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Information on EC 1.1.1.289 - sorbose reductase and Organism(s) Candida albicans and UniProt Accession P87219

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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.
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This record set is specific for:
Candida albicans
UNIPROT: P87219
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Word Map
The taxonomic range for the selected organisms is: Candida albicans
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
nadph-dependent l-sorbose reductase, nadph-dependent sorbose reductase, l-sorbose reductase, fad-dependent d-sorbitol dehydrogenase, nadph-sr, sorbose reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NADPH-dependent sorbose reductase
-
-
PATHWAY SOURCE
PATHWAYS
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-chloro-3-oxobutanoate + NADPH + H+
(S)-4-chloro-3-hydroxybutanoate + NADP+
show the reaction diagram
-
-
-
?
D-fructose + NADPH
D-mannitol + NADP+
show the reaction diagram
-
less effective than reaction with L-sorbose
-
-
?
D-mannitol + NADP+
D-mannose + NADPH + H+
show the reaction diagram
-
-
-
-
r
D-sorbitol + NADP+
L-sorbose + NADPH + H+
show the reaction diagram
D-xylitol + NADP+
D-xylose + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-sorbose + NADPH + H+
L-sorbitol + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-sorbitol + NADP+
L-sorbose + NADPH + H+
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1873
D-fructose
-
K0.5-value, positive cooperativity
3953
L-sorbose
-
pH 7.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
154
D-fructose
-
pH 7.5, 25°C, positive cooperativity
782
L-sorbose
-
pH 7.5, 25°C, Michaelis-Menten kinetics
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
145
-
substrate L-sorbose, pH 6.2, 25°C
2.93
-
substrate D-sorbitol, pH 6.2, 25°C
33.1
-
substrate D-fructose, pH 6.2, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
-
isoelectric focusing and calculated
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
124000
-
MALDI-TOF
31000
-
4 * 31000, SDS-PAGE and calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
4 * 31000, SDS-PAGE and calculated
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
2 min, more than 90% inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme with FLAG-tag
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3) cells
expression in Escherichia coli strain Rosseta (DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team