BRENDA - Enzyme Database show
show all sequences of 1.4.3.5

Partial purification and property of pyridoxine (pyridoxamine)-5-phosphate oxidase isozymes from wheat seedlings

Tsuge, H.; Kuroda, Y.; Iwamoto, A.; Ohashi, K.; Arch. Biochem. Biophys. 217, 479-484 (1982)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
ammonium sulfate
short incubation activates isozyme E-II, not E-I
Triticum aestivum
Inhibitors
Inhibitors
Commentary
Organism
Structure
ammonium sulfate
1.9 M, E II: activation at short incubation time, E I: complete inactivation after 10 h incubation; inactivation of isozyme E-I after 10 h
Triticum aestivum
Cd2+
0.5 mM, isozyme E I: insensitive, isozyme E II: 44% inhibition; 44% reduced activity of isozyme E-II, no inhibition of isozyme E-I
Triticum aestivum
citrate-phosphate buffer
-
Triticum aestivum
Hg2+
0.5 mM, isozyme E I: insensitive, isozyme E II: 54% inhibition; 72% reduced activity of isozyme E-II, no inhibition of isozyme E-I
Triticum aestivum
Zn2+
0.5 mM, isozyme E I: insensitive, isozyme E II: 54% inhibition; 72% reduced activity of isozyme E-II, no inhibition of isozyme E-I
Triticum aestivum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0067
-
pyridoxamine 5'-phosphate
isozyme E-II, pH 8.0, 37C
Triticum aestivum
0.008
-
pyridoxine 5'-phosphate
isozyme E-II, pH 8.0, 37C
Triticum aestivum
0.02
-
pyridoxine 5'-phosphate
isozyme E-I, pH 8.0, 37C
Triticum aestivum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Triticum aestivum
-
isozymes: E1 and E2; two isozymes E-I and E-II
-
Purification (Commentary)
Commentary
Organism
two isozymes from seedlings, partially by anion exchange and adsorption chromatography
Triticum aestivum
Source Tissue
Source Tissue
Commentary
Organism
Textmining
seedling
-
Triticum aestivum
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.00188
-
isozyme EII
Triticum aestivum
0.00367
-
isozyme EI
Triticum aestivum
0.113
-
purified isozyme E-II, substrate pyridoxine 5'-phosphate
Triticum aestivum
0.45
-
purified isozyme E-I, substrate pyridoxine 5'-phosphate
Triticum aestivum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
1.6fold preferred substrate of isozyme E-II
391881
Triticum aestivum
pyridoxal 5'-phosphate + FMNH2 + NH3
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
E II uses pyridoxine 5'-phosphate and pyridoxamine 5'-phosphate
391881
Triticum aestivum
pyridoxal 5'-phosphate + NH3 + H2O2
-
391881
Triticum aestivum
?
pyridoxamine 5'-phosphate + H2O + O2
isozymes E I uses only pyridoxine 5'-phosphate as substrate
391881
Triticum aestivum
pyridoxal 5'-phosphate + NH3 + H2O2
-
391881
Triticum aestivum
?
pyridoxine 5'-phosphate + FMN
9fold preferred substrate of isozyme E-I
391881
Triticum aestivum
pyridoxal 5'-phosphate + FMNH2
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Triticum aestivum
40
-
isozymes EI and EII, rapid decrease above
Triticum aestivum
Temperature Range [C]
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
additional information
-
rapid decrease in activity above 40C, both isozymes
Triticum aestivum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.5
-
; both isozymes
Triticum aestivum
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
6.1
-
37C, 30 min, isozyme E I: 85% loss of activity, isozyme E II: 50% loss of activity
Triticum aestivum
Cofactor
Cofactor
Commentary
Organism
Structure
FMN
-
Triticum aestivum
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Triticum aestivum
the pI values of the isozymes differ from each other
-
additional information
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
ammonium sulfate
short incubation activates isozyme E-II, not E-I
Triticum aestivum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FMN
-
Triticum aestivum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ammonium sulfate
1.9 M, E II: activation at short incubation time, E I: complete inactivation after 10 h incubation; inactivation of isozyme E-I after 10 h
Triticum aestivum
Cd2+
0.5 mM, isozyme E I: insensitive, isozyme E II: 44% inhibition; 44% reduced activity of isozyme E-II, no inhibition of isozyme E-I
Triticum aestivum
citrate-phosphate buffer
-
Triticum aestivum
Hg2+
0.5 mM, isozyme E I: insensitive, isozyme E II: 54% inhibition; 72% reduced activity of isozyme E-II, no inhibition of isozyme E-I
Triticum aestivum
Zn2+
0.5 mM, isozyme E I: insensitive, isozyme E II: 54% inhibition; 72% reduced activity of isozyme E-II, no inhibition of isozyme E-I
Triticum aestivum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0067
-
pyridoxamine 5'-phosphate
isozyme E-II, pH 8.0, 37C
Triticum aestivum
0.008
-
pyridoxine 5'-phosphate
isozyme E-II, pH 8.0, 37C
Triticum aestivum
0.02
-
pyridoxine 5'-phosphate
isozyme E-I, pH 8.0, 37C
Triticum aestivum
Purification (Commentary) (protein specific)
Commentary
Organism
two isozymes from seedlings, partially by anion exchange and adsorption chromatography
Triticum aestivum
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
seedling
-
Triticum aestivum
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.00188
-
isozyme EII
Triticum aestivum
0.00367
-
isozyme EI
Triticum aestivum
0.113
-
purified isozyme E-II, substrate pyridoxine 5'-phosphate
Triticum aestivum
0.45
-
purified isozyme E-I, substrate pyridoxine 5'-phosphate
Triticum aestivum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
1.6fold preferred substrate of isozyme E-II
391881
Triticum aestivum
pyridoxal 5'-phosphate + FMNH2 + NH3
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
E II uses pyridoxine 5'-phosphate and pyridoxamine 5'-phosphate
391881
Triticum aestivum
pyridoxal 5'-phosphate + NH3 + H2O2
-
391881
Triticum aestivum
?
pyridoxamine 5'-phosphate + H2O + O2
isozymes E I uses only pyridoxine 5'-phosphate as substrate
391881
Triticum aestivum
pyridoxal 5'-phosphate + NH3 + H2O2
-
391881
Triticum aestivum
?
pyridoxine 5'-phosphate + FMN
9fold preferred substrate of isozyme E-I
391881
Triticum aestivum
pyridoxal 5'-phosphate + FMNH2
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Triticum aestivum
40
-
isozymes EI and EII, rapid decrease above
Triticum aestivum
