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Information on EC 1.1.1.123 - sorbose 5-dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.123
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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
1.1.1.123 sorbose 5-dehydrogenase (NADP+)
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
5-ketofructose reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-keto-D-fructose reductase
-
-
-
-
5-ketofructose reductase
-
-
-
-
AJA48273.1
CP-AKR
reduced nicotinamide adenine dinucleotide phosphate-linked reductase
-
-
-
-
sorbose (nicotinamide adenine dinucleotide phosphate) dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-sorbose + NADP+ = 5-dehydro-D-fructose + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-sorbose:NADP+ 5-oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
37250-52-5
-
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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
5-keto-D-fructose 1-phosphate + NADPH
L-sorbose 1-phosphate + NADP+
-
Substrates: low activity, maximal rate of 1.8% that observed for 5-keto-D-fructose
Products: -
Products: -
?
1-phenyl-1,2-propandione + NADP+
?
AJA48273.1
Substrates: 14.8% of the specific activity as compared to 5-dehydro-D-fructose
Products: -
Products: -
?
1-phenyl-1,2-propandione + NADP+
?
AJA48273.1
Substrates: 14.8% of the specific activity as compared to 5-dehydro-D-fructose
Products: -
Products: -
?
5-dehydro-D-fructose + NADPH + H+
L-sorbose + NADP+
AJA48273.1
Substrates: -
Products: -
Products: -
?
5-dehydro-D-fructose + NADPH + H+
L-sorbose + NADP+
AJA48273.1
Substrates: -
Products: -
Products: -
?
5-keto-D-fructose + NADPH
L-sorbose + NADP+
-
Substrates: -
Products: -
Products: -
ir
5-keto-D-fructose + NADPH
L-sorbose + NADP+
-
Substrates: -
Products: -
Products: -
ir
diacetyl + NADP+
?
AJA48273.1
Substrates: 38% of the specific activity as compared to 5-dehydro-D-fructose
Products: -
Products: -
?
diacetyl + NADP+
?
AJA48273.1
Substrates: 38% of the specific activity as compared to 5-dehydro-D-fructose
Products: -
Products: -
?
fructose + NADPH
sorbitol + NADP+
-
Substrates: -
Products: -
Products: -
?
fructose + NADPH
sorbitol + NADP+
-
Substrates: sorbitol synthesis
Products: -
Products: -
?
L-sorbose + NADP+
5-dehydro-D-fructose + NADPH + H+
AJA48273.1
Substrates: -
Products: -
Products: -
?
L-sorbose + NADP+
5-dehydro-D-fructose + NADPH + H+
AJA48273.1
Substrates: -
Products: -
Products: -
?
pyruvaldehyde + NADP+
?
AJA48273.1
Substrates: 5% of the specific activity as compared to 5-dehydro-D-fructose
Products: -
Products: -
?
pyruvaldehyde + NADP+
?
AJA48273.1
Substrates: 5% of the specific activity as compared to 5-dehydro-D-fructose
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
fructose + NADPH
sorbitol + NADP+
-
Substrates: sorbitol synthesis
Products: -
Products: -
?
L-sorbose + NADP+
5-dehydro-D-fructose + NADPH + H+
AJA48273.1
Substrates: -
Products: -
Products: -
?
