BRENDA - Enzyme Database show
show all sequences of 1.1.1.105

Biochemical characterization of human epidermal retinol dehydrogenase 2

Lee, S.A.; Belyaeva, O.V.; Kedishvili, N.Y.; Chem. Biol. Interact. 178, 182-187 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Sf9 insect cells and in HEK-293 cells; RDH-E2 is expressed in Sf9 insect cells as a fusion to the C-terminal His6-tag
Homo sapiens
General Stability
General Stability
Organism
gel-filtration of RDH-E2 preparation to remove imidazole results in significant loss of activity (about 90%) despite nearly complete recovery of the protein suggesting that RDH-E2 is sensitive to desalting
Homo sapiens
the enzyme is sensitive to desalting
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
imidazole
; increasing the amount of imidazole in the reaction mixture with purified RDH-E2 from 25 to 225mM significantly decreases RDH-E2 activity
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum
; RDH-E2 protein exhibits a punctuate localization pattern, surrounding the nucleus suggesting that RDH-E2 is associated with endoplasmic reticulum
Homo sapiens
5783
-
membrane
of endoplasmic reticulum
Homo sapiens
16020
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
all-trans-retinol + NAD+
Homo sapiens
exhibits a strong preference for NAD+/NADH as cofactors. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+. The preference for NAD+ suggests that RDH-E2 is likely to function in the oxidative direction in vivo, further supporting its potential role in the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in human keratinocytes
all-trans-retinal + NADH + H+
-
-
r
additional information
Homo sapiens
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
Q8N3Y7
-
-
Purification (Commentary)
Commentary
Organism
Ni2+-NTA resin column chromatography; recombinant enzyme
Homo sapiens
Source Tissue
Source Tissue
Commentary
Organism
Textmining
epidermis
retinal dehydrogenase 2 is significantly elevated in psoriatic skin
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
all-trans-retinal + NADH + H+
-
691750
Homo sapiens
all-trans-retinol + NAD+
-
-
-
?
all-trans-retinaldehyde + NADH + H+
-
691750
Homo sapiens
?
-
-
-
?
all-trans-retinol + NAD+
exhibits a strong preference for NAD+/NADH as cofactors. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+. The preference for NAD+ suggests that RDH-E2 is likely to function in the oxidative direction in vivo, further supporting its potential role in the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in human keratinocytes
691750
Homo sapiens
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol + NAD+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+
691750
Homo sapiens
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol + NADP+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+
691750
Homo sapiens
all-trans-retinal + NADPH + H+
-
-
-
r
additional information
no activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
691750
Homo sapiens
?
-
-
-
-
additional information
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
691750
Homo sapiens
?
-
-
-
-
additional information
no activity is detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
691750
Homo sapiens
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+
Homo sapiens
NADH
exhibits a strong preference for NAD+/NADH as cofactors
Homo sapiens
NADP+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Sf9 insect cells and in HEK-293 cells; RDH-E2 is expressed in Sf9 insect cells as a fusion to the C-terminal His6-tag
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+
Homo sapiens
NADH
exhibits a strong preference for NAD+/NADH as cofactors
Homo sapiens
NADP+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+
Homo sapiens
General Stability (protein specific)
General Stability
Organism
gel-filtration of RDH-E2 preparation to remove imidazole results in significant loss of activity (about 90%) despite nearly complete recovery of the protein suggesting that RDH-E2 is sensitive to desalting
Homo sapiens
the enzyme is sensitive to desalting
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
imidazole
; increasing the amount of imidazole in the reaction mixture with purified RDH-E2 from 25 to 225mM significantly decreases RDH-E2 activity
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum
; RDH-E2 protein exhibits a punctuate localization pattern, surrounding the nucleus suggesting that RDH-E2 is associated with endoplasmic reticulum
Homo sapiens
5783
-
membrane
of endoplasmic reticulum
Homo sapiens
16020
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
all-trans-retinol + NAD+
Homo sapiens
exhibits a strong preference for NAD+/NADH as cofactors. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+. The preference for NAD+ suggests that RDH-E2 is likely to function in the oxidative direction in vivo, further supporting its potential role in the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in human keratinocytes
all-trans-retinal + NADH + H+
-
-
r
additional information
Homo sapiens
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
Ni2+-NTA resin column chromatography; recombinant enzyme
Homo sapiens
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
epidermis
retinal dehydrogenase 2 is significantly elevated in psoriatic skin
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
all-trans-retinal + NADH + H+
-
691750
Homo sapiens
all-trans-retinol + NAD+
-
-
-
?
all-trans-retinaldehyde + NADH + H+
-
691750
Homo sapiens
?
-
-
-
?
all-trans-retinol + NAD+
exhibits a strong preference for NAD+/NADH as cofactors. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+. The preference for NAD+ suggests that RDH-E2 is likely to function in the oxidative direction in vivo, further supporting its potential role in the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in human keratinocytes
691750
Homo sapiens
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol + NAD+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+
691750
Homo sapiens
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol + NADP+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+
691750
Homo sapiens
all-trans-retinal + NADPH + H+
-
-
-
r
additional information
no activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
691750
Homo sapiens
?
