BRENDA - Enzyme Database show
show all sequences of 1.1.1.87

Kinetic analysis of human enzyme RDH10 defines the characteristics of a physiologically relevant retinol dehydrogenase

Belyaeva, O.V.; Johnson, M.P.; Kedishvili, N.Y.; J. Biol. Chem. 283, 20299-20308 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Sf9 cell; RDH10 is expressed the enzyme in insect Sf9 cells using the Baculovirus expression system. Purification of RDH10-His6 from Sf9 cells using nickel affinity chromatography produces an inactive enzyme. Therefore, microsomal preparations of RDH10 are used for its kinetic characterization
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
11-cis-retinol
substrate inhibition above 0.005 mM
Homo sapiens
9-cis-retinol
substrate inhibition above 0.001 mM
Homo sapiens
all-trans-retinol
substrate inhibition
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.035
-
all-trans-retinol
; microsomal preparations of RDH10, cofactor: NAD+
Homo sapiens
0.04
-
9-cis-retinol
microsomal preparations of RDH10
Homo sapiens
0.06
-
11-cis-retinol
microsomal preparations of RDH10
Homo sapiens
0.1
-
NAD+
; microsomal preparations of RDH10
Homo sapiens
0.4
-
all-trans-retinal
; microsomal preparations of RDH10
Homo sapiens
6
-
9-cis-retinol
-
Homo sapiens
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
39600
-
x * 39600, SDS-PAGE and calculated
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Homo sapiens
dual physiological role of isoform RDH10: in the biosynthesis of 11-cis-retinaldehyde for vision and in the biosynthesis of all-trans-retinoic acid for differentiation and development
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
isoform Rdh10
-
Homo sapiens
Q8IZV5
-
-
Purification (Commentary)
Commentary
Organism
purification of His-tagged enzyme using nickel affinity chromatography results in an inactive enzyme
Homo sapiens
Storage Stability
Storage Stability
Organism
-20C, some loss of activity after repeated freeze-thawing cycles
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
11-cis-retinol + NAD+
microsomal preparations of RDH10 are not active in presence of NADP+
687735
Homo sapiens
11-cis-retinal + NADH + H+
-
-
-
r
11-cis-retinol + NADP+
-
687735
Homo sapiens
11-cis-retinal + NADPH
-
-
-
?
9-cis-retinol + NAD+
microsomal preparations of RDH10 are not active in presence of NADP+
687735
Homo sapiens
9-cis-retinal + NADH + H+
-
-
-
r
9-cis-retinol + NADP+
-
687735
Homo sapiens
9-cis-retinal + NADPH
-
-
-
?
all-trans-retinal + NADPH + H+
-
687735
Homo sapiens
all-tans-retinol + NADP+
-
-
-
r
all-trans-retinol + NAD+
RDH10 is a more efficient retinol dehydrogenase than a retinaldehyde reductase. Microsomal preparations of RDH10 are not active in presence of NADP+
687735
Homo sapiens
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol + NADPH
-
687735
Homo sapiens
all-trans-retinal + NADP+
-
-
-
r
additional information
dual physiological role of isoform RDH10: in the biosynthesis of 11-cis-retinaldehyde for vision and in the biosynthesis of all-trans-retinoic acid for differentiation and development
687735
Homo sapiens
?
-
-
-
-
additional information
enzyme does not recognizes retinol bound to cellular retinol-binding protein type I as a substrate and functions exclusively in the oxidative reaction in cells
687735
Homo sapiens
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 39600, SDS-PAGE and calculated
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
isoform RDH10 is strictly NAD+-dependent; microsomal preparations of RDH10 are not active in presence of NADP+
Homo sapiens
NADH
-
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Sf9 cell
Homo sapiens
RDH10 is expressed the enzyme in insect Sf9 cells using the Baculovirus expression system. Purification of RDH10-His6 from Sf9 cells using nickel affinity chromatography produces an inactive enzyme. Therefore, microsomal preparations of RDH10 are used for its kinetic characterization
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
isoform RDH10 is strictly NAD+-dependent
Homo sapiens
NAD+
microsomal preparations of RDH10 are not active in presence of NADP+
Homo sapiens
NADH
-
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
11-cis-retinol
substrate inhibition above 0.005 mM
Homo sapiens
9-cis-retinol
substrate inhibition above 0.001 mM
Homo sapiens
all-trans-retinol
substrate inhibition
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.035
-
all-trans-retinol
-
Homo sapiens
0.035
-
all-trans-retinol
microsomal preparations of RDH10, cofactor: NAD+
Homo sapiens
0.04
-
9-cis-retinol
microsomal preparations of RDH10
Homo sapiens
0.06
-
11-cis-retinol
microsomal preparations of RDH10
Homo sapiens
0.1
-
NAD+
-
Homo sapiens
0.1
-
NAD+
microsomal preparations of RDH10
Homo sapiens
0.4
-
all-trans-retinal
-
Homo sapiens
0.4
-
all-trans-retinal
microsomal preparations of RDH10
Homo sapiens
6
-
9-cis-retinol
-
Homo sapiens
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
39600
-
x * 39600, SDS-PAGE and calculated
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Homo sapiens
dual physiological role of isoform RDH10: in the biosynthesis of 11-cis-retinaldehyde for vision and in the biosynthesis of all-trans-retinoic acid for differentiation and development
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
purification of His-tagged enzyme using nickel affinity chromatography results in an inactive enzyme
Homo sapiens
Storage Stability (protein specific)
Storage Stability
Organism
-20C, some loss of activity after repeated freeze-thawing cycles
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
11-cis-retinol + NAD+
microsomal preparations of RDH10 are not active in presence of NADP+
687735
Homo sapiens
11-cis-retinal + NADH + H+
-
-
-
r
11-cis-retinol + NADP+
-
687735
Homo sapiens
11-cis-retinal + NADPH
-
-
-
?
