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EC Tree
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: Bacteria, Eukaryota
Synonyms
nadph-dependent l-sorbose reductase, nadph-dependent sorbose reductase, nadph-sr, l-sorbose reductase, fad-dependent d-sorbitol dehydrogenase, sorbose reductase,
more
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FAD-dependent D-sorbitol dehydrogenase
flavin adenine dinucleotide-dependent D-sorbitol dehydrogenase
NADPH-dependent L-sorbose reductase
NADPH-dependent sorbose reductase
-
-
FAD-dependent D-sorbitol dehydrogenase
-
-
FAD-dependent D-sorbitol dehydrogenase
-
-
-
flavin adenine dinucleotide-dependent D-sorbitol dehydrogenase
-
-
flavin adenine dinucleotide-dependent D-sorbitol dehydrogenase
-
-
-
L-sorbose reductase
-
L-sorbose reductase
-
-
-
NADPH-dependent L-sorbose reductase
-
-
NADPH-dependent L-sorbose reductase
-
-
-
SboA
-
-
SLDH
-
-
SOU1
-
-
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D-glucitol + NADP+ = L-sorbose + NADPH + H+
-
-
-
-
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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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4-chloro-3-oxobutanoate + NADPH + H+
(S)-4-chloro-3-hydroxybutanoate + NADP+
-
-
-
?
5-keto-D-fructose + NADPH
? + NADP+
D-fructose + NADPH
D-mannitol + NADP+
D-glucitol + NADP+
D-sorbose + NADPH + H+
D-glucitol + NADP+
L-sorbose + NADPH + H+
D-mannitol + NADP+
D-mannose + NADPH + H+
-
-
-
-
r
D-mannitol + NADP+
L-fructose + NADPH + H+
D-sorbitol + NADP+
L-sorbose + NADPH + H+
D-xylitol + NADP+
D-xylose + NADPH + H+
-
-
-
-
r
erythritol + NADP+
? + NADPH
L-fructose + NADPH
D-mannitol + NADP+
-
142% of the rate with L-sorbose
-
-
r
L-sorbose + NADPH + H+
D-sorbitol + NADP+
L-sorbose + NADPH + H+
L-sorbitol + NADP+
ribulose + NADPH
? + NADP+
-
2.4% of the rate with L-sorbose
-
-
r
tagatose + NADPH
? + NADP+
-
0.8% of the rate with L-sorbose
-
-
r
xylulose + NADPH
? + NADP+
-
25.7% of the rate with L-sorbose
-
-
r
additional information
?
-
5-keto-D-fructose + NADPH
? + NADP+
-
86.8% of the rate with L-sorbose
-
-
r
5-keto-D-fructose + NADPH
? + NADP+
-
86.8% of the rate with L-sorbose
-
-
r
D-fructose + NADPH
D-mannitol + NADP+
-
less effective than reaction with L-sorbose
-
-
?
D-fructose + NADPH
D-mannitol + NADP+
-
-
-
-
?
D-fructose + NADPH
D-mannitol + NADP+
-
-
-
-
?
D-glucitol + NADP+
D-sorbose + NADPH + H+
-
-
-
-
r
D-glucitol + NADP+
D-sorbose + NADPH + H+
-
-
-
-
r
D-glucitol + NADP+
L-sorbose + NADPH + H+
-
-
-
-
r
D-glucitol + NADP+
L-sorbose + NADPH + H+
-
-
-
-
r
D-mannitol + NADP+
L-fructose + NADPH + H+
-
134% of the rate with L-sorbose
-
-
r
D-mannitol + NADP+
L-fructose + NADPH + H+
-
134% of the rate with L-sorbose
-
-
r
D-sorbitol + NADP+
L-sorbose + NADPH + H+
-
-
-
-
r
D-sorbitol + NADP+
L-sorbose + NADPH + H+
-
low efficiency
-
-
?