Temperature Range [C] (protein specific)
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
additional information
-
rapid decrease in activity above 40C, both isozymes
Triticum aestivum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.5
-
; both isozymes
Triticum aestivum
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
6.1
-
37C, 30 min, isozyme E I: 85% loss of activity, isozyme E II: 50% loss of activity
Triticum aestivum
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Triticum aestivum
the pI values of the isozymes differ from each other
-
additional information
Other publictions for EC 1.4.3.5
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)
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2
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2
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2
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2
-
-
-
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2
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-
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-
-
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2
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4
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4
2
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-
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-
2
2
-
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-
-
2
-
3
-
-
2
2
-
-
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-
4
-
-
-
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4
2
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1
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1
2
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4
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4
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1
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1
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1
1
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-
1
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-
3
4
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-
1
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4
1
-
-
-
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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1
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1
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1
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9
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9
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1
2
2
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2
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4
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1
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2
2
1
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1
1
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1
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2
2
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1
-
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2
2
1
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1
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1
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1
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4
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2
1
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1
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1
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2
1
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667083
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62
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-
1
1
-
-
-
-
-
-
1
-
-
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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1
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1
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1
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667048
Biswal
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Acta Crystallogr. Sect. D
61
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2005
-
-
1
1
-
-
-
-
-
-
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-
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5
-
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1
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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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-
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-
667050
Safo
Structure of Escherichia coli ...
Escherichia coli
Acta Crystallogr. Sect. D
61
599-604
2005
-
-
-
1
-
-
-
-
-
-
-
2
-
3
-
-
1
2
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
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2
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1
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2
-
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668875
Mills
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Mus musculus
Hum. Mol. Genet.
14
1077-1086
2005
-
-
1
-
3
-
-
-
-
-
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3
-
4
-
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3
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1
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1
1
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3
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3
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3
-
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-
655483
Kang
Genomic organization, tissue d ...
Homo sapiens
Eur. J. Biochem.
271
2452-2461
2004
-
-
1
-
2
-
1
4
-
-
-
-
-
3
-
-
-
-
-
61
-
-
2
-
-
-
-
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2
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1
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2
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1
2
4
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-
61
-
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2
-
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-
-
-
654870
di Salvo
Structure and mechanism of Esc ...
