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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms d-erythrulose reductase, more
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D-erythrulose reductase
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D-threitol:NADP+ oxidoreductase
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reductase, D-erythrulose
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D-threitol + NADP+ = D-erythrulose + NADPH + H+
D-threitol + NADP+ = D-erythrulose + NADPH + H+
in an early reference the enzymatic reaction product of D-erythrulose was incorrectly identified as erythritol, gas-liquid and thin-layer chromatographic data have since confirmed the product to be D-threitol, not erythritol, for this reason the systematic name D-threitol:NADP+ oxidoreductase is now used instead of erythritol:NADP+ oxidoreductase
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D-threitol + NADP+ = D-erythrulose + NADPH + H+
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D-threitol:NADP+ oxidoreductase
NAD+ is also utilized, but more slowly.
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(1S)-(+)-camphorquinone + NADPH
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Substrates: stereospecific Products: -
?
1,2-cyclohexanedione + NADPH
?
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Substrates: - Products: -
?
2,3-heptanedione + NADPH
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Substrates: - Products: -
?
2,3-pentanedione + NADPH
?
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Substrates: - Products: -
?
3,4-hexanedione + NADPH
?
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Substrates: - Products: -
?
acetoin + NADPH + H+
2,3-butanediol + NADP+
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Substrates: only slight reversibility, low activity Products: -
r
D-erythrulose + NAD(P)+
?
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Substrates: one route of formation of tetritols in mammalia Products: -
r
D-erythrulose + NAD(P)H
D-threitol + NAD(P)+
D-erythrulose + NADH + H+
D-threitol + NAD+
diacetyl + NAD(P)H
acetoin + NADP+
ethyl pyruvate + NADPH
ethyllactate + NADP+
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Substrates: - Products: -
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isatin + NADPH
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Substrates: s-cis configuration of the neighbouring carbonyls is important for activity Products: -
?
methyl pyruvate + NADPH
methyllactate + NADP+
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Substrates: - Products: -
?
Phenanthrenequinone + NADPH
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Substrates: s-cis configuration of the neighbouring carbonyls is important for activity Products: -
?
D-erythrulose + NAD(P)H
D-threitol + NAD(P)+
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Substrates: several substrates listed that do not serve as substrates Products: -
r
D-erythrulose + NAD(P)H
D-threitol + NAD(P)+
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Substrates: highly specific for D-erythrulose Products: -
ir
D-erythrulose + NAD(P)H
D-threitol + NAD(P)+
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Substrates: highly specific for D-erythrulose Products: -
r
D-erythrulose + NAD(P)H
D-threitol + NAD(P)+
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Substrates: highly specific for D-erythrulose Products: in reference 2 the enzymatic reaction product of D-erythrulose is incorrectly identified as erythritol, gas-liquid and thin-layer chromatographic data have confirmed the product to be D-threitol, not erythritol, for this reason the systematic name D-threitol:NADP+ oxidoreductase should be used instead of erythritol:NADP+ oxidoreductase which has been designated by the IUB Enzyme commission
r
D-erythrulose + NAD(P)H
D-threitol + NAD(P)+
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Substrates: reversibility could not be demonstrated Products: -
ir
D-erythrulose + NAD(P)H
D-threitol + NAD(P)+
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Substrates: the equilibrium of the reaction strongly favors the reduction of D-erythrulose, the reverse reaction is slightly detectable when carried out at pH 7.5-9.0 using NADP+, erythritol does not serve as substrate Products: in reference 2 the enzymatic reaction product of D-erythrulose is incorrectly identified as erythritol, gas-liquid and thin-layer chromatographic data have confirmed the product to be D-threitol, not erythritol, for this reason the systematic name D-threitol:NADP+ oxidoreductase should be used instead of erythritol:NADP+ oxidoreductase which has been designated by the IUB Enzyme commission
r
D-erythrulose + NAD(P)H
D-threitol + NAD(P)+
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Substrates: - Products: -
r
D-erythrulose + NAD(P)H
D-threitol + NAD(P)+
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Substrates: several substrates listed that do not serve as substrates Products: -
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D-erythrulose + NAD(P)H
D-threitol + NAD(P)+
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Substrates: highly specific for D-erythrulose Products: -
r
D-erythrulose + NAD(P)H
D-threitol + NAD(P)+
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Substrates: highly specific for D-erythrulose Products: reverse reaction rate is very low
r
D-erythrulose + NAD(P)H
D-threitol + NAD(P)+