D-sorbitol + NADP+
L-sorbose + NADPH + H+
-
-
-
-
r
D-sorbitol + NADP+
L-sorbose + NADPH + H+
-
134% of the rate with L-sorbose
-
-
r
D-sorbitol + NADP+
L-sorbose + NADPH + H+
-
-
-
-
r
D-sorbitol + NADP+
L-sorbose + NADPH + H+
-
134% of the rate with L-sorbose
-
-
r
erythritol + NADP+
? + NADPH
-
65.3% of the rate with L-sorbose
-
-
r
erythritol + NADP+
? + NADPH
-
65.3% of the rate with L-sorbose
-
-
r
L-sorbose + NADPH + H+
D-sorbitol + NADP+
-
-
-
-
r
L-sorbose + NADPH + H+
D-sorbitol + NADP+
-
-
-
-
r
L-sorbose + NADPH + H+
L-sorbitol + NADP+
-
-
-
-
?
L-sorbose + NADPH + H+
L-sorbitol + NADP+
-
-
-
?
additional information
?
-
-
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
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-
?
additional information
?
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-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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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
-
-
?
additional information
?
-
-
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
-
-
?
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D-glucitol + NADP+
D-sorbose + NADPH + H+
D-glucitol + NADP+
L-sorbose + NADPH + H+
D-sorbitol + NADP+
L-sorbose + NADPH + H+
-
-
-
-
r
D-glucitol + NADP+
D-sorbose + NADPH + H+
-
-
-
-
r
D-glucitol + NADP+
D-sorbose + NADPH + H+
-
-
-
-
r
D-glucitol + NADP+
L-sorbose + NADPH + H+
-
-
-
-
r
D-glucitol + NADP+
L-sorbose + NADPH + H+
-
-
-
-
r
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additional information
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no cofactor: NAD+, NADH
-
NADP+
-
-
NADPH
-
-
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N-ethylmaleimide
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0.97 mM, 81% residual activity
Na2HAsO4
-
0.97 mM, 90% residual activity
p-chloromercuribenzoate
-
0.19 mM, 43% residual activity
Quinine
-
0.49 mM, complete loss of activity
Sodium azide
-
0.97 mM, 90% residual activity
additional information
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not inhibitory: sodium fluoroacetate, sodium fluoride, KCN, monoiodoacetate
-
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7.3
D-mannitol
-
pH 10.0, 25°C
167
D-sorbitol
-
pH 10.0, 25°C
160
D-fructose
-
pH 7.0, 25°C
1873
D-fructose
-
K0.5-value, positive cooperativity
35
L-sorbose
-
pH 6.0, 25°C
328
L-sorbose
-
pH 7.0, 25°C
3953
L-sorbose
-
pH 7.5, 25°C
0.032
NADPH
-
pH 6.0, 25°C
0.111
NADPH
-
pH 7.0, 25°C
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154
D-fructose
-
pH 7.5, 25°C, positive cooperativity
782
L-sorbose
-
pH 7.5, 25°C, Michaelis-Menten kinetics
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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
77
-
pH 6.0, 25°C, substrate L-sorbose
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10
-
oxidation of D-sorbitol
10 - 10.5
-
oxidation of D-sorbitol
6
-
reduction of L-sorbose
6 - 7
-
oxidation of L-sorbitol
7
-
reduction of L-sorbose
8
-
oxidation of D-sorbitol
9
-
reduction reaction, assay at
6.2
-
-
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5 - 7
-
reduction of L-sorbose
7 - 9
-
oxidation of D-sorbitol
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30
-
assay at
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4.8
-
isoelectric focusing and calculated
5.72
-
SboA, sequence calculation
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-
UniProt
brenda
genes sldSLC and sboA
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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UniProt
brenda
recombinant enzyme with FLAG-tag
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-
brenda
-
UniProt
brenda
genes sldSLC and sboA
-
-
brenda
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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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-
-
brenda
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-