9-cis-retinol + NAD+
microsomal preparations of RDH10 are not active in presence of NADP+
687735
Homo sapiens
9-cis-retinal + NADH + H+
-
-
-
r
9-cis-retinol + NADP+
-
687735
Homo sapiens
9-cis-retinal + NADPH
-
-
-
?
all-trans-retinal + NADPH + H+
-
687735
Homo sapiens
all-tans-retinol + NADP+
-
-
-
r
all-trans-retinol + NAD+
RDH10 is a more efficient retinol dehydrogenase than a retinaldehyde reductase. Microsomal preparations of RDH10 are not active in presence of NADP+
687735
Homo sapiens
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol + NADPH
-
687735
Homo sapiens
all-trans-retinal + NADP+
-
-
-
r
additional information
dual physiological role of isoform RDH10: in the biosynthesis of 11-cis-retinaldehyde for vision and in the biosynthesis of all-trans-retinoic acid for differentiation and development
687735
Homo sapiens
?
-
-
-
-
additional information
enzyme does not recognizes retinol bound to cellular retinol-binding protein type I as a substrate and functions exclusively in the oxidative reaction in cells
687735
Homo sapiens
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 39600, SDS-PAGE and calculated
Homo sapiens
Other publictions for EC 1.1.1.87
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)
722303
Gabriel
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-
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1
-
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3
4
-
2
3
2
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8
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1
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6
2
1
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1
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3
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3
2
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1
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6
2
1
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4
1
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1
1
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4
4
722569
Nango
Structure of Thermus thermophi ...
Thermus thermophilus
J. Biochem.
150
607-614
2011
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1
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2
1
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1
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1
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5
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2
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1
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1
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1
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1
1
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690842
Takahashi
Characterization of key residu ...
Homo sapiens
Biochem. J.
419
113-122
2009
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1
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13
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8
1
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692705
Farjo
RDH10 has 11-cis-retinol dehyd ...
Homo sapiens
Invest. Ophthalmol. Vis. Sci.
50
5089-5097
2009
1
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1
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4
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696350
Lin
Site-directed mutagenesis as a ...
Saccharomyces cerevisiae
Biochemistry
48
7305-7312
2009
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2
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1
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2
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1
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2
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2
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1
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2
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1
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2
1
-
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685232
Lin
Chemical mechanism of homoisoc ...
Saccharomyces cerevisiae
Biochemistry
47
4169-4180
2008
-
-
-
-
-
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2
5
-
1
-
-
-
2
-
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1
-
-
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4
-
3
-
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-
1
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1
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1
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2
1
5
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1
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4
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3
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1
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1
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685539
Yamamoto
Thiahomoisocitrate: a highly p ...
Saccharomyces cerevisiae
Bioorg. Med. Chem.
16
3372-3376
2008
-
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-
-
-
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4
3
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1
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4
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3
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3
1
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3
3
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1
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3
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3
1
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687735
Belyaeva
Kinetic analysis of human enzy ...
Homo sapiens
J. Biol. Chem.
283
20299-20308
2008
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1
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3
6
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1
1
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1
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9
1
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1
9
1
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687988
Romand
Dynamic expression of the reti ...
Mus musculus
J. Comp. Neurol.
508
879-892
2008
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696220
Lin
Potassium is an activator of h ...
Saccharomyces cerevisiae
Biochemistry
47
10809-10815
2008
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4
3
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5
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1
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3
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1
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1
1
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667934
Yamamoto
Substrate specificity analysis ...
Deinococcus radiodurans, Saccharomyces cerevisiae
Bioorg. Med. Chem.
15
1346-1355
2007
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1
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11
20
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2
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7
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1
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2
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24
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2
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20
2
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9
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1
2
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11
9
20
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2
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24
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2
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2
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686287
Cammas
Expression of the murine retin ...
Mus musculus
Dev. Dyn.
236
2899-2908
2007
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686950
Sandell
RDH10 is essential for synthes ...
Mus musculus
Genes Dev.
21
1113-1124
2007
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669670
Szamtari
PPARgamma controls CD1d expres ...
Homo sapiens
J. Exp. Med.
203
2351-2362
2006
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660907
Miyazaki
Bifunctional isocitrate-homois ...
Pyrococcus horikoshii
Biochem. Biophys. Res. Commun.
331
341-346
2005
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1
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2
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660918
Miyazaki
Identification of a novel trif ...
Deinococcus radiodurans
Biochem. Biophys. Res. Commun.
336
596-602
2005
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4
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7
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2
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1
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1
1
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7
1
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669109
Miyazaki
Crystal structure of tetrameri ...
Thermus thermophilus
J. Bacteriol.
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