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EC Tree
IUBMB Comments Contains FAD. The enzyme from cyanobacteria can also act on other basic amino acids with lower activity. The enzyme from the bacterium Pseudomonas sp. TPU 7192 is highly specific.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
l-arginine oxidase,
more
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aoxA
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aroD
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L-arginine + H2O + O2 = 5-guanidino-2-oxopentanoate + NH3 + H2O2
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L-arginine:oxygen oxidoreductase (deaminating)
Contains FAD. The enzyme from cyanobacteria can also act on other basic amino acids with lower activity. The enzyme from the bacterium Pseudomonas sp. TPU 7192 is highly specific.
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
L-canavanine + H2O + O2
2-oxocanavanine + NH3 + H2O2
L-histidine + H2O + O2
2-oxohistidine + NH3 + H2O2
L-homoarginine + H2O + O2
2-oxohomoarginine + NH3 + H2O2
L-lysine + H2O + O2
2-oxolysine + NH3 + H2O2
L-ornithine + H2O + O2
2-oxoornithine + NH3 + H2O2
additional information
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enzyme catalyzes the oxidative deamination of the basic amino acids: L-arginine, L-lysine, L-ornithine and L-histidine. In the presence of catalase and of any of these amino acids, 0.5 mol O2 is consumed, and 1 mol ammonia is formed for each mol amino acid oxidized
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
HW613270
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the enzyme catalyzes the oxidative deamination of L-arginine and converts L-arginine to 2-ketoarginine, which is nonenzymatically converted into 4-guanidinobutyric acid when the hydrogen peroxide formed by L-arginine oxidation is not removed
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
HW613270
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the enzyme catalyzes the oxidative deamination of L-arginine and converts L-arginine to 2-ketoarginine, which is nonenzymatically converted into 4-guanidinobutyric acid when the hydrogen peroxide formed by L-arginine oxidation is not removed
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
wild-type L-glutamate oxidase enzyme shows strict substrate specificity for L-glutamate. The R305E mutant variant of L-glutamate oxidase exhibits strict specificity for L-arginine
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
Synechococcus cedorum
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
Synechococcus cedorum PCC 6908
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
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L-canavanine + H2O + O2
2-oxocanavanine + NH3 + H2O2
HW613270
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L-canavanine + H2O + O2
2-oxocanavanine + NH3 + H2O2
HW613270
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L-histidine + H2O + O2
2-oxohistidine + NH3 + H2O2
Synechococcus cedorum
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less than 2% of the activity with L-arginine
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L-histidine + H2O + O2
2-oxohistidine + NH3 + H2O2
Synechococcus cedorum PCC 6908
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less than 2% of the activity with L-arginine
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L-histidine + H2O + O2
2-oxohistidine + NH3 + H2O2
less than 2% of the activity with L-arginine
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L-histidine + H2O + O2
2-oxohistidine + NH3 + H2O2
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less than 2% of the activity with L-arginine
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L-histidine + H2O + O2
2-oxohistidine + NH3 + H2O2
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L-homoarginine + H2O + O2
2-oxohomoarginine + NH3 + H2O2
HW613270
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L-homoarginine + H2O + O2
2-oxohomoarginine + NH3 + H2O2
HW613270
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L-lysine + H2O + O2
2-oxolysine + NH3 + H2O2
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15% of the activity with L-arginine
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L-lysine + H2O + O2
2-oxolysine + NH3 + H2O2
HW613270
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L-lysine + H2O + O2
2-oxolysine + NH3 + H2O2
HW613270
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L-lysine + H2O + O2
2-oxolysine + NH3 + H2O2
Synechococcus cedorum
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81% of the activity with L-arginine
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L-lysine + H2O + O2
2-oxolysine + NH3 + H2O2
Synechococcus cedorum PCC 6908
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81% of the activity with L-arginine