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Substrates: the equilibrium of the reaction strongly favors the reduction of D-erythrulose, the reverse reaction is slightly detectable when carried out at pH 7.5-9.0 using NADP+, erythritol does not serve as substrate Products: reverse reaction rate is very low
r
D-erythrulose + NADH + H+
D-threitol + NAD+
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Substrates: - Products: -
r
D-erythrulose + NADH + H+
D-threitol + NAD+
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Substrates: - Products: -
r
diacetyl + NAD(P)H
acetoin + NADP+
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Substrates: utilizes mainly vicinal alpha-dicarbonyls Products: -
?, ir
diacetyl + NAD(P)H
acetoin + NADP+
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Substrates: reaction is also performed by acetoin:NAD+ oxidoreductase, EC 1.1.1.5 Products: -
?, ir
diacetyl + NAD(P)H
acetoin + NADP+
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Substrates: specific for alpha-dicarbonyls Products: -
?, ir
diacetyl + NAD(P)H
acetoin + NADP+
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Substrates: detoxification of food derived dicarbonyls Products: -
ir
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D-erythrulose + NAD(P)+
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Substrates: one route of formation of tetritols in mammalia Products: -
r
diacetyl + NAD(P)H
acetoin + NADP+
diacetyl + NAD(P)H
acetoin + NADP+
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Substrates: reaction is also performed by acetoin:NAD+ oxidoreductase, EC 1.1.1.5 Products: -
ir
diacetyl + NAD(P)H
acetoin + NADP+
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Substrates: detoxification of food derived dicarbonyls Products: -
ir
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NADH
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NADH
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NADH usage is recommended for the developed assay because it is more stable than NADPH under the assay conditions
NADH
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NADH usage is recommended for the developed assay because it is more stable than NADPH under the assay conditions
NADH
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utilized more slowly than NADPH
NADP+
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NADP+
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enzyme contains 2-3 mol of bound NADP+
NADP+
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enzyme contains 2-3 mol of bound NADP+
NADPH
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0.68
(1S)-(+)-Camphorquinone
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0.67
1,2-Cyclohexanedione
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0.26
2,3-heptanedione
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0.24
2,3-Pentanedione
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0.11 - 0.38
D-erythrulose
0.021
Phenanthrenequinone
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0.11
D-erythrulose
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0.36
D-erythrulose
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with NADH
0.067
NADH
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0.0068
NADPH
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320
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purified enzyme, D-erythrulose
64
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(1S)-(+)-camphorquinone
120
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2,3-pentanedione
120
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1,2-cyclohexanedione
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5.8
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D-erythrulose + NADPH
5.8 - 6
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diacetyl + NADPH
5.85
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D-erythrulose + NADH
6 - 6.8
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diacetyl + NADH
6.25
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D-erythrulose + NADH
6.3
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D-erythrulose + NADH
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7.5 - 9
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oxidation of acetoin to 2,3-butanediol
6.25 - 8
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depending on the assay conditions
6.25 - 8
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depending on the assay conditions
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25
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assay at
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brenda
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brenda
NCBI Nucleotide:AB049356
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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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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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most abundant
brenda
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brenda
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brenda
additional information
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minimal activity also in lens, spleen, lung and pancreas
brenda
additional information
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enzyme is detected in all organs tested
brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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DER_CHICK
