BRENDA - Enzyme Database
show all sequences of 1.4.3.1

Possible role of a histidine residue in the substrate specificity of yeast D-aspartate oxidase

Takahashi, S.; Shimada, K.; Nozawa, S.; Goto, M.; Abe, K.; Kera, Y.; J. Biochem. 159, 371-378 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Vanrija humicola
Engineering
Amino acid exchange
Commentary
Organism
H56A
the mutant exhibits no significant activity toward acidic D-amino acids; the mutant gains the ability to utilize neutral D-amino acids as substrates, such as D-methionine, D-phenylalanine and D-glutamine
Vanrija humicola
H56D
the mutant exhibits no significant activity toward acidic D-amino acids
Vanrija humicola
H56F
the mutant exhibits no significant activity toward acidic D-amino acids
Vanrija humicola
H56K
the mutant exhibits no significant activity toward acidic D-amino acids
Vanrija humicola
H56N
the mutant exhibits no significant activity toward acidic D-amino acids; the mutant gains the ability to utilize neutral D-amino acids as substrates, such as D-methionine, D-phenylalanine and D-glutamine
Vanrija humicola
Inhibitors
Inhibitors
Commentary
Organism
Structure
D-malate
87.8% residual activity at 10 mM
Vanrija humicola
malonate
62.1% residual activity at 10 mM
Vanrija humicola
additional information
not inhibited by 10 mM meso-tartrate, benzoate, anthranilate, and crotonate
Vanrija humicola
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.5
-
D-Asp
wild type enzyme, at pH 7.5 and 37°C
Vanrija humicola
8.5
-
D-Met
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
8.8
-
D-Leu
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
14.3
-
D-Phe
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
21
-
D-Gln
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
31.8
-
D-Met
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
34.8
-
D-Phe
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
39.4
-
D-Gln
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
83.4
-
D-Asn
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
106
-
D-Glu
wild type enzyme, at pH 7.5 and 37°C
Vanrija humicola
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-Asp + H2O + O2
Vanrija humicola
the enzyme shows high activity only with D-aspartate
oxaloacetate + NH3 + H2O2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Vanrija humicola
Q75WF1
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-Asn + H2O + O2
substrate for mutant enzyme H56N
742805
Vanrija humicola
? + NH3 + H2O2
-
-
-
?
D-Asn + H2O + O2
low activity
742805
Vanrija humicola
oxaloacetate + NH3 + H2O2
-
-
-
?
D-Asp + H2O + O2
the enzyme shows high activity only with D-aspartate
742805
Vanrija humicola
oxaloacetate + NH3 + H2O2
-
-
-
?
D-Gln + H2O + O2
substrate for mutant enzymes H56A and H56N
742805
Vanrija humicola
? + NH3 + H2O2
-
-
-
?
D-Glu + H2O + O2
low activity
742805
Vanrija humicola
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-Leu + H2O + O2
substrate for mutant enzyme H56N
742805
Vanrija humicola
? + NH3 + H2O2
-
-
-
?
D-Met + H2O + O2
substrate for mutant enzymes H56A and H56N
742805
Vanrija humicola
4-(methylsulfonyl)-2-oxobutanoate + NH3 + H2O2
-
-
-
?
D-Phe + H2O + O2
substrate for mutant enzymes H56A and H56N
742805
Vanrija humicola
? + NH3 + H2O2
-
-
-
?
