BRENDA - Enzyme Database show
show all sequences of 1.1.1.116

NAD(+)-specific D-arabinose dehydrogenase and its contribution to erythroascorbic acid production in Saccharomyces cerevisiae

Amako, K.; Fujita, K.; Shimohata, T.A.; Hasegawa, E.; Kishimoto, R.; Goda, K.; FEBS Lett. 580, 6428-6434 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene YMR041c or ARA2, phylogenetic tree, expression of His6-tagged Ara2p in Escherichia coli
Saccharomyces cerevisiae
Engineering
Amino acid exchange
Commentary
Organism
additional information
ARA2 gene disruption leads to complete loss of NAD+-specific D-arabinose dehydrogenase activity
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
D-arabinose
substrate inhibition of Ara2p at concentrations above 5 mM
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.78
-
D-arabinose
pH 8.2, 25°C, recombinant His-tagged Ara2p
Saccharomyces cerevisiae
4.1
-
NAD+
pH 8.2, 25°C, recombinant His-tagged Ara2p
Saccharomyces cerevisiae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
recombinant Ara2p, gel filtration
Saccharomyces cerevisiae
42400
-
1 * 42400, recombinant Ara2p, SDS-PAGE
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-arabinose + NAD+
Saccharomyces cerevisiae
the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
D-arabinono-1,4-lactone + NADH
-
-
?
D-arabinose + NAD+
Saccharomyces cerevisiae YPH250
the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
D-arabinono-1,4-lactone + NADH
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
Q04212
ARA2; strain YPH250, gene YMR041c or ARA2, isozyme Ara2p
-
Saccharomyces cerevisiae YPH250
Q04212
ARA2; strain YPH250, gene YMR041c or ARA2, isozyme Ara2p
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged Ara2p from Escherichia coli by anion exchange and nickel affinity chromatography to homogeneity
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.00071
-
NAD+-dependent Ara2p reaction in presence of 200 mM D-arabinose, native cell extract
Saccharomyces cerevisiae
1.8
-
purified recombinant His-tagged ARA2p
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinose + NAD+
the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
668641
Saccharomyces cerevisiae
D-arabinono-1,4-lactone + NADH
-
-
-
?
D-arabinose + NAD+
preferred sugar substrate
668641
Saccharomyces cerevisiae
D-arabinono-1,4-lactone + NADH
-
-
-
?
D-arabinose + NAD+
the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
668641
Saccharomyces cerevisiae YPH250
D-arabinono-1,4-lactone + NADH
-
-
-
?
D-arabinose + NAD+
preferred sugar substrate
668641
Saccharomyces cerevisiae YPH250
D-arabinono-1,4-lactone + NADH
-
-
-
?
L-fucose + NAD+
-
668641
Saccharomyces cerevisiae
?
-
-
-
?
L-fucose + NAD+
-
668641
Saccharomyces cerevisiae YPH250
?
-
-
-
?
L-galactose + NAD+
-
668641
Saccharomyces cerevisiae
?
-
-
-
?
L-galactose + NAD+
-
668641
Saccharomyces cerevisiae YPH250
?
-
-
-
?
L-xylose + NAD+
-
668641
Saccharomyces cerevisiae
?
-
-
-
?
additional information
ARa2p shows a broad sugar substrate specificity, but prefers D-arabinose
668641
Saccharomyces cerevisiae
?
-
-
-
-
additional information
ARa2p shows a broad sugar substrate specificity, but prefers D-arabinose
668641
Saccharomyces cerevisiae YPH250
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 42400, recombinant Ara2p, SDS-PAGE
Saccharomyces cerevisiae
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.2
-
-
Saccharomyces cerevisiae
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6.5
9
20% of maximal activity at pH 6.5 and pH 9.0, pH profile
Saccharomyces cerevisiae
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
Ara2p is specific for NAD+, while Ara1p utilizes NADP+
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
gene YMR041c or ARA2, phylogenetic tree, expression of His6-tagged Ara2p in Escherichia coli
Saccharomyces cerevisiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
Ara2p is specific for NAD+, while Ara1p utilizes NADP+
Saccharomyces cerevisiae
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
ARA2 gene disruption leads to complete loss of NAD+-specific D-arabinose dehydrogenase activity
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
D-arabinose
substrate inhibition of Ara2p at concentrations above 5 mM
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.78
-
D-arabinose
pH 8.2, 25°C, recombinant His-tagged Ara2p
Saccharomyces cerevisiae
4.1
-
NAD+
pH 8.2, 25°C, recombinant His-tagged Ara2p
Saccharomyces cerevisiae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
recombinant Ara2p, gel filtration
Saccharomyces cerevisiae
42400
-
1 * 42400, recombinant Ara2p, SDS-PAGE
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-arabinose + NAD+
Saccharomyces cerevisiae
the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
D-arabinono-1,4-lactone + NADH
-
-
?
D-arabinose + NAD+
Saccharomyces cerevisiae YPH250
the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
D-arabinono-1,4-lactone + NADH
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged Ara2p from Escherichia coli by anion exchange and nickel affinity chromatography to homogeneity
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.00071
-
NAD+-dependent Ara2p reaction in presence of 200 mM D-arabinose, native cell extract
Saccharomyces cerevisiae
1.8
-
purified recombinant His-tagged ARA2p
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinose + NAD+
the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
668641
Saccharomyces cerevisiae
D-arabinono-1,4-lactone + NADH
-
-
-
?
D-arabinose + NAD+
preferred sugar substrate
668641
Saccharomyces cerevisiae
D-arabinono-1,4-lactone + NADH
-
-
-
?
