + NADPH + H+
(S)-4-chloro-3-hydroxybutanoate + NADP+
Substrates: -
Products: -
Products: -
?
5-keto-D-fructose + NADPH
? + NADP+
-
Substrates: 86.8% of the rate with L-sorbose
Products: -
Products: -
r
ribulose + NADPH
? + NADP+
-
Substrates: 2.4% of the rate with L-sorbose
Products: -
Products: -
r
tagatose + NADPH
? + NADP+
-
Substrates: 0.8% of the rate with L-sorbose
Products: -
Products: -
r
xylulose + NADPH
? + NADP+
-
Substrates: 25.7% of the rate with L-sorbose
Products: -
Products: -
r
D-fructose + NADPH
D-mannitol + NADP+
-
Substrates: less effective than reaction with L-sorbose
Products: -
Products: -
?
D-glucitol + NADP+
D-sorbose + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucitol + NADP+
D-sorbose + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucitol + NADP+
L-sorbose + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucitol + NADP+
L-sorbose + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-mannitol + NADP+
L-fructose + NADPH + H+
-
Substrates: 134% of the rate with L-sorbose
Products: -
Products: -
r
D-mannitol + NADP+
L-fructose + NADPH + H+
-
Substrates: 134% of the rate with L-sorbose
Products: -
Products: -
r
D-sorbitol + NADP+
L-sorbose + NADPH + H+
-
Substrates: low efficiency
Products: -
Products: -
?
D-sorbitol + NADP+
L-sorbose + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-sorbitol + NADP+
L-sorbose + NADPH + H+
-
Substrates: 134% of the rate with L-sorbose
Products: -
Products: -
r
D-sorbitol + NADP+
L-sorbose + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-sorbitol + NADP+
L-sorbose + NADPH + H+
-
Substrates: 134% of the rate with L-sorbose
Products: -
Products: -
r
erythritol + NADP+
? + NADPH
-
Substrates: 65.3% of the rate with L-sorbose
Products: -
Products: -
r
erythritol + NADP+
? + NADPH
-
Substrates: 65.3% of the rate with L-sorbose
Products: -
Products: -
r
L-fructose + NADPH
D-mannitol + NADP+
-
Substrates: 142% of the rate with L-sorbose
Products: -
Products: -
r
L-fructose + NADPH
D-mannitol + NADP+
-
Substrates: 142% of the rate with L-sorbose
Products: -
Products: -
r
L-sorbose + NADPH + H+
D-sorbitol + NADP+
-
Substrates: -
Products: -
Products: -
r
L-sorbose + NADPH + H+
D-sorbitol + NADP+
-
Substrates: -
Products: -
Products: -
r
L-sorbose + NADPH + H+
D-sorbitol + NADP+
-
Substrates: -
Products: -
Products: -
r
L-sorbose + NADPH + H+
L-sorbitol + NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: development of a substrate-coupled biocatalytic process driven by NADPH-dependent sorbose reductase for the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate, overview. Ethyl 4-chloro-3-oxobutanoate is reduced to (S)-4-chloro-3-hydroxybutanoate, while NADPH is regenerated by the enzyme via oxidation of sorbitol, mannitol, or xylitol in crude extract of recombinant Escherichia coli cells, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate, reaction of (S)-specific secondary alcohol dehydrogenase, with an optical purity of 99% (e.e.) and an activity of 6.2 U/mg towards ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate, reaction of (S)-specific secondary alcohol dehydrogenase, with an optical purity of 99% (e.e.) and an activity of 6.2 U/mg towards ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate, reaction of (S)-specific secondary alcohol dehydrogenase, with an optical purity of 99% (e.e.) and an activity of 6.2 U/mg towards ethyl 4-chloro-3-oxobutanoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: highly specific for D-sorbitol and L-sorbose. Reaction rate in L-sorbose reduction highly predominates over L-sorbitol oxidation over a wide pH range
Products: -
Products: -
?
additional information
?
