Information on EC 1.1.1.289 - sorbose reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.289
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RECOMMENDED NAME
GeneOntology No.
sorbose reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucitol + NADP+ = L-sorbose + NADPH + H+
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fructose and mannose metabolism
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
138440-90-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain THD32, NBRC 101656, genes sldSLC and sboA
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Manually annotated by BRENDA team
strain IFO 3291
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Manually annotated by BRENDA team
strain IFO 3294
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Manually annotated by BRENDA team
strain N44-1
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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
5-keto-D-fructose + NADPH
? + NADP+
show the reaction diagram
D-fructose + NADPH
D-mannitol + NADP+
show the reaction diagram
D-glucitol + NADP+
D-sorbose + NADPH
show the reaction diagram
D-glucitol + NADP+
L-sorbose + NADPH
show the reaction diagram
D-mannitol + NADP+
D-mannose + NADPH + H+
show the reaction diagram
-
-
-
-
r
D-mannitol + NADP+
L-fructose + NADPH + H+
show the reaction diagram
D-sorbitol + NADP+
L-sorbose + NADPH + H+
show the reaction diagram
D-xylitol + NADP+
D-xylose + NADPH + H+
show the reaction diagram
-
-
-
-
r
erythritol + NADP+
? + NADPH
show the reaction diagram
L-fructose + NADPH
D-mannitol + NADP+
show the reaction diagram
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142% of the rate with L-sorbose
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-
r
L-sorbose + NADPH
D-sorbitol + NADP+
show the reaction diagram
L-sorbose + NADPH
L-sorbitol + NADP+
show the reaction diagram
-
-
-
-
?
L-sorbose + NADPH + H+
L-sorbitol + NADP+
show the reaction diagram
-
-
-
?
ribulose + NADPH
? + NADP+
show the reaction diagram
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2.4% of the rate with L-sorbose
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r
tagatose + NADPH
? + NADP+
show the reaction diagram
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0.8% of the rate with L-sorbose
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r
xylulose + NADPH
? + NADP+
show the reaction diagram
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25.7% of the rate with L-sorbose
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-
r
additional information
?
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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
D-glucitol + NADP+
D-sorbose + NADPH
show the reaction diagram
D-glucitol + NADP+
L-sorbose + NADPH
show the reaction diagram
D-sorbitol + NADP+
L-sorbose + NADPH + H+
show the reaction diagram
-
-
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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dependent on
additional information
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no cofactor: NAD+, NADH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
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0.97 mM, 81% residual activity
Na2HAsO4
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0.97 mM, 90% residual activity
p-chloromercuribenzoate
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0.19 mM, 43% residual activity
Quinine
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0.49 mM, complete loss of activity
Sodium azide
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0.97 mM, 90% residual activity
additional information
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not inhibitory: sodium fluoroacetate, sodium fluoride, KCN, monoiodoacetate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
160 - 1873
D-fructose
7.3
D-mannitol
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pH 10.0, 25C
167
D-sorbitol
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pH 10.0, 25C
35 - 3953
L-sorbose
0.032 - 0.111
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
154
D-fructose
Candida albicans
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pH 7.5, 25C, positive cooperativity
782
L-sorbose
Candida albicans
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pH 7.5, 25C, Michaelis-Menten kinetics
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.93
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substrate D-sorbitol, pH 6.2, 25C
33.1
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substrate D-fructose, pH 6.2, 25C
77
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pH 6.0, 25C, substrate L-sorbose
145
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substrate L-sorbose, pH 6.2, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
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oxidation of L-sorbitol
6
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reduction of L-sorbose
7
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reduction of L-sorbose
8
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oxidation of D-sorbitol
9
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reduction reaction, assay at
10
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oxidation of D-sorbitol
10 - 10.5
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oxidation of D-sorbitol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
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reduction of L-sorbose
7 - 9
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oxidation of D-sorbitol
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
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isoelectric focusing and calculated
5.72
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SboA, sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
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gel filtration
60000
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gel filtration
87000
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recombinant SboA, gel filtration
124000
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MALDI-TOF
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
tetramer
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4 * 31000, SDS-PAGE and calculated
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with L-sorbose or NADPH using the sitting-drop vapour-diffusion method, at 20C, 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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
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30C, stable for 30 min
663570
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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pH 6.5-7.5, 30 min, stable
55
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stable up to, for 10 min
65
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2 min, more than 90% inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.01 M potassium buffer, pH 7.0, stable for at least one month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by sonication, centrifugation and gel filtration
recombinant enzyme with FLAG-tag
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain Rosseta (DE3)
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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)
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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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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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