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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SOU1_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
281
0
30038
Swiss-Prot
other Location (Reliability: 2 )
SOU1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
255
0
27437
Swiss-Prot
other Location (Reliability: 5 )
W1QF86_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
282
0
30438
TrEMBL
other Location (Reliability: 2 )
A0A0F8B3S3_CERFI
280
0
29972
TrEMBL
other Location (Reliability: 2 )
A0A8J5BWJ0_9ASCO
313
0
33185
TrEMBL
other Location (Reliability: 4 )
X7VQH2_9MYCO
254
0
26861
TrEMBL
-
A0A090DZI4_9HYPH
257
0
27537
TrEMBL
-
A0A8J5B6X8_9ASCO
291
0
31035
TrEMBL
other Location (Reliability: 3 )
A0A084G0H8_PSEDA
265
0
28716
TrEMBL
other Location (Reliability: 2 )
X7XY10_MYCKA
253
0
26788
TrEMBL
-
M5EKC6_9HYPH
262
0
28323
TrEMBL
-
A0A0H5CFK8_CYBJN
Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 / NRRL Y-1542)
256
0
27871
TrEMBL
other Location (Reliability: 2 )
X7ZDR7_MYCKA
255
0
26974
TrEMBL
-
F5YMI6_TREPZ
Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2)
255
0
27137
TrEMBL
-
A0A8J8VWY0_9EURO
265
0
28449
TrEMBL
other Location (Reliability: 2 )
W1QLS7_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
273
0
29111
TrEMBL
other Location (Reliability: 1 )
W6K4X0_9MICO
252
0
25915
TrEMBL
-
F7S9Y5_9PROT
257
0
27389
TrEMBL
-
C5QMM3_9STAP
260
0
28140
TrEMBL
-
X8CW50_MYCIT
256
0
27276
TrEMBL
-
X8A798_MYCIT
256
0
27276
TrEMBL
-
K0KRU6_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
288
0
31545
TrEMBL
other Location (Reliability: 1 )
A0A840QKW0_9PSEU
499
0
54451
TrEMBL
-
A0A087B5R7_9BIFI
294
0
31751
TrEMBL
-
X8B1I5_MYCAV
256
0
27119
TrEMBL
-
A0A8J5BYQ7_9ASCO
291
0
30942
TrEMBL
other Location (Reliability: 3 )
W1QFA8_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
290
0
31361
TrEMBL
other Location (Reliability: 1 )
A0A8J8W1R9_9EURO
276
0
29740
TrEMBL
other Location (Reliability: 2 )
F7S661_9PROT
260
0
26890
TrEMBL
-
F5Y7Q2_TREAZ
Treponema azotonutricium (strain ATCC BAA-888 / DSM 13862 / ZAS-9)
255
0
26711
TrEMBL
-
A0A1V3X4P4_MYCKA
255
0
26974
TrEMBL
-
A0A8J5BL52_9ASCO
311
0
32826
TrEMBL
other Location (Reliability: 3 )
W1QKW3_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
284
0
30136
TrEMBL
other Location (Reliability: 2 )
A0A841QHN6_9PROT
488
0
53800
TrEMBL
-
A0A087A0I8_9BIFI
283
0
30276
TrEMBL
-
A4PB64_9PROT
263
0
28321
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
28320
-
3 * 29000, recombinant SboA, SDS-PAGE, 3 * 28320, SboA, sequence calculation
29000
-
3 * 29000, recombinant SboA, SDS-PAGE, 3 * 28320, SboA, sequence calculation
30000
-
2 * 30000, SDS-PAGE
31000
-
4 * 31000, SDS-PAGE and calculated
87000
-
recombinant SboA, gel filtration
60000
-
gel filtration
60000
-
1 * 60000, SDS-PAGE
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tetramer
-
4 * 31000, SDS-PAGE and calculated
dimer
-
2 * 30000, SDS-PAGE
dimer
-
2 * 30000, SDS-PAGE
-
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
-
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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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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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6.5 - 7.5
-
30°C, stable for 30 min
663570
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30
-
pH 6.5-7.5, 30 min, stable
55
-
stable up to, for 10 min
65
-
2 min, more than 90% inactivation
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-20°C, 0.01 M potassium buffer, pH 7.0, stable for at least one month
-
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by sonication, centrifugation and gel filtration
recombinant enzyme with FLAG-tag
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli Rosetta (DE3) cells
expression in Escherichia coli strain Rosseta (DE3)
-
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
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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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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