additional information
no activity with D-Ala, D-Ser, D-Pro, D-Val, D-Thr, D-Ile, D-Leu, D-Gln, D-Met, D-Phe, D-Tyr, D-Trp, D-Lys, D-His, D-Arg, and Gly
742805
Vanrija humicola
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 40000, SDS-PAGE
Vanrija humicola
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.7
-
D-Leu
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
2.2
-
D-Gln
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
2.6
-
D-Glu
wild type enzyme, at pH 7.5 and 37°C
Vanrija humicola
3.1
-
D-Phe
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
3.9
-
D-Asn
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
4
-
D-Met
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
4.1
-
D-Phe
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
4.5
-
D-Gln
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
11.5
-
D-Met
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
74.5
-
D-Asp
wild type enzyme, at pH 7.5 and 37°C
Vanrija humicola
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Vanrija humicola
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H56A
the mutant exhibits no significant activity toward acidic D-amino acids; the mutant gains the ability to utilize neutral D-amino acids as substrates, such as D-methionine, D-phenylalanine and D-glutamine
Vanrija humicola
H56D
the mutant exhibits no significant activity toward acidic D-amino acids
Vanrija humicola
H56F
the mutant exhibits no significant activity toward acidic D-amino acids
Vanrija humicola
H56K
the mutant exhibits no significant activity toward acidic D-amino acids
Vanrija humicola
H56N
the mutant exhibits no significant activity toward acidic D-amino acids; the mutant gains the ability to utilize neutral D-amino acids as substrates, such as D-methionine, D-phenylalanine and D-glutamine
Vanrija humicola
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
D-malate
87.8% residual activity at 10 mM
Vanrija humicola
malonate
62.1% residual activity at 10 mM
Vanrija humicola
additional information
not inhibited by 10 mM meso-tartrate, benzoate, anthranilate, and crotonate
Vanrija humicola
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.5
-
D-Asp
wild type enzyme, at pH 7.5 and 37°C
Vanrija humicola
8.5
-
D-Met
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
8.8
-
D-Leu
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
14.3
-
D-Phe
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
21
-
D-Gln
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
31.8
-
D-Met
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
34.8
-
D-Phe
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
39.4
-
D-Gln
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
83.4
-
D-Asn
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
106
-
D-Glu
wild type enzyme, at pH 7.5 and 37°C
Vanrija humicola
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-Asp + H2O + O2
Vanrija humicola
the enzyme shows high activity only with D-aspartate
oxaloacetate + NH3 + H2O2
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-Asn + H2O + O2
substrate for mutant enzyme H56N
742805
Vanrija humicola
? + NH3 + H2O2
-
-
-
?
D-Asn + H2O + O2
low activity
742805
Vanrija humicola
oxaloacetate + NH3 + H2O2
-
-
-
?
D-Asp + H2O + O2
the enzyme shows high activity only with D-aspartate
742805
Vanrija humicola
oxaloacetate + NH3 + H2O2
-
-
-
?
D-Gln + H2O + O2
substrate for mutant enzymes H56A and H56N
742805
Vanrija humicola
? + NH3 + H2O2
-
-
-
?
D-Glu + H2O + O2
low activity
742805
Vanrija humicola
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-Leu + H2O + O2
substrate for mutant enzyme H56N
742805
Vanrija humicola
? + NH3 + H2O2
-
-
-
?
D-Met + H2O + O2
substrate for mutant enzymes H56A and H56N
742805
Vanrija humicola
4-(methylsulfonyl)-2-oxobutanoate + NH3 + H2O2
-
-
-
?
D-Phe + H2O + O2
substrate for mutant enzymes H56A and H56N
742805
Vanrija humicola
? + NH3 + H2O2
-
-
-
?
additional information
no activity with D-Ala, D-Ser, D-Pro, D-Val, D-Thr, D-Ile, D-Leu, D-Gln, D-Met, D-Phe, D-Tyr, D-Trp, D-Lys, D-His, D-Arg, and Gly
742805
Vanrija humicola
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 40000, SDS-PAGE
Vanrija humicola
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.7
-
D-Leu
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
2.2
-
D-Gln
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
2.6
-
D-Glu
wild type enzyme, at pH 7.5 and 37°C
Vanrija humicola
3.1
-
D-Phe
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
3.9
-
D-Asn
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
4
-
D-Met
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
4.1
-
D-Phe
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
4.5
-
D-Gln
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
11.5
-
D-Met
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
74.5
-
D-Asp
wild type enzyme, at pH 7.5 and 37°C
Vanrija humicola
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.024
-
D-Glu
wild type enzyme, at pH 7.5 and 37°C
Vanrija humicola
0.047
-
D-Asn
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
0.055
-
D-Gln
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
0.074
-
D-Leu
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
0.119
-
D-Phe
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
0.125
-
D-Met
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
0.213
-
D-Gln
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
0.218
-
D-Phe
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
1.35
-
D-Met
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
29.8
-
D-Asp
wild type enzyme, at pH 7.5 and 37°C
Vanrija humicola
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.024
-
D-Glu
wild type enzyme, at pH 7.5 and 37°C
Vanrija humicola
0.047
-
D-Asn
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
0.055
-
D-Gln
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
0.074
-
D-Leu
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
0.119
-
D-Phe
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
0.125
-
D-Met
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
0.213
-
D-Gln
mutant enzyme H56N, at pH 7.5 and 37°C
Vanrija humicola
0.218
-
D-Phe
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
1.35
-
D-Met
mutant enzyme H56A, at pH 7.5 and 37°C
Vanrija humicola
29.8
-
D-Asp
wild type enzyme, at pH 7.5 and 37°C
Vanrija humicola
Other publictions for EC 1.4.3.1
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)
742426
Florio
Tracking the evolution of epi ...