Escherichia coli
Biochim. Biophys. Acta
1647
76-82
2003
-
-
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1
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3
4
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2
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2
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4
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2
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1
2
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1
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2
4
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2
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4
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2
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-
-
657296
Musayev
Structure and properties of re ...
Homo sapiens
Protein Sci.
12
1455-1463
2003
-
-
-
1
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1
2
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2
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4
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1
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4
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2
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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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4
-
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-
2
-
-
-
-
-
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-
-
-
391906
Di Salvo
Active site structure and ster ...
Escherichia coli
J. Mol. Biol.
315
385-397
2002
-
-
1
1
8
-
-
7
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2
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1
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1
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7
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1
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1
8
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7
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1
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7
-
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-
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391905
Di Salvo
Expression, purification, and ...
Escherichia coli
Protein Expr. Purif.
13
349-356
1998
-
-
1
-
-
-
-
1
-
-
2
-
-
2
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1
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1
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1
1
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2
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1
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1
1
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1
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2
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1
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-
1
-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
391902
Loubbardi
Sterol uptake induced by an im ...
Saccharomyces cerevisiae
J. Bacteriol.
177
1817-1823
1995
-
-
1
-
-
-
-
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1
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4
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2
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1
1
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1
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1
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2
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391903
Zhao
Kinetic limitation and cellula ...
Escherichia coli
J. Bacteriol.
177
883-891
1995
-
-
1
-
-
-
2
2
-
-
2
-
-
3
-
-
1
-
-
-
1
2
1
1
1
-
1
2
2
2
-
-
2
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-
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-
1
-
-
-
-
-
2
2
2
-
-
2
-
-
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-
1
-
-
1
2
1
1
1
-
1
2
2
2
-
-
-
-
-
-
-
-
391904
Notheis
Purification and characterizat ...
Escherichia coli
Biochim. Biophys. Acta
1247
265-271
1995
-
-
1
-
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-
1
2
-
-
1
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2
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-
-
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1
1
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2
1
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1
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1
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1
1
2
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-
1
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-
-
-
-
-
1
1
-
-
-
2
1
-
-
-
-
-
-
-
-
-
391867
Miyata
-
Effects of culture medium on p ...
Triticum aestivum
Agric. Biol. Chem.
52
343-348
1988
-
-
-
-
-
-
-
-
-
2
-
2
-
1
-
-
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-
-
2
7
-
3
-
1
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-
1
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-
1
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-
1
-
-
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2
-
2
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-
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-
-
2
7
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
391868
Merrill
Highly sensitive methods for a ...
Homo sapiens, Oryctolagus cuniculus
Methods Enzymol.
122
110-115
1986
-
-
-
-
-
-
2
-
-
-
-
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2
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4
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2
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-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391869
Bowers-Komro
Modified purification of pyrid ...
Oryctolagus cuniculus
Methods Enzymol.
122
116-120
1986
-
-
-
-
-
-
-
-
-
-
-
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-
2
-
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1
-
-
2
1
1
1
-
-
-
-
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-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
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-
-
-
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1
-
2
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391871
Tsuge
Distribution of pyridoxamineph ...
Avena sativa, Brassica juncea, Brassica rapa, Daucus carota, Glebionis coronaria, Glycine max, Lactuca sativa, Medicago sativa, Oryza sativa, Raphanus sativus, Spinacia oleracea, Triticum aestivum, Vigna mungo, Vigna radiata var. radiata
Agric. Biol. Chem.
50
289-296
1986
-
-
-
-
-
-
-
-
-
-
-
14
-
14
-
-
-
-
-
29
14
-
28
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
14
-
-
-
-
-
29
14
-
28
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391872
Bowers-Komro
Pyridoxamine-5-phosphate oxida ...
Oryctolagus cuniculus
J. Biol. Chem.
260
9580-9582
1985
-
-
-
-
-
-
-
-
-
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1
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1
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-
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1
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-
-
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-
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-
-
-
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-
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-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391873
Takeuchi
Effect of tryptophan metabolit ...
Rattus norvegicus
Biochem. J.
227
537-544
1985
6
-
-
-
-
-
2
2
-
-
-
-
-
1
-
-
1
-
-
1
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
1
-
1
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391874
Tsuge
Immobilization of yeast pyrido ...
Saccharomyces cerevisiae
Biotechnol. Bioeng.