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L-lysine + H2O + O2
2-oxolysine + NH3 + H2O2
73% of the activity with L-arginine
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L-lysine + H2O + O2
2-oxolysine + NH3 + H2O2
82% of the activity with L-arginine
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L-lysine + H2O + O2
2-oxolysine + NH3 + H2O2
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82% of the activity with L-arginine
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L-lysine + H2O + O2
2-oxolysine + NH3 + H2O2
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L-ornithine + H2O + O2
2-oxoornithine + NH3 + H2O2
Synechococcus cedorum
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35% of the activity with L-arginine
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L-ornithine + H2O + O2
2-oxoornithine + NH3 + H2O2
Synechococcus cedorum PCC 6908
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35% of the activity with L-arginine
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L-ornithine + H2O + O2
2-oxoornithine + NH3 + H2O2
28% of the activity with L-arginine
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L-ornithine + H2O + O2
2-oxoornithine + NH3 + H2O2
46% of the activity with L-arginine
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L-ornithine + H2O + O2
2-oxoornithine + NH3 + H2O2
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28% of the activity with L-arginine
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L-ornithine + H2O + O2
2-oxoornithine + NH3 + H2O2
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
Synechococcus cedorum
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
Synechococcus cedorum PCC 6908
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
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L-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
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FAD
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1 mol per mol of enzyme
FAD
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FAD-dependent enzyme
FAD
HW613270
1 mol of FAD being contained per mol of subunit. Purified enzyme shows absorption maxima at 275, 375, and 460 nm
FAD
evaluation of the binding site
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1-naphthol
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10 mM, 53% inhibition
nordihydroguaiaretic acid
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0.5 mM, 63% inhibition
o-phenanthroline
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5 mM, 72% inhibition
Sodium azide
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100 mM, 77% inhibition
additional information
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not inhibitory: EDTA, p-chloromercuric acid, hydroxylamine, p-aminobenzoic acid, 8-hydroxyquinoline, sodium cyanide
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Ca2+
Synechococcus cedorum
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5.25
L-lysine
HW613270
pH 7.0, 37°C
0.149
L-arginine
HW613270
pH 7.0, 37°C
0.223
L-arginine
pH 8.0, 40°C, L-glutamate oxidase mutant R305E
3
L-arginine
pH not specified in the publication, temperature not specified in the publication
4
L-arginine
Synechococcus cedorum
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pH not specified in the publication, temperature not specified in the publication
5
L-arginine
pH not specified in the publication, temperature not specified in the publication
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3.42
L-arginine
pH 8.0, 40°C, L-glutamate oxidase mutant R305E
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15.3
L-arginine
pH 8.0, 40°C, L-glutamate oxidase mutant R305E
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0.15
Cd2+
Synechococcus elongatus PCC 7942 = FACHB-805
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pH 7.0, 20°C
0.38
Co2+
Synechococcus elongatus PCC 7942 = FACHB-805
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pH 7.0, 20°C
0.06
Cu2+
Synechococcus elongatus PCC 7942 = FACHB-805
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pH 7.0, 20°C
0.16
Mn2+
Synechococcus elongatus PCC 7942 = FACHB-805
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pH 7.0, 20°C
0.065
Zn2+
Synechococcus elongatus PCC 7942 = FACHB-805
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pH 7.0, 20°C
1.1
Ca2+
Synechococcus elongatus
pH not specified in the publication, temperature not specified in the publication
1.1
Ca2+
Synechococcus cedorum
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pH not specified in the publication, temperature not specified in the publication
1.6
Ca2+
Synechococcus elongatus
pH not specified in the publication, temperature not specified in the publication
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120.3