D-arabinose + NAD+
the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
668641
Saccharomyces cerevisiae YPH250
D-arabinono-1,4-lactone + NADH
-
-
-
?
D-arabinose + NAD+
preferred sugar substrate
668641
Saccharomyces cerevisiae YPH250
D-arabinono-1,4-lactone + NADH
-
-
-
?
L-fucose + NAD+
-
668641
Saccharomyces cerevisiae
?
-
-
-
?
L-fucose + NAD+
-
668641
Saccharomyces cerevisiae YPH250
?
-
-
-
?
L-galactose + NAD+
-
668641
Saccharomyces cerevisiae
?
-
-
-
?
L-galactose + NAD+
-
668641
Saccharomyces cerevisiae YPH250
?
-
-
-
?
L-xylose + NAD+
-
668641
Saccharomyces cerevisiae
?
-
-
-
?
additional information
ARa2p shows a broad sugar substrate specificity, but prefers D-arabinose
668641
Saccharomyces cerevisiae
?
-
-
-
-
additional information
ARa2p shows a broad sugar substrate specificity, but prefers D-arabinose
668641
Saccharomyces cerevisiae YPH250
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 42400, recombinant Ara2p, SDS-PAGE
Saccharomyces cerevisiae
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.2
-
-
Saccharomyces cerevisiae
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6.5
9
20% of maximal activity at pH 6.5 and pH 9.0, pH profile
Saccharomyces cerevisiae
Other publictions for EC 1.1.1.116
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)
695806
Lin
Application of comparative pro ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae LH1
Appl. Microbiol. Biotechnol.
80
831-839
2008
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1
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668641
Amako
NAD(+)-specific D-arabinose de ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH250
FEBS Lett.
580
6428-6434
2006
-
-
1
-
1
-
1
2
-
-
2
2
-
4
-
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1
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2
-
11
1
1
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1
1
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1
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-
1
1
-
1
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-
1
-
2
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2
2
-
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-
1
-
-
2
-
11
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
668709
Baroja-Mazo
Characterisation and biosynthe ...
Phycomyces blakesleeanus
Fungal Genet. Biol.
42
390-402
2005
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-
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1
3
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3
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1
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1
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1
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1
3
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1
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1
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4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
654283
Sauer
Production of L-ascorbic acid ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae GRF18U
Appl. Environ. Microbiol.
70
6086-6091
2004
-
1
1
-
-
-
-
-
-
-
-
2
-
8
-
-
-
-
-
-
1
-
2
-
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-
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-
1
-
-
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1
1
1
-
-
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-
2
-
-
-
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-
1
-
2
-
-
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-
-
-
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-
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-
-
-
-
-
285774
Kim
D-Arabinose dehydrogenase and ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1429
29-39
1998
-
-
-
-
-
-
-
4
1
-
3
-
-
2
-
-
1
-
-
-
1
-
6
1
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
4
1
-
3
-
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-
1
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-
1
-
6
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
10663
Kim
D-Arabinose dehydrogenase and ...
Candida albicans
Biochim. Biophys. Acta
1297
1-8
1996
-
-
-
-
-
-
9
4
1
-
2
-
-
2
-
-
1
-
-
-
1
-
5
1
1
-
-
-
1
-
1
1
-
-
-
-
-
-
1
-
-
-
-
9
-
4
1
-
2
-
-
-
-
1
-
-
1
-
5
1
1
-
-
-
1
-
1
-
-
-
-
-
-
-
285771
Carrasco
Genetic and biochemical charac ...
Neurospora crassa
J. Bacteriol.
145
164-170
1981
-
-
-
-
-
-
-
2
-
-
2
-
-
2
-
-
1
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-
1
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1
1
1
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1
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1
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1
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1
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2
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2
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1
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1
-
1
1
1
-
1
-
1
-
-
-
-
-
-
-
-
-
285772
Yamanaka
-
Specific microassay of D-arabi ...
Pseudomonas sp.
Agric. Biol. Chem.
39
2227-2234
1975
-
-
-
-
-
-
2
4
-
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1
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1
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4
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1
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1
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1
2
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2
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2
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4
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1
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4
-
1
-
-
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1
-
1
-
-
-
-
-
-
-
285770
Carper
Arabinose (fucose) dehydrogena ...
Sus scrofa
Biochim. Biophys. Acta
358
49-56
1974
-
-
-
-
-
-
3
-
-
-
-
-
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1
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1
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5
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1
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1
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1
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1
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3
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1
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5
-
1
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-
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1
-
-
-
-
-
-
-
-
-
285768
Pincheira G.; Leon G.; Ureta
Aldosugar dehydrogenases from ...
Neurospora crassa
FEBS Lett.
30
111-114
1973
-
-
-
-
-
2
-
2
-
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1
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1
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8
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1
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1
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2
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2
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1
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8
-
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285769
Maijub
Arabinose (fucose) dehydrogena ...
Sus scrofa
Biochim. Biophys. Acta
315
37-42
1973
-
-
-
-
-
1
-
3
-
-
1
1
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1
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1
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1
2
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3
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1
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1
1
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1
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1
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1
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3
-
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1
1
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1
-
1
2
-
3
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
285767
Schiwara
Differenzierung verschiedener ...
Sus scrofa
Hoppe-Seyler's Z. Physiol. Chem.
349
1575-1581
1968
-
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4
5
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1
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1
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1
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7
-
1
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1
1
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2
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2
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4
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5
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1
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1
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7
-
1
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1
1
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