BRENDA - Enzyme Database show
show all sequences of 1.4.3.16

A thermostable L-aspartate oxidase: a new tool for biotechnological applications

Bifulco, D.; Pollegioni, L.; Tessaro, D.; Servi, S.; Molla, G.; Appl. Microbiol. Biotechnol. 97, 7285-7295 (2013)

Data extracted from this reference:

Application
Application
Commentary
Organism
biotechnology
StLASPO represents an appropriate biocatalyst for the resolution of racemic solutions of D,L-aspartate and a well-suited protein scaffold to evolve a L-amino acid oxidase activity by protein engineering
Sulfurisphaera tokodaii
Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells; expression in Escherichia coli in the active form as holoenzyme
Sulfurisphaera tokodaii
Inhibitors
Inhibitors
Commentary
Organism
Structure
D-Aspartate
weak inhibition; weak inhibition
Sulfurisphaera tokodaii
oxaloacetate
weak inhibition; weak inhibition
Sulfurisphaera tokodaii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.33
-
O2
pH 8, 37C
Sulfurisphaera tokodaii
1.3
-
L-aspartate
apparent value, at pH 8.0 and 37C
Sulfurisphaera tokodaii
13.3
-
L-aspartate
pH 8, 37C
Sulfurisphaera tokodaii
18.1
-
L-asparagine
apparent value, at pH 8.0 and 37C
Sulfurisphaera tokodaii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
51000
-
gel filtration; gel filtration
Sulfurisphaera tokodaii
53647
-
1 * 53647, calculated from amino acid sequence
Sulfurisphaera tokodaii
536467
-
x * 536467, calculated from sequence
Sulfurisphaera tokodaii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-asparagine + H2O + O2
Sulfurisphaera tokodaii
-
4-amino-2,4-dioxobutanoate + NH3 + H2O2
-
-
?
L-aspartate + H2O + O2
Sulfurisphaera tokodaii
the enzyme oxidizes L-aspartate to iminosuccinate, which is then non-enzymatically hydrolyzed to oxaloacetate
oxaloacetate + NH3 + H2O2
-
-
?
additional information
Sulfurisphaera tokodaii
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate. The enzyme shows no activity with L-phenylalanine, L-glutamate, glycine, L-proline, and L-alanine
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sulfurisphaera tokodaii
KC333624
synthetic construct
-
Sulfurisphaera tokodaii
Q972D2
-
-
Purification (Commentary)
Commentary
Organism
; HiTrap nickel chelating affinity column chromatography, and Superdex 200 gel filtration
Sulfurisphaera tokodaii
Storage Stability
Storage Stability
Organism
4, purified enzyme at pH 7.5, several months, nploss of activity
Sulfurisphaera tokodaii
4C, pH 7.5, in the dark, stable for months
Sulfurisphaera tokodaii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-asparagine + H2O + O2
-
721394
Sulfurisphaera tokodaii
4-amino-2,4-dioxobutanoate + NH3 + H2O2
-
-
-
?
L-asparagine + O2
Vmax/Km is 63fold lower compared to L-aspartate
721394
Sulfurisphaera tokodaii
4-amino-2-imino-4-oxobutanoate + H2O2
-
-
-
?
L-aspartate + H2O + O2
the enzyme oxidizes L-aspartate to iminosuccinate, which is then non-enzymatically hydrolyzed to oxaloacetate
721394
Sulfurisphaera tokodaii
oxaloacetate + NH3 + H2O2
-
-
-
?
L-aspartate + O2
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate
721394
Sulfurisphaera tokodaii
iminosuccinate + H2O2
-
-
-
?
additional information
the enzyme does not show activity on L-phenylalanine (50100 mM), L-glutamate (50100 mM), glycine (50100 mM), L-proline (50100 mM) and L-alanine (50100 mM)
721394
Sulfurisphaera tokodaii
?