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substrate L-arginine, 20°C, pH 7.0
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6 - 6.5
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substrate L-histidine
8
L-glutamate oxidase mutant R305E
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6 - 10
pH 6.0: about 15% of maximal activity, pH 10: about 35% of maximal activity, L-glutamate oxidase mutant R305E
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40
L-glutamate oxidase mutant R305E
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30 - 60
30°C: more than 90% of maximal activity, 60°C: about 75% of maximal activity, L-glutamate oxidase mutant R305E
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brenda
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HW613270
GenBank
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HW613270
GenBank
brenda
wild-type L-glutamate oxidase enzyme shows strict substrate specificity for L-glutamate. The R305E mutant variant of L-glutamate oxidase exhibits strict specificity for L-arginine, cf. EC 1.4.3.11
UniProt
brenda
Synechococcus cedorum
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brenda
Synechococcus cedorum PCC 6908
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brenda
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brenda
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brenda
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UniProt
brenda
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small part of the protein
brenda
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small part of the protein
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brenda
Synechococcus cedorum
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40-60% of total activity
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brenda
Synechococcus cedorum PCC 6908
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40-60% of total activity
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brenda
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predominant localization
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brenda
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predominant localization
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brenda
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evolution
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L-arginine oxidase evolves from a highly thermostable and promiscuous FAD-dependent amino acid oxidase
physiological function
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growth on L-arginine as the sole source of carbon and nitrogen induces synthesis of the enzymes of a catabolic pathway for arginine. The catabolic sequence in this pathway is: L-arginine - alpha-ketoarginine - gamma-guanidinobutanoate - gamma-aminobutanoate. Cell-free extracts of cultures grown on L-arginine produce ammonia from L-arginine, CO2 from alpha-ketoarginine, and show hydrolytic removal of urea from gamma-guanidinobutanoate
physiological function
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mutant cells lacking L-amino acid oxidase protein cannot grow on L-arginine as sole N-source. Mutant cells can grow on nitrate or ammonium as N-source under photoautotropic conditions with a growth rate of about 75% of the wild-type rate. Under these conditions the photosynthetic O2 evolving activity is reduced by about the same amount, and the pigment content, especially the phycobiliprotein content, is much lower than in wild-type
physiological function
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mutant cells lacking L-amino acid oxidase protein cannot grow on L-arginine as sole N-source. Mutant cells can grow on nitrate or ammonium as N-source under photoautotropic conditions with a growth rate of about 75% of the wild-type rate. Under these conditions the photosynthetic O2 evolving activity is reduced by about the same amount, and the pigment content, especially the phycobiliprotein content, is much lower than in wild-type
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physiological function
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growth on L-arginine as the sole source of carbon and nitrogen induces synthesis of the enzymes of a catabolic pathway for arginine. The catabolic sequence in this pathway is: L-arginine - alpha-ketoarginine - gamma-guanidinobutanoate - gamma-aminobutanoate. Cell-free extracts of cultures grown on L-arginine produce ammonia from L-arginine, CO2 from alpha-ketoarginine, and show hydrolytic removal of urea from gamma-guanidinobutanoate
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OXLA_HUMAN
567
0
62881
Swiss-Prot
Secretory Pathway (Reliability: 1 )
OXLA_MOUSE
630
0
70191
Swiss-Prot
Secretory Pathway (Reliability: 1 )
OXLA_MUSSP
46