-
-
Substrates: highly specific for D-sorbitol and L-sorbose. Reaction rate in L-sorbose reduction highly predominates over L-sorbitol oxidation over a wide pH range
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glucitol + NADP+
D-sorbose + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucitol + NADP+
D-sorbose + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucitol + NADP+
L-sorbose + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucitol + NADP+
L-sorbose + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibitory: sodium fluoroacetate, sodium fluoride, KCN, monoiodoacetate
-
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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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
SboA is required for effective growth on D- or L-sorbose, the organism also grows on glycerol
brenda
additional information
-
SboA is required for effective growth on D- or L-sorbose, the organism also grows on glycerol
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SOU1_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
281
0
30038
Swiss-Prot
-
SOU1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
255
0
27437
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28320
-
3 * 29000, recombinant SboA, SDS-PAGE, 3 * 28320, SboA, sequence calculation
29000
-
3 * 29000, recombinant SboA, SDS-PAGE, 3 * 28320, SboA, sequence calculation
60000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
trimer
trimer
-
3 * 29000, recombinant SboA, SDS-PAGE, 3 * 28320, SboA, sequence calculation
trimer
-
3 * 29000, recombinant SboA, SDS-PAGE, 3 * 28320, SboA, sequence calculation
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with L-sorbose or NADPH using the sitting-drop vapour-diffusion method, at 20°C, to 2.38 and 1.90 A resolution, respectively. Crystal of the L-sorbose reductase-L-sorbose complex belongs to space group C2221, with unit-cell parameters a=124.2, b=124.1, c=60.8 A. The crystal of the L-sorbose reductase-NADPH complex belongs to space group P21, with unit-cell parameters a=124.3, b=61.0, c=124.5A, beta= 89.99°. The crystals contain two and eight molecules, respectively, in the asymmetric unit
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of disruption mutants, a mutant defective in sboA shows significantly reduced growth on L-sorbose, while a sboR mutant grows on L-sorbose even better than the wild-type strain with higher NADPH-SR activity in cytoplasm fractions
additional information
-
construction of disruption mutants, a mutant defective in sboA shows significantly reduced growth on L-sorbose, while a sboR mutant grows on L-sorbose even better than the wild-type strain with higher NADPH-SR activity in cytoplasm fractions
-
additional information
-
gene disruption mutant, no enzymic activity, no assimilation of once-produced L-sorbose
additional information
-
gene disruption mutant, no enzymic activity, no assimilation of once-produced L-sorbose
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.01 M potassium buffer, pH 7.0, stable for at least one month
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes sldSLC and sboA, DNA and amino acid sequence determination and analysis, genetic organization, a putational transcription regulator encoded by gene sboR is located upstream, sboRA comprises an operon, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
into the HindIII/NotI site of pET-28a(+) plasmid, expression construct is designed to overexpress only L-sorbose reductase protein (residues 1-263), overexpressed in Escherichia coli BL21 (DE3) cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
usage of a substrate-coupled biocatalytic process driven by an NADPH-dependent sorbose reductase from Candida albicans for the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sugisawa, T.; Hoshino, T.; Fujiwara, A.
Purification and properties of NADPH-linked L-sorbose reductase from Gluconobacter melanogenus N44-1
Agric. Biol. Chem.
55
2043-2049
1991
Gluconobacter oxydans, Gluconobacter oxydans N44-1
-
brenda
Adachi, O.; Ano, Y.; Moonmangmee, D.; Shinagawa, E.; Toyama, H.; Theeragool, G.; Lotong, N.; Matsushita, K.
Crystallization and properties of NADPH-dependent L-sorbose reductase from Gluconobacter melanogenus IFO 3294
Biosci. Biotechnol. Biochem.
63
2137-2143
1999
Gluconobacter oxydans, Gluconobacter oxydans IFO 3294
-
brenda
Shinjoh, M.; Tazoe, M.; Hoshino, T.
NADPH-dependent L-sorbose reductase is responsible for L-sorbose assimilation in Gluconobacter suboxydans IFO 3291
J. Bacteriol.
184
861-863
2002
Gluconobacter oxydans, Gluconobacter oxydans IFO 3291
brenda
Greenberg, J.R.; Price, N.P.; Oliver, R.P.; Sherman, F.; Rustchenko, E.
Candida albicans SOU1 encodes a sorbose reductase required for L-sorbose utilization
Yeast
22
957-969
2005
Candida albicans
brenda
Soemphol, W.; Toyama, H.; Moonmangmee, D.; Adachi, O.; Matsushita, K.
L-sorbose reductase and its transcriptional regulator involved in L-sorbose utilization of Gluconobacter frateurii
J. Bacteriol.
189
4800-4808
2007
Gluconobacter frateurii, Gluconobacter frateurii THD32
brenda
Kubota, K.; Nagata, K.; Miyazono, K.; Toyama, H.; Matsushita, K.; Tanokura, M.
Purification, crystallization and preliminary X-ray analysis of L-sorbose reductase from Gluconobacter frateurii complexed with L-sorbose or NADPH
Acta Crystallogr. Sect. F
65
562-564
2009
Gluconobacter frateurii (A4PB64), Gluconobacter frateurii
brenda
Cai, P.; An, M.; Xu, L.; Xu, S.; Hao, N.; Li, Y.; Guo, K.; Yan, M.
Development of a substrate-coupled biocatalytic process driven by an NADPH-dependent sorbose reductase from Candida albicans for the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate
Biotechnol. Lett.
34
2223-2227
2012
Candida albicans
brenda
Cai, P.; An, M.; Xu, S.; Yan, M.; Hao, N.; Li, Y.; Xu, L.
Asymmetric synthesis of (S)-4-chloro-3-hydroxybutanoate by sorbose reductase from Candida albicans with two co-existing recombinant Escherichia coli strains
Biosci. Biotechnol. Biochem.
79
1090-1093
2015
Candida albicans, Candida albicans (P87219), Candida albicans ATCC MYA-2876 (P87219)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.289)
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