-
-
-
-
additional information
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate. The enzyme shows no activity with L-phenylalanine, L-glutamate, glycine, L-proline, and L-alanine
721394
Sulfurisphaera tokodaii
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 536467, calculated from sequence
Sulfurisphaera tokodaii
monomer
1 * 53647, calculated from amino acid sequence
Sulfurisphaera tokodaii
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Sulfurisphaera tokodaii
60
80
-
Sulfurisphaera tokodaii
Temperature Range [C]
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
40
95
40C: about 50% of maximal activity, 95C: about 60% of maximal activity
Sulfurisphaera tokodaii
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
37
-
more than 70% of the initial activity is recovered after 60 min at 37C
Sulfurisphaera tokodaii
80
-
stable up to; the enzyme is fully stable up to 80C (400 min). When the temperature is increased to above 85C, a sharp decrease in enzyme stability is apparent and the activity is lost in about 100 min at 100C
Sulfurisphaera tokodaii
83
-
Tm-value determinedv by fluoresecence at 340 nm
Sulfurisphaera tokodaii
86
-
Tm-value determinedv by fluoresecence at 525 nm
Sulfurisphaera tokodaii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.05
-
L-aspartate
apparent value, at pH 8.0 and 37C; pH 8, 37C
Sulfurisphaera tokodaii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
10
-
;
Sulfurisphaera tokodaii
pH Range
pH Minimum
pH Maximum
Commentary
Organism
8.8
12
pH 8.8: about 50% of maximal activity, pH 12.0: about 70% of maximal activity
Sulfurisphaera tokodaii
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
7
10
60 min, stable; no significant change in activity is observed up to 400 min of incubation at pH 7.5. More than 70% of the initial activity is recovered after 60 min at 37C. Below pH 8.0 and above pH 10.0, a significant time-dependent inactivation is apparent
Sulfurisphaera tokodaii
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
contains 1 FAD per protein monomer; FAD-containing flavoprotein, tight binding of the FAD cofactor
Sulfurisphaera tokodaii
Application (protein specific)
Application
Commentary
Organism
biotechnology
StLASPO represents an appropriate biocatalyst for the resolution of racemic solutions of D,L-aspartate and a well-suited protein scaffold to evolve a L-amino acid oxidase activity by protein engineering
Sulfurisphaera tokodaii
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Sulfurisphaera tokodaii
expression in Escherichia coli in the active form as holoenzyme
Sulfurisphaera tokodaii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
FAD-containing flavoprotein, tight binding of the FAD cofactor
Sulfurisphaera tokodaii
FAD
contains 1 FAD per protein monomer
Sulfurisphaera tokodaii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
D-Aspartate
weak inhibition
Sulfurisphaera tokodaii
oxaloacetate
weak inhibition
Sulfurisphaera tokodaii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.33
-
O2
pH 8, 37C
Sulfurisphaera tokodaii
1.3
-
L-aspartate
apparent value, at pH 8.0 and 37C
Sulfurisphaera tokodaii
13.3
-
L-aspartate
pH 8, 37C
Sulfurisphaera tokodaii
18.1
-
L-asparagine
apparent value, at pH 8.0 and 37C
Sulfurisphaera tokodaii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
51000
-
gel filtration
Sulfurisphaera tokodaii
53647
-
1 * 53647, calculated from amino acid sequence
Sulfurisphaera tokodaii
536467
-
x * 536467, calculated from sequence
Sulfurisphaera tokodaii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-asparagine + H2O + O2
Sulfurisphaera tokodaii
-
4-amino-2,4-dioxobutanoate + NH3 + H2O2
-
-
?
L-aspartate + H2O + O2
Sulfurisphaera tokodaii
the enzyme oxidizes L-aspartate to iminosuccinate, which is then non-enzymatically hydrolyzed to oxaloacetate
oxaloacetate + NH3 + H2O2
-
-
?
additional information
Sulfurisphaera tokodaii
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate. The enzyme shows no activity with L-phenylalanine, L-glutamate, glycine, L-proline, and L-alanine
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Sulfurisphaera tokodaii
HiTrap nickel chelating affinity column chromatography, and Superdex 200 gel filtration
Sulfurisphaera tokodaii
Storage Stability (protein specific)
Storage Stability
Organism
4, purified enzyme at pH 7.5, several months, nploss of activity
Sulfurisphaera tokodaii
4C, pH 7.5, in the dark, stable for months
Sulfurisphaera tokodaii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-asparagine + H2O + O2
-
721394
Sulfurisphaera tokodaii
4-amino-2,4-dioxobutanoate + NH3 + H2O2
-
-
-
?