-
-
-
-
additional information
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
691750
Homo sapiens
?
-
-
-
-
additional information
no activity is detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
691750
Homo sapiens
?
-
-
-
-
Other publictions for EC 1.1.1.105
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738036
Adams
Characterization of human shor ...
Homo sapiens
Chem. Biol. Interact.
FEHLT
0000
2016
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1
1
1
1
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737923
Hong
Characterization of alcohol de ...
Kangiella koreensis
Biotechnol. Lett.
37
849-856
2015
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1
1
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1
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738033
Belyaeva
Evolutionary origins of retino ...
Ciona intestinalis, Lytechinus variegatus
Chem. Biol. Interact.
234
135-143
2015
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2
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11
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5
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738670
Obrochta
Insulin regulates retinol dehy ...
Homo sapiens, Mus musculus
J. Biol. Chem.
290
7259-7268
2015
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7
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3
2
3
5
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738610
Adams
The retinaldehyde reductase ac ...
Homo sapiens
J. Biol. Chem.
289
14868-14880
2014
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1
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3
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2
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1
1
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721724
Napoli
Physiological insights into al ...
Homo sapiens, Mus musculus, Rattus norvegicus
Biochim. Biophys. Acta
1821
152-167
2012
-
-
2
-
1
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1
1
6
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3
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3
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1
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6
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3
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2
3
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1
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1
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1
6
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3
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1
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6
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7
7
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722769
Chen
Reduction of all-trans-retinal ...
Mus musculus 129/Sv and C57BL/6, Mus musculus
J. Biol. Chem.
287
24662-24670
2012
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4
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1
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1
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3
3
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723076
Yu
Investigation of the associati ...
Homo sapiens
J. Zhejiang Univ. Sci. B
11
836-841
2010
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1
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1
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1
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690842
Takahashi
Characterization of key residu ...
Homo sapiens
Biochem. J.
419
113-122
2009
-
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1
-
12
-
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6
1
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1
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1
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12
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6
1
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1
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691750
Lee
Biochemical characterization o ...
Homo sapiens
Chem. Biol. Interact.
178
182-187
2009
-
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1
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2
1
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2
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2
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2
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1
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8
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3
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1
3
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1
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1
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8
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697544
Strate
Retinol dehydrogenase 10 is a ...
Xenopus laevis
Development
136
461-472
2009
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1
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691705
Pares
Medium- and short-chain dehydr ...
Homo sapiens, Mus musculus, Rattus norvegicus
Cell. Mol. Life Sci.
65
3936-3949
2008
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697796
Moradi
Focus on molecules: Retinol de ...
Homo sapiens
Exp. Eye Res.
87
160-161
2008
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1
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686662
Dalfo
Analysis of the NADH-dependent ...
Branchiostoma floridae
FEBS J.
274
3739-3752
2007
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1
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689771
Maeda
Redundant and unique roles of ...
Mus musculus
Proc. Natl. Acad. Sci. USA
104
19565-19570
2007
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667537
Gallego
Comparative functional analysi ...
Homo sapiens
Biochem. J.
399
101-109
2006
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669445
Liden
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656260
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Elements in the N-terminal sig ...
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51482-51489
2004
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654431
Karlsson
13-cis-retinoic acid competiti ...
Homo sapiens
Biochem. Biophys. Res. Commun.
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273-278
2003
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654713
Lapshina
Differential recognition of th ...
Homo sapiens
Biochemistry
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776-784
2003
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691736
Belyaeva
Characterization of truncated ...
Homo sapiens
Chem. Biol. Interact.
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2003
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287272
Tajima
Co-ordinated induction of beta ...
Gallus gallus
Comp. Biochem. Physiol. B
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425-434
2001
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692959
Zhang
Chen, W.; Smith, S.M.; Napoli, ...
Mus musculus
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44083-44090
2001
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285728
Jurukovski
Cloning and characterization o ...
Homo sapiens
Mol. Genet. Metab.
67
62-73
1999
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285727
Gough
cDNA cloning and characterizat ...
Homo sapiens
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1998
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285724
Leo
NAD+-dependent retinol dehydro ...
Rattus norvegicus
Methods Enzymol.
189
520-524
1990
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285725
Leo
NAD+-dependent retinol dehydro ...
Peromyscus maniculatus, Rattus norvegicus
Arch. Biochem. Biophys.
259
241-249
1987
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285726
Kishore
Enzymatic oxidation and reduct ...
Mus musculus
Biochem. Biophys. Res. Commun.
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1381-1386
1980
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285723
Koen
Retinol and alcohol dehydrogen ...
Rattus norvegicus
Biochim. Biophys. Acta
128
48-54
1966
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