26
412-418
1984
-
1
-
-
-
1
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
2
-
2
1
2
2
3
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
2
1
2
2
3
-
-
-
-
-
-
-
-
-
391875
Churchich
Brain pyridoxine-5-phosphate o ...
Sus scrofa
Eur. J. Biochem.
138
327-332
1984
-
-
-
-
-
-
2
8
-
-
2
-
-
1
-
-
1
-
-
1
1
-
10
1
-
-
-
9
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
8
-
-
2
-
-
-
-
1
-
1
1
-
10
1
-
-
-
9
-
-
-
-
-
-
-
-
-
-
391876
Pflug
Occurrence of pydixaminephosph ...
Agrobacterium tumefaciens, Chloridazon-degrading bacterium, Deinococcus radiodurans, Escherichia coli, Flavobacterium sp., Flavobacterium sp. CB6, no activity in Arthrobacter globiformis, no activity in Arthrobacter sp., no activity in Arthrobacter sp. SuC 3, no activity in Bacillus cereus, no activity in Bacillus circulans, no activity in Bacillus pasteurii, no activity in Bacillus polymyxa, no activity in Bacillus subtilis, no activity in Micrococcus luteus, no activity in Nocardia sp., no activity in Nocardia sp. CBS 2, Proteus mirabilis, Pseudomonas chlororaphis subsp. aureofaciens, Pseudomonas fluorescens, Pseudomonas putida, Pseudomonas sp., Pseudomonas sp. CBS 4, Rhodospirillum rubrum, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Xanthomonas sp.
Hoppe-Seyler's Z. Physiol. Chem.
364
1627-1630
1983
-
-
-
-
-
-
-
-
-
-
-
-
-
29
-
-
-
-
-
-
14
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
14
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391877
Nutter
Absence of pyridoxine- (pyrido ...
Rattus norvegicus
Biochemistry
22
1599-1604
1983
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391878
Choi
Kinetic properties of pyridoxa ...
Oryctolagus cuniculus
J. Biol. Chem.
258
840-845
1983
-
-
-
-
-
-
2
4
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
1
4
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
391879
Langham
A radiometric assay of pyridox ...
Rattus norvegicus
Anal. Biochem.
125
329-334
1982
-
1
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
9
1
-
3
-
1
-
-
-
1
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
9
1
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
391881
Tsuge
Partial purification and prope ...
Triticum aestivum
Arch. Biochem. Biophys.
217
479-484
1982
1
-
-
-
-
-
5
3
-
-
-
-
-
1
-
-
1
-
-
1
4
-
4
-
2
1
-
-
1
-
1
1
-
1
-
1
-
-
1
-
-
-
-
5
-
3
-
-
-
-
-
-
-
1
-
1
4
-
4
-
2
1
-
-
1
-
1
1
-
-
-
-
-
-
391896
Tsuge
Separation and characterizatio ...
Saccharomyces cerevisiae
Agric. Biol. Chem.
46
1075-1077
1982
-
-
-
-
-
-
-
3
-
-
-
2
-
1
-
-
1
-
-
-
2
-
6
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
3
-
-
-
2
-
-
-
1
-
-
2
-
6
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
391870
Choi
Roles of arginyl residues in p ...
Oryctolagus cuniculus
Biochemistry
20
5722-5728
1981
-
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391897
Tsuge
Induction of plant pyridoxine ...
Triticum aestivum
Agric. Biol. Chem.
45
1725-1726
1981
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
2
1
-
1
-
1
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
1
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
391882
Gregory III
Effects of epsilon-pyridoxylly ...
Oryctolagus cuniculus
J. Biol. Chem.
255
2355-2359
1980
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391883
DePecol
Syntheses, properties, and use ...
Oryctolagus cuniculus
Anal. Biochem.
101
435-441
1980
-
-
-
-
-
-
-
1
1
-
-
2
-
1
-
-
-
-
-
1
-
-
9
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
2
-
-
-
-
-
1
-
-
9
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
391893
Clements
Glutathione reductase activity ...
Homo sapiens
Biochim. Biophys. Acta
632
159-163
1980
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391894
Clements
Pyridoxine (pyridoxamine) phos ...
Homo sapiens
Biochim. Biophys. Acta
613
401-409
1980
-
-
-
-
-
-
-
1
-
-
-
1
-
2
-
-
-
-
-
1
1
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
1
1
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
391898
Cash
Rapid purification by affinity ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
96
1755-1760
1980
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
2
2
-
3
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
2
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
391899
Tsuge
Molecular and enzymatic proper ...