L-asparagine + O2
Vmax/Km is 63fold lower compared to L-aspartate
721394
Sulfurisphaera tokodaii
4-amino-2-imino-4-oxobutanoate + H2O2
-
-
-
?
L-aspartate + H2O + O2
the enzyme oxidizes L-aspartate to iminosuccinate, which is then non-enzymatically hydrolyzed to oxaloacetate
721394
Sulfurisphaera tokodaii
oxaloacetate + NH3 + H2O2
-
-
-
?
L-aspartate + O2
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate
721394
Sulfurisphaera tokodaii
iminosuccinate + H2O2
-
-
-
?
additional information
the enzyme does not show activity on L-phenylalanine (50100 mM), L-glutamate (50100 mM), glycine (50100 mM), L-proline (50100 mM) and L-alanine (50100 mM)
721394
Sulfurisphaera tokodaii
?
-
-
-
-
additional information
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate. The enzyme shows no activity with L-phenylalanine, L-glutamate, glycine, L-proline, and L-alanine
721394
Sulfurisphaera tokodaii
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 536467, calculated from sequence
Sulfurisphaera tokodaii
monomer
1 * 53647, calculated from amino acid sequence
Sulfurisphaera tokodaii
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Sulfurisphaera tokodaii
60
80
-
Sulfurisphaera tokodaii
Temperature Range [C] (protein specific)
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
40
95
40C: about 50% of maximal activity, 95C: about 60% of maximal activity
Sulfurisphaera tokodaii
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
37
-
more than 70% of the initial activity is recovered after 60 min at 37C
Sulfurisphaera tokodaii
80
-
stable up to
Sulfurisphaera tokodaii
80
-
the enzyme is fully stable up to 80C (400 min). When the temperature is increased to above 85C, a sharp decrease in enzyme stability is apparent and the activity is lost in about 100 min at 100C
Sulfurisphaera tokodaii
83
-
Tm-value determinedv by fluoresecence at 340 nm
Sulfurisphaera tokodaii
86
-
Tm-value determinedv by fluoresecence at 525 nm
Sulfurisphaera tokodaii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.05
-
L-aspartate
pH 8, 37C
Sulfurisphaera tokodaii
1.05
-
L-aspartate
apparent value, at pH 8.0 and 37C
Sulfurisphaera tokodaii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
10
-
-
Sulfurisphaera tokodaii
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
8.8
12
pH 8.8: about 50% of maximal activity, pH 12.0: about 70% of maximal activity
Sulfurisphaera tokodaii
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
7
10
60 min, stable
Sulfurisphaera tokodaii
7
10
no significant change in activity is observed up to 400 min of incubation at pH 7.5. More than 70% of the initial activity is recovered after 60 min at 37C. Below pH 8.0 and above pH 10.0, a significant time-dependent inactivation is apparent
Sulfurisphaera tokodaii
Other publictions for EC 1.4.3.16
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)
743783
Armenia
-
L-aspartate oxidase magnetic ...
Sulfurisphaera tokodaii
RSC Adv.
7
21136-21143
2017
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
1
-
1
-
-
-
-
-
1
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
742229
D'Arrigo
-
Immobilization of L-aspartate ...
Sulfurisphaera tokodaii
Catal. Sci. Technol.
5
1106-1114
2015
-
-
1
-
-
1
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
1
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
721394
Bifulco
A thermostable L-aspartate oxi ...
Sulfurisphaera tokodaii
Appl. Microbiol. Biotechnol.
97
7285-7295
2013
-
1
1
-
-
-
2
4
-
-
3
3
-
4
-
-
1
-
-
-
-
2
6
2
2
1
4
1
1
1
1
1
-
-
-
-
1
2
2
-
-
-
-
4
-
4
-
-
4
3
-
-
-
2
-
-
-
2
6
2
2
1
5
2
2
1
2
-
-
-
-
-
-
-
725741
Leese
-
Cloning, expression, character ...
Pseudomonas putida
J. Mol. Catal. B
85-86
17-22
2013
-
-
1
-
7
-
1
5
-
-
2
3
-
1
-
-
1
-
-
-
-
-
3
1
-
-
1
5
1
1
-
1
-
-
-
-
-
1
1
-
7
-
-
1
-
5
-
-
2
3
-
-
-
1
-
-
-
-
3
1
-
-
1
5
1
1
-
-
-
-
-
-
5
5
726225
Macho
Aspartate oxidase plays an imp ...