246
0
26167
Swiss-Prot
Mitochondrion (Reliability: 4 )
A0A0E0UF07_SINMB
Sinorhizobium meliloti (strain BL225C)
241
0
24566
TrEMBL
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E0VB89_PEDHC
200
0
21610
TrEMBL
other Location (Reliability: 2 )
D5RTL5_9PROT
199
0
19743
TrEMBL
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A0A1B9VNB7_9PROT
243
0
25201
TrEMBL
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B7Q1L6_IXOSC
244
0
25736
TrEMBL
Mitochondrion (Reliability: 4 )
D5RR15_9PROT
228
1
23260
TrEMBL
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D5RSH8_9PROT
258
0
26723
TrEMBL
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22000
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4 * 22000, SDS-PAGE
22400
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4 * 22400, SDS-PAGE
90000
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sedimentation equilibrium analysis, gel filtration, sucrose density gradient centrifugation
96000
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sedimentation equilibrium analysis
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additional information
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comparative modeling of enzyme based on structure of tetrameric carbonyl reductase
tetramer
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4 * 22000, SDS-PAGE
tetramer
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4 * 22400, SDS-PAGE
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additional information
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probably acetylated methionine at N-terminal
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8.5
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maximal stability
286089
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0
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23.5 h, 90% loss of activity, regains about 55-65% of its original activity after 60 min
21
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23.5 h, 20-25% loss of activity
additional information
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cold inactivation
additional information
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cold inactivation
additional information
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cold inactivation
additional information
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cold inactivation accelerated by increasing salt concentration and decreasing enzyme concentration
additional information
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chicken: quite stable, even when a dilute solution at high ionic strength is incubated at low temperatures
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2,5'-ADP protects against Rose bengal-sensitized photoinactivation, to a lesser extent than NADP+
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NADP+ protects against heat inactivation or Rose bengal-sensitized photoinactivation and cold inactivation
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NADP+ protects against pH inactivation
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photooxidation, in presence of Rose bengal, protection by NADP+ and to a lesser extent by 2',5'-ADP
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286086, 286090
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4°C, as crystalline suspension in 1.43 mM ammonium sulfate, pH 8.2, 15 mM dithiothreitol, 0.2 mM NADP+, several months
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analysis
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assay development for microdetection of D-erythrulose in catabolic pathway analysis
analysis
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assay development for microdetection of D-erythrulose in catabolic pathway analysis
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Uehara, K.; Hosomi, S.
D-Erythrulose reductase from beef liver
Methods Enzymol.
89
232-237
1982
Bos taurus
brenda
Uehara, K.; Tanimoto, T.; Sato, H.
Studies on D-tetrose metabolism. IV. Purification and some properties of D-erythrulose reductase from beef liver
J. Biochem.
75
333-345
1974
Bos taurus
brenda
Uehara, K.; Mannen, S.; Hosomi, S.; Miyashita, T.
Studies on D-tetrose metabolism. Crystallization and properties of D-erythrulose reductase from chicken liver
J. Biochem.
87
47-55
1980
Gallus gallus
brenda
Uehara, K.; Tanimoto, T.
Studies on D-tetrose metabolism. VI. Crystallization and some properties of D-erythrulose reducatase from beef liver
J. Biochem.
78
519-526
1975
Bos taurus
brenda
Uehara, K.; Mannen, S.; Hosomi, S.
Effect of NADP+ and its analogs on the Rose Bengal-sensitized photoinactivation of D-erythrulose reductase from beef liver
J. Biochem.
85
1003-1008
1979
Bos taurus
brenda
Maeda, M.; Hosomi, S.; Mizoguchi, T.; Nishihara, T.
D-erythrulose reductase can also reduce diacetyl: further purification and characterization of D-erythrulose reductase from chicken liver
J. Biochem.
123
602-606
1998
Gallus gallus
brenda
Morii, K.; Hosomi, S.; Terada, T.; Mizoguchi, T.
Methods for enzymatic and colorimetric determinations of D-erythrulose (D-tetrulose)
Anal. Biochem.
151
188-191
1985
Bos taurus, Gallus gallus
brenda
Maeda, M.; Kaku, H.; Shimada, M.; Nishioka, T.
Cloning and sequence analysis of D-erythrulose reductase from chicken: its close structural relation to tetrameric carbonyl reductases
Protein Eng.
15
611-617
2002
Gallus gallus
brenda
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