Mus musculus
Epigenetics
12
41-54
2017
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
6
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
6
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
743836
Sacchi
Olanzapine, but not clozapine ...
Homo sapiens, Mus musculus
Sci. Rep.
7
46288
2017
-
-
-
-
-
-
4
-
-
-
-
2
-
6
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
2
4
-
-
-
-
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
742805
Takahashi
Possible role of a histidine ...
Vanrija humicola
J. Biochem.
159
371-378
2016
-
-
1
-
5
-
3
10
-
-
-
1
-
3
-
-
-
-
-
-
-
-
9
1
-
-
-
10
-
-
-
-
-
-
-
-
-
1
-
-
5
-
-
3
-
10
-
-
-
1
-
-
-
-
-
-
-
-
9
1
-
-
-
10
-
-
-
-
-
-
-
-
10
10
743133
Punzo
Age-related changes in D-aspa ...
Mus musculus
J. Neurosci.
36
3064-3078
2016
-
-
-
-
-
-
-
-
-
-
-
1
-
5
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
742035
Katane
Characterization of the enzym ...
Homo sapiens, Mus musculus, Rattus norvegicus
Biol. Pharm. Bull.
38
298-305
2015
-
-
3
-
-
-
15
3
-
1
-
3
-
9
-
-
3
-
-
1
12
-
19
-
1
-
1
3
-
1
1
3
9
-
-
-
-
3
3
-
-
-
-
15
9
3
-
1
-
3
-
-
-
3
-
1
12
-
19
-
1
-
1
3
-
1
1
-
-
-
-
-
3
3
743063
Katane
Identification of novel D-asp ...
Homo sapiens
J. Med. Chem.
58
7328-7340
2015
-
-
1
-
-
-
37
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
33
-
-
1
-
-
-
-
33
37
3
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
743140
Han
Changes in D-aspartic acid an ...
Mus musculus
J. Pharm. Biomed. Anal.
116
47-52
2015
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
7
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
7
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
743350
Cristino
D-aspartate oxidase influence ...
Mus musculus
Neurobiol. Aging
36
1890-1902
2015
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
741688
Takahashi
A highly stable d-amino acid ...
no activity in Rubrobacter xylanophilus
Appl. Environ. Microbiol.
80
7219-7229
2014
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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723870
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1
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1
1
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724597
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Enzymatic assay for D-aspartic ...
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725959
Saitoh
Spatiotemporal localization of ...
Caenorhabditis elegans, Caenorhabditis elegans N2
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1
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3
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6
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6
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1
3
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711325
Katane
Thiolactomycin inhibits D-aspa ...
Homo sapiens, Mus musculus
Biochimie
92
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2010
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1
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1
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6
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6
4
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4
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1
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711718
Katane
Comparative characterization o ...
Caenorhabditis elegans
Chem. Biodivers.
7
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2010
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1
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10
3
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3
3
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4
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1
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9
1
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1
1
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10
3
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3
3
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4
1
1
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9
1
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1
1
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9
9
711719
Katane
D-aspartate oxidase: The sole ...
Bos taurus, Caenorhabditis elegans, Homo sapiens, Mus musculus, Ovis aries, Rattus norvegicus, Sus scrofa, Vanrija humicola
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2010
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5
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24
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5
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40
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28
8
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8
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2
5
8
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4
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24
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17
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40
-
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28
8
-
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4
4
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711721
Burrone
Effects of D-aspartate treatme ...
Pelophylax esculentus
Chem. Biodivers.
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2010
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-
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5
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1
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1
2
2
1
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-
711722
Topo
Thyroid hormones and D-asparti ...
Mus musculus, Rattus norvegicus
Chem. Biodivers.
7
1467-1478
2010
-
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2
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5
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2
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2
2
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712616
di Giovanni
Distribution of free D-asparti ...
Pelophylax esculentus
J. Exp. Zool.
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137-143
2010
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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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D-aspartate oxidase localisati ...
Sus scrofa
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2010
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7
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1
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1
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1
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712787
Takahashi
-
An active-site mutation enhanc ...
Vanrija humicola
J. Mol. Catal. B
61
235-240
2009
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1
1
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5
1
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1
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5
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11
-
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1
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1
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15
-
5
1
1
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5
1
-
-
-
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7
7
684387
Katane
Hyperactive mutants of mouse D ...