Arabidopsis thaliana
Plant Physiol.
159
1845-1856
2012
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
4
4
-
-
-
711324
Tedeschi
On the catalytic role of the a ...
Escherichia coli
Biochimie
92
1335-1342
2010
-
-
1
-
4
-
1
10
-
-
-
3
-
3
-
-
-
-
-
-
-
-
7
1
1
-
-
10
1
-
-
1
-
-
-
-
-
1
1
-
4
-
-
1
-
10
-
-
-
3
-
-
-
-
-
-
-
-
7
1
1
-
-
10
1
-
-
-
-
2
2
-
10
10
685396
Sakuraba
Structure of L-aspartate oxida ...
Sulfurisphaera tokodaii
Biochim. Biophys. Acta
1784
563-571
2008
-
-
1
1
-
-
-
1
-
-
3
-
-
4
-
-
1
-
-
-
1
-
1
1
-
-
1
-
1
-
1
1
-
-
-
-
-
1
1
1
-
-
-
-
-
1
-
-
3
-
-
-
-
1
-
-
1
-
1
1
-
-
1
-
1
-
1
-
-
-
-
-
-
-
686712
Marinoni
Characterization of L-aspartat ...
Bacillus subtilis
FEBS J.
275
5090-5107
2008
-
-
1
-
-
-
-
2
-
-
2
-
-
5
-
-
1
-
-
-
-
-
2
2
1
-
-
2
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
2
-
-
2
-
-
-
-
1
-
-
-
-
2
2
1
-
-
2
1
-
-
-
-
1
1
-
2
2
676612
Katoh
Early steps in the biosynthesi ...
Arabidopsis thaliana
Plant Physiol.
141
851-857
2006
-
1
1
-
1
-
-
-
1
-
-
-
-
5
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391763
Bossi
Structure of FAD-bound L-aspar ...
Escherichia coli
Biochemistry
41
3018-3024
2002
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391765
Sakuraba
L-Aspartate oxidase is present ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Extremophiles
6
275-281
2002
-
-
-
-
-
1
-
-
-
-
2
-
-
50
-
-
1
-
-
-
1
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
1
-
-
1
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
656090
Messner
Mechanism of superoxide and hy ...
Escherichia coli
J. Biol. Chem.
277
42563-42571
2002
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391762
Tedeschi
Probing the active site of L-a ...
Escherichia coli
Biochemistry
40
4738-4744
2001
-
-
-
-
5
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
5
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391761
Tedeschi
L-Aspartate oxidase from Esche ...
Escherichia coli
Eur. J. Biochem.
239
427-433
1996
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
1
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
391764
Mortarino
L-aspartate oxidase from Esche ...
Escherichia coli
Eur. J. Biochem.
239
418-426
1996
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391756
Seifert
Expression of the E. coli nadB ...
Escherichia coli
Biol. Chem. Hoppe-Seyler
371
239-248
1990
-
-
-
-
-
1
6
2
-
-
1
1
-
3
-
-
1
-
-
-
1
-
2
1
1
-
-
1
-
-
-
1
-
-
-
-
-
-
1
-
-
1
-
6
-
2
-
-
1
1
-
-
-
1
-
-
1
-
2
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
391757
Flachmann
Molecular biology of pyridine ...
Escherichia coli
Eur. J. Biochem.
175
221-229
1988
-
-
1
-
-
-
-
-
-
-
1
1
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
391759
Wilder
The L-aspartate oxidase report ...
Gossypium hirsutum
Biochem. Biophys. Res. Commun.
123
836-841
1984
1
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391758
Hosokawa
Higher plants contain L-aspara ...
Gossypium hirsutum
Biochem. Biophys. Res. Commun.
111
188-193
1983
-
-
-
-
-
-
1
1
-
-
1
-
-
4
-
-
1
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391760
Nasu
L-Aspartate oxidase, a newly d ...
Escherichia coli
J. Biol. Chem.
257
626-632
1982
1
-
-
-
-
-
1
-
-
-
-
1
-
2
-
-
1
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
1
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-