Saccharomyces cerevisiae
Agric. Biol. Chem.
44
2329-2335
1980
-
-
-
-
-
-
-
1
-
-
3
-
-
1
-
-
1
-
-
-
2
-
1
1
-
-
-
-
-
-
-
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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-
2
-
1
1
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-
391901
Merrill
Spectroscopic studies of compl ...
Oryctolagus cuniculus
Biochim. Biophys. Acta
626
57-63
1980
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-
-
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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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1
1
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1
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-
1
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-
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391884
Horiike
Evidence for an essential hist ...
Oryctolagus cuniculus
J. Biol. Chem.
254
6638-6643
1979
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-
-
-
-
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2
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2
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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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-
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-
-
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-
391885
Horiike
Activation and inactivation of ...
Oryctolagus cuniculus
Arch. Biochem. Biophys.
195
325-335
1979
3
-
-
-
-
-
3
6
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1
1
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2
-
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1
-
1
2
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3
1
1
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-
-
1
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1
4
-
-
3
-
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1
-
-
-
-
3
4
6
-
1
1
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-
-
-
1
1
2
-
-
3
1
1
-
-
-
1
-
-
-
-
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-
-
-
-
391895
Merrill
Pyridoxamine (pyridoxine) 5-ph ...
Oryctolagus cuniculus
Methods Enzymol.
62
568-574
1979
-
-
-
-
-
2
4
-
-
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1
1
-
2
-
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1
-
-
1
1
1
3
1
-
-
-
-
-
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-
2
3
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-
2
-
-
2
-
4
3
-
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1
1
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1
-
1
1
1
3
1
-
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-
391900
Tsuge
Purification and properties of ...
Saccharomyces cerevisiae
Agric. Biol. Chem.
43
1801-1807
1979
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-
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-
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6
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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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1
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1
-
2
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6
-
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1
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-
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1
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1
-
1
-
1
-
1
-
2
-
-
-
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-
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-
391886
Tsuge
Immobilization of yeast pyrido ...
Saccharomyces cerevisiae
FEBS Lett.
93
331-334
1978
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-
-
-
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4
-
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2
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1
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2
1
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2
2
1
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3
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4
-
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1
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2
1
-
2
2
1
-
3
-
-
-
-
-
-
-
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-
391887
Merrill
Evidence for the regulation of ...
Oryctolagus cuniculus, Rattus norvegicus
Biochem. Biophys. Res. Commun.
83
984-990
1978
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-
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-
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2
11
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2
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2
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1
-
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2
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5
-
1
-
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-
1
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-
1
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-
-
-
-
-
-
-
-
-
2
1
11
-
-
-
2
-
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1
-
2
-
-
5
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
391892
Tsuge
-
Evidence for a pyridoxine (pyr ...
Triticum aestivum
FEBS Lett.
88
205-207
1978
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-
-
-
-
-
-
-
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1
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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
1
-
1
-
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-
-
-
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-
-
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-
-
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-
391891
Kazarinoff
Rabbit liver pyridoxamine (pyr ...
Oryctolagus cuniculus
J. Biol. Chem.
250
3436-3442
1975
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1
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27
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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
9
1
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2
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-
-
-
-
2
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-
1
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-
27
-
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2
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1
-
2
-
1
9
1
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-
-
-
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-
-
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391888
Guerrieri
Intracellular localization of ...
Oryctolagus cuniculus
FEBS Lett.
41
11-13
1974
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-
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2
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2
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2
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1
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2
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2
-
-
1
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-
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391889
Kazarinoff
Specificity of pyridoxine (pyr ...
Oryctolagus cuniculus
Biochim. Biophys. Acta
359
282-287
1974
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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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-
-
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-
-
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391890
Kazarinoff
N-(5-phospho-4-pyridoxyl)amine ...
Oryctolagus cuniculus
Biochem. Biophys. Res. Commun.
52
440-446
1973
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-
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1
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1
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1
2
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1
2
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20
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1
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1
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1
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1
2
-
20
-
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-
-
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1
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-
-
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391880
Wada
The enzymatic oxidation of pyr ...
Oryctolagus cuniculus
J. Biol. Chem.
236
2089-2095
1961
5
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7
3
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1
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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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2
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5
-
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2
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7
-
3
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-
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-
1
-
1
1
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1
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1
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-