0
5165
Swiss-Prot
other Location (Reliability: 1 )
P72346_SYNP6
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
495
0
54131
TrEMBL
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Q8L3C7_9ACTN
701
0
77891
TrEMBL
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49000
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2 * 49000, SDS-PAGE
50000
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x * 50000, SDS-PAGE
528000
HW613270
gel filtration
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dimer
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2 * 49000, SDS-PAGE
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x * 50000, SDS-PAGE
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x * 50000, SDS-PAGE
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octamer
HW613270
8 * 66000, SDS-PAGE, 8 * 66300, calculated
octamer
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8 * 66000, SDS-PAGE, 8 * 66300, calculated
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structure of the L-glutamate oxidase R305E mutant enzymed is determined at 2.65 A resolution
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R305E
wild-type enzyme shows strict substrate specificity for L-glutamate. The mutant variant of L-glutamate oxidase exhibits strict specificity for L-arginine. L-Glutamate oxidase R305E mutant is a thermostable and pH stable enzyme
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5 - 11
1 h, 40°C, residual activity is over 80% in the pH range of 5.0-11.0, L-glutamate oxidase mutant R305E
765731
5.5 - 7.5
HW613270
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740395
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50
pH 7.4, remaining activity is 100% after 1 h incubation, L-glutamate oxidase mutant R305E
70
pH 7.4, remaining activity is 60% after 1 h incubation, L-glutamate oxidase mutant R305E
71
pH 7.4, melting temperature,L-glutamate oxidase mutant R305E
60
HW613270
stable up to
60
pH 7.4, remaining activity is 88% after 1 h incubation, L-glutamate oxidase mutant R305E
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both native and recombinant protein
HW613270
L-glutamate oxidase R305E mutant enzyme
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analysis
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an amperometric biosensors for L-arginine determination is described that is based on L-arginine oxidase and peroxidase-like nanozymes
diagnostics
the R305E mutant enzyme is suitable for the determination of L-arginine. L-Arginine can be a medical biomarker because patients with argininemia or cancer show unusual concentrations of L-arginine in the blood
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Pistorius, E.K.; Voss, H.
Some properties of a basic L-amino-acid oxidase from Anacystis nidulans
Biochim. Biophys. Acta
611
227-240
1980
Synechococcus elongatus PCC 7942 = FACHB-805
brenda
Gau, A.E.; Heindl, A.; Nodop, A.; Kahmann, U.; Pistorius, E.K.
L-amino acid oxidases with specificity for basic L-amino acids in cyanobacteria
Z. Naturforsch. C
62
273-284
2007
Synechococcus elongatus, Synechococcus elongatus (P72346), Synechococcus cedorum, Synechococcus cedorum PCC 6908, Synechococcus elongatus PCC 7942
brenda
Bockholt, R.; Scholten-Beck, G.; Pistorius, E.K.
Construction and partial characterization of an L-amino acid oxidase-free Synechococcus PCC 7942 mutant and localization of the L-amino acid oxidase in the corresponding wild type
Biochim. Biophys. Acta
1307
111-121
1996
Synechococcus sp., Synechococcus sp. PCC 7942
brenda
Matsui, D.; Terai, A.; Asano, Y.
L-Arginine oxidase from Pseudomonas sp. TPU 7192: Characterization, gene cloning, heterologous expression, and application to L-arginine determination
Enzyme Microb. Technol.
82
151-157
2016
Pseudomonas sp. (HW613270), Pseudomonas sp., Pseudomonas sp. TPU 7192 (HW613270)
brenda
Miller, D.; Rodwell, V.
Metabolism of basic amino acids in Pseudomonas putida. Intermediates in L-arginine catabolism
J. Biol. Chem.
246
5053-5058
1971
Pseudomonas putida, Pseudomonas putida ATCC 25571
brenda
Nakano, S.; Niwa, M.; Asano, Y.; Ito, S.
Following the evolutionary track of a highly specific L-arginine oxidase by reconstruction and biochemical analysis of ancestral and native enzymes
Appl. Environ. Microbiol.
85
e00459-19
2019
Oceanobacter kriegii
brenda
Stasyuk, N.; Gayda, G.; Demkiv, O.; Darmohray, L.; Gonchar, M.; Nisnevitch, M.
Amperometric biosensors for L-arginine determination based on L-arginine oxidase and peroxidase-like nanozymes
Appl. Sci.
11
7024
2021
Amanita phalloides
-
brenda
Yano, Y.; Matsuo, S.; Ito, N.; Tamura, T.; Kusakabe, H.; Inagaki, K.; Imada, K.
A new L-arginine oxidase engineered from L-glutamate oxidase
Protein Sci.
30
1044-1055
2021
Streptomyces sp. X-119-6 (Q8L3C7)
brenda
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