Mus musculus
Amino Acids
35
75-82
2008
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1
-
3
-
-
12
-
-
-
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-
3
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1
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1
12
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2
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1
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1
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1
12
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2
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686597
Huang
D-Aspartate and D-aspartate ox ...
Mus musculus
Exp. Eye Res.
86
704-709
2008
-
-
-
-
-
-
-
-
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4
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2
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1
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2
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1
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-
-
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-
-
-
-
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-
-
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673583
Katane
Caenorhabditis elegans has two ...
Caenorhabditis elegans
FEBS J.
274
137-149
2007
-
-
1
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-
10
-
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4
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3
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1
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17
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10
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1
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1
1
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10
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4
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1
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-
17
-
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-
10
-
-
-
-
-
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-
-
684383
Katane
Molecular cloning of a cDNA en ...
Mus musculus
Amino Acids
32
69-78
2007
-
-
1
-
7
-
3
-
-
-
1
-
-
3
-
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-
2
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7
-
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2
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1
2
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7
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3
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1
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2
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7
-
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Yamamoto
Functional and structural char ...
Sus scrofa
J. Biochem.
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363-376
2007
2
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1
-
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2
3
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4
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3
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1
-
-
2
2
-
3
1
-
-
-
3
1
-
1
1
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-
2
-
1
1
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-
2
-
3
-
-
4
-
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1
-
2
2
-
3
1
-
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-
3
1
-
1
-
-
-
-
-
-
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677271
Takahashi
Physiological role of D-aspart ...
Vanrija humicola
Yeast
22
1203-1212
2005
-
-
-
-
-
-
-
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1
-
3
-
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1
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1
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-
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655928
Takahashi
Cloning and expression in Esch ...
Vanrija humicola
J. Biochem.
135
533-540
2004
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1
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2
3
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3
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6
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1
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1
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3
1
1
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2
3
1
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1
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2
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3
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3
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1
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1
-
3
1
1
-
2
3
1
-
-
-
-
-
-
-
-
-
657350
Sarower
-
Distribution and substrate spe ...
Meretrix lusoria, Mizuhopecten yessoensis, Mytilus galloprovincialis, Octopus vulgaris, Penaeus japonicus, Procambarus clarkii, Todarodes pacificus, Turbo cornutus
Science Asia
30
335-340
2004
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-
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-
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8
-
8
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14
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16
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-
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-
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8
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-
-
14
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656415
Sarower
Distribution and characteristi ...
Chaunax fimbriatus, Cololabis saira, Cyprinus carpio, Dentex tumifrons, Lateolabrax japonicus, Oncorhynchus keta, Oncorhynchus masou, Oncorhynchus mykiss, Pagrus major, Paralichthys olivaceus, Plecoglossus altivelis, Pseudopleuronectes yokohamae, Sardinops melanostictus, Scomber japonicus, Thamnaconus tessellatus, Trachurus japonicus, Verasper variegatus
J. Exp. Zool. A
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151-159
2003
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-
-
-
-
1
1
17
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-
17
-
23
-
-
-
-
-
38
-
-
25
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
17
-
-
17
-
-
-
-
-
38
-
-
25
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
391705
Sacchi
Engineering the substrate spec ...
Bos taurus
J. Biol. Chem.
277
27510-27516
2002
-
-
-
-
-
-
1
4
-
-
-
1
-
3
-
-
-
-
-
1
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
-
-
1
-
-
-
-
-
1
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391706
Zaar
Cellular and subcellular distr ...
Bos taurus, Homo sapiens, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
J. Comp. Neurol.
450
272-282
2002
-
-
-
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3
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166
-
-
-
-
-
5
-
-
16
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
3
-
-
4
-
-
-
-
-
5
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391707
Negri
Purification of beef kidney D- ...
Bos taurus
Biochim. Biophys. Acta
1431
212-222
1999
-
-
1
-
-
-
1
10
-
-
3
1
-
3
-
-
1
-
-
3
1
-
11
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
10
-
-
3
1
-
-
-
1
-
3
1
-
11
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391708
Tedeschi
D-Aspartate oxidase is present ...
Bos taurus, Xenopus laevis
Comp. Biochem. Physiol. B
124
489-494
1999
-
-
-
-
-
-
2
-
-
-
1
2
-
7
-
-
2
-
-
6
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
1
2
-
-
-
2
-
6
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391709
Amery
C-terminal tripeptide Ser-Asn- ...
Homo sapiens
Biochem. J.