L-sorbose + NADP+
5-dehydro-D-fructose + NADPH + H+
AJA48273.1
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
stereospecific transfer of hydrogen from the A side of reduced pyridine to the ketohexose substrate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphate
-
in active site, likely position for the adenyl phasphate of NADP(H)
Zn2+
Zn2+
-
catalytical, conserved sites of the sorbitol dehydrogenase sub-family
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-hydroxymercuribenzoate
-
0.4 mM and 1 mM inhibit activity to 21% and 41% respectively
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
5-dehydro-D-fructose
AJA48273.1
pH and temperature not specified in the publication
12.4
NADPH
AJA48273.1
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
29.3
5-dehydro-D-fructose
AJA48273.1
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
pH 5: about 20% of activity maximum, pH 9: about 35% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 38
-
activity decreases gradually with increasing temperature from 0°C to 27°C, falls rapidly above 27°C and is completely lost at 38°C
25 - 41
-
sorbitol content increases in a temperature dependent manner
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
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.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
AJA48273.1
an important function in the degradation of this substrate and might be responsible for the formation of fructose, which is then channelled into the central metabolism of Clostridium pasteurianum
metabolism
-
an important function in the degradation of this substrate and might be responsible for the formation of fructose, which is then channelled into the central metabolism of Clostridium pasteurianum
-
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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). A5AB81_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
279
0
30095
TrEMBL
other Location (Reliability: 2)
A5AB79_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
270
0
29007
TrEMBL
other Location (Reliability: 5)
A0A0F4YR00_TALEM
263
0
28277
TrEMBL
other Location (Reliability: 2)
A0A0F4YPU4_TALEM
270
0
29074
TrEMBL
other Location (Reliability: 4)
A0A060T309_BLAAD
268
0
28803
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
structural similarity of enzyme to sorbitol dehydrogenase
additional information
-
monomer has a very similar fold to the alcohol dehydrogenases
additional information
-
amino acid sequence has 60% identity with sheep liver, 41% with Bombyx mori sorbitol dehydrogenase and 21% with horse liver alcohol dehydrogenase
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
addition of Arg and loss of Asp decrease the electric potential of the adenosine ribose-binding-pocket, creating an environment favorable for NADPH-binding, the replacement of an Asp with an Ala and the adjacent Leu with an Arg change the potential
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, affinity chromatography, ion exchange chromatography
-
ammonium sulfate precipitation, DEAE-Sepharose-, Gel Red A-, Phenyl Sepharose column chromatography
-
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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
Yagi, S.; Kobayahi, K.; Sonoyama, T.
Purification and properties of 5-keto-D-fructose reductase from a mutant strain derived from Corynebacterium sp.
J. Ferment. Bioeng.
67
212-214
1989
Corynebacterium sp.
-
brenda
Englard, S.; Avigad, G.
5-keto-D-Fructose reductase from yeast
Methods Enzymol.
41B
132-138
1975
Bacillus subtilis, Bacillus subtilis 168-2, Brevibacillus brevis, Cyberlindnera jadinii, Enterobacter cloacae, Gluconobacter oxydans, Klebsiella aerogenes, no activity in Candida tropicalis, Priestia megaterium, Proteus vulgaris, Saccharomyces cerevisiae
brenda
Englard, S.; Kaysen, G.; Avigad, G.
5-keto-D-Fructose. VI. A specific reduced nicotinamide adenine dinucleotide phosphate-linked reductase from yeast
J. Biol. Chem.
245
1311-1318
1970
Bacillus subtilis, Bacillus subtilis 168-2, Brevibacillus brevis, Cyberlindnera jadinii, Enterobacter cloacae, Gluconobacter cerinus, Gluconobacter oxydans, Klebsiella aerogenes, no activity in Bacillus cereus, no activity in Candida tropicalis, no activity in Escherichia coli K12, Priestia megaterium, Proteus vulgaris, Saccharomyces cerevisiae
brenda
Salvucci, M.E.; Hendrix, D.L.; Wolfe, G.R.
Effect of high temperature on the metabolic process affecting sorbitol synthesis in the silverleaf whitefly, Bemisia argentifolii
J. Insect Physiol.
45
21-27
1999
Bemisia argentifolii
brenda
Wolfe, G.R.; Smith, C.A.; Hendrix, D.L.; Salvucci, M.E.
Molecular basis for thermoprotection in Bemisia: structural differences between whitefly ketose reductase and other medium-chain dehydrogenases/reductases
Insect Biochem. Mol. Biol.
29
113-120
1999
Bemisia argentifolii
brenda
Banfield, M.J.; Salvucci, M.E.; Baker, E.N.; Smith, C.A.
Crystal structure of the NADP(H)-dependent ketose reductase from Bemisia argentifolii at 2.3 A resolution
J. Mol. Biol.
306
239-250
2001
Bemisia argentifolii
brenda
Salvucci, M.E.; Wolfe, G.R.; Hendrix, D.L.
Purification and properties of an unusual NADPH-dependent ketose reductase from the silverleaf whitefly
Insect Biochem. Mol. Biol.
28
357-363
1998
Bemisia argentifolii
-
brenda
Schiessl, J.; Kosciow, K.; Garschagen, L.S.; Hoffmann, J.J.; Heymuth, J.; Franke, T.; Deppenmeier, U.
Degradation of the low-calorie sugar substitute 5-ketofructose by different bacteria
Appl. Microbiol. Biotechnol.
105
2441-2453
2021
Clostridium pasteurianum (AJA48273.1), Clostridium pasteurianum DSM 525 (AJA48273.1)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.123)
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