336
367-371
1998
-
1
1
-
-
-
-
-
1
-
-
1
-
3
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-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
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-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391710
Kera
-
D-Aspartate oxidase and free a ...
Carassius auratus langsdorfii, Cyprinus carpio, Oncorhynchus mykiss, Pagrus major, Seriola quinqueradiata
Comp. Biochem. Physiol. B
119
95-100
1998
-
-
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7
-
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9
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11
11
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24
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-
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4
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-
-
-
-
-
4
-
-
-
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7
-
-
-
-
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9
-
-
-
-
-
11
11
-
24
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391711
Simonic
cDNA cloning and expression of ...
Bos taurus
Biochem. J.
322
729-735
1997
-
-
1
-
-
-
-
-
-
-
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1
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2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391712
Setoyama
Structural and functional char ...
Homo sapiens
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798-803
1997
-
-
1
-
-
-
-
2
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1
1
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1
-
-
2
-
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4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
2
-
-
1
1
-
-
-
1
-
2
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391713
Yamada
Purification and properties of ...
Vanrija humicola, Vanrija humicola UJ1
Biochim. Biophys. Acta
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153-158
1996
-
-
-
-
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3
3
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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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8
1
1
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-
-
1
-
-
1
3
-
-
-
-
-
1
-
-
-
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3
3
3
-
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1
2
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1
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1
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8
1
1
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-
1
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391714
Tedeschi
Properties of the flavoenzyme ...
Octopus vulgaris
Biochim. Biophys. Acta
1207
217-222
1994
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6
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1
1
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5
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7
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7
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1
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391715
Wakayama
-
Isolation, enzyme production a ...
Fusarium sacchari
J. Ferment. Bioeng.
78
377-379
1994
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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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4
-
1
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1
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1
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1
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-
391716
D'Aniello
Biological role of D-amino aci ...
Mus musculus, Octopus vulgaris, Rattus norvegicus
J. Biol. Chem.
268
26941-26949
1993
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3
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5
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6
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6
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3
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3
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6
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6
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391717
D'Aniello
Further study on the specifici ...
Bos taurus, Octopus vulgaris
Comp. Biochem. Physiol. B
105
731-734
1993
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-
-
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14
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2
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4
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2
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13
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2
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2
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14
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2
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2
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13
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391718
Tedeschi
Chemical modification of funct ...
Bos taurus
Eur. J. Biochem.
205
127-132
1992
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1
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2
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2
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3
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391719
Negri
-
Structural studies of beef kid ...
Bos taurus
Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York
179-187
1990
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2
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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5
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1
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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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1
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5
-
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1
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391720
Tedeschi
-
Modification of substrate spec ...
Bos taurus
Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York
189-192
1990
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1
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1
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1
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1
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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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6
-
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391721
Negri
The kinetic mechanism of beef ...
Bos taurus
J. Biol. Chem.
263
13557-13563
1988
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-
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2
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1
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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1
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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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2
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391722
Negri
D-Aspartate oxidase from beef ...
Bos taurus
J. Biol. Chem.
262
10026-10034
1987
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-
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1
1
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2
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3
1
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1
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3
1
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2
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391723
Burns
Thiazolidine-2-carboxylate der ...
Bos taurus
Biochem. Biophys. Res. Commun.
125
1039-1045
1984
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-
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4
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1
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2
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2
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4
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4
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2
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4
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391724
Nasu
The mammalian enzyme which rep ...
Bos taurus
Biochim. Biophys. Acta
704
240-252
1982
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1
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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
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1
1
-
2
-
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-
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-
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-
391725
Rinaldi
Oxidation of meso-diaminosucci ...
Bos taurus
Eur. J. Biochem.
117
635-638
1981
-
-
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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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2
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3
-
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391726
Jaroszewicz
D-Asparatate oxidase in the th ...
Sus scrofa
Enzyme
20
80-89
1975
-
-
-
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1
-
1
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1
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2
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2
1
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2
1
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3
-
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1
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391727
Dixon
D-aspartate oxidase of kidney ...
Oryctolagus cuniculus
Biochim. Biophys. Acta
146
54-76
1967
-
-
-
-
-
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15
4
-
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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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3
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2
1
1
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2
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15
2
4
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1
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1
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1
1
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3
-
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2
1
1
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391728
Still
-
On the prosthetic group of the ...
Oryctolagus cuniculus, Ovis aries, Sus scrofa
J. Biol. Chem.
182
585-589
1950
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1
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3
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3
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2
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6
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2
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2
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6
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