We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Information on EC 1.1.3.28 - nucleoside oxidase for references in articles please use BRENDA:EC1.1.3.28Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Stenotrophomonas maltophilia
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
inosine + O2 = 9-riburonosylhypoxanthine + H2O
Other purine and pyrimidine nucleosides, as well as 2'-deoxynucleoside, are substrates, but ribose and nucleotides are not substrates. The overall reaction takes place in two separate steps: 1. 2 inosine + O2 = 2 5'-dehydroinosine + 2 H2O. 2. 2 5'-dehydroinosine + O2 = 2 9-riburonosylhypoxanthine + 2 H2O, with the 5'-dehydro nucleoside being released from the enzyme to serve as substrate for the second reaction. This enzyme differs from EC 1.1.3.39, nucleoside oxidase (H2O2-forming), as it produces water rather than hydrogen peroxide
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
nucleoside:oxygen 5'-oxidoreductase
Other purine and pyrimidine nucleosides (as well as 2'-deoxyribonucleosides) are substrates, but ribose and nucleotides are not substrates. The overall reaction takes place in two separate steps, with the 5'-dehydro nucleoside being released from the enzyme to serve as substrate for the second reaction. This enzyme differs from EC 1.1.3.39, nucleoside oxidase (H2O2-forming), as it produces water rather than hydrogen peroxide.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2'-deoxyadenosine + O2
9-(2-deoxy-beta-D-erythro-pentofuranuronosyl)-9H-purin-6-amine + H2O
-
81.4% of the activity compared to inosine
-
?
adenosine + O2
9-riburonosyladenine + H2O
cytidine + O2
1-riburonosylcytosine + H2O
deoxycytidine + O2
1-riburonosylcytosine + H2O
-
77.3% of the activity compared to inosine
-
?
deoxyguanosine + O2
9-riburonosyldeoxyguanine + H2O
-
92.3% of the activity compared to inosine
-
?
deoxyinosine + O2
9-riburonosyldeoxyhypoxanthine + H2O
-
80.7% of the activity compared to inosine
-
?
guanosine + O2
9-riburonosylguanine + H2O
hydroquinone + inosine + O2
p-quinone + 9-riburonosylhypoxanthine + H2O
inosine + O2
9-riburonosylhypoxanthine + H2O
thymidine + O2
1-riburonosylthymine + H2O
-
55.8% of the activity compared to inosine
-
?
uridine + O2
1-riburonosyluracil + H2O
xanthosine + O2
9-riburonosylxanthine + H2O
adenosine + O2
9-riburonosyladenine + H2O
-
97.3% of the activity compared to inosine
-
?
adenosine + O2
9-riburonosyladenine + H2O
-
97.3% of the activity compared to inosine
-
?
cytidine + O2
1-riburonosylcytosine + H2O
-
77.3% of the activity compared to inosine
-
?
cytidine + O2
1-riburonosylcytosine + H2O
-
77.3% of the activity compared to inosine
-
?
guanosine + O2
9-riburonosylguanine + H2O
-
121% of the activity compared to inosine
-
?
guanosine + O2
9-riburonosylguanine + H2O
-
121% of the activity compared to inosine
-
?
hydroquinone + inosine + O2
p-quinone + 9-riburonosylhypoxanthine + H2O
-
oxidation of hydroquinone only in the presence of nucleosides, laccase-like activity, 2 times more O2 consumed if hydroquinone is added in a large excess over inosine
2:1-ratio of p-quinone to 9-riburonosylhypoxanthine
?
hydroquinone + inosine + O2
p-quinone + 9-riburonosylhypoxanthine + H2O
-
oxidation of hydroquinone only in the presence of nucleosides, laccase-like activity, 2 times more O2 consumed if hydroquinone is added in a large excess over inosine
2:1-ratio of p-quinone to 9-riburonosylhypoxanthine
?
inosine + O2
9-riburonosylhypoxanthine + H2O
-
-
-
?
inosine + O2
9-riburonosylhypoxanthine + H2O
-
catalysing the oxidation via inosine-5'-aldehyde
-
?
inosine + O2
9-riburonosylhypoxanthine + H2O
-
oxidation of various nucleosides, but no oxidation of nucleotides, bases and ribose
-
?
inosine + O2
9-riburonosylhypoxanthine + H2O
-
-
-
?
inosine + O2
9-riburonosylhypoxanthine + H2O
-
catalysing the oxidation via inosine-5'-aldehyde
-
?
uridine + O2
1-riburonosyluracil + H2O
-
-
-
?
uridine + O2
1-riburonosyluracil + H2O
-
-
-
?
xanthosine + O2
9-riburonosylxanthine + H2O
-
best substrate tested, 125% of the activity compared to inosine
-
?
xanthosine + O2
9-riburonosylxanthine + H2O
-
best substrate tested, 125% of the activity compared to inosine
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
inosine + O2
9-riburonosylhypoxanthine + H2O
inosine + O2
9-riburonosylhypoxanthine + H2O
-
-
-
?
inosine + O2
9-riburonosylhypoxanthine + H2O
-
catalysing the oxidation via inosine-5'-aldehyde
-
?
inosine + O2
9-riburonosylhypoxanthine + H2O
-
oxidation of various nucleosides, but no oxidation of nucleotides, bases and ribose
-
?
inosine + O2
9-riburonosylhypoxanthine + H2O
-
-
-
?
inosine + O2
9-riburonosylhypoxanthine + H2O
-
catalysing the oxidation via inosine-5'-aldehyde
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FAD
-
1 FAD covalently bound to the alpha subunit
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fe2+
-
2 g non-heme iron per mol of enzyme, contains also a heme component
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
HgCl2
-
30.8% inhibition at 1 mM
KCN
-
65.2% inhibition at 1 mM, complete inhibition at 10 mM
N-bromosuccinimide
-
complete inhibition at 1 mM
NaN3
-
18.5% inhibition at 1 mM
Pb(CH3COO)2
-
18.7% inhibition at 1 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
14000
-
alpha,beta,gamma,delta 1 * 76000 + 1 * 33000 + 1 * 18000 + 1 * 14000, SDS-PAGE, subunits beta and delta appear to be linked together by disulfide bonds
18000
-
alpha,beta,gamma,delta 1 * 76000 + 1 * 33000 + 1 * 18000 + 1 * 14000, SDS-PAGE, subunits beta and delta appear to be linked together by disulfide bonds
33000
-
alpha,beta,gamma,delta 1 * 76000 + 1 * 33000 + 1 * 18000 + 1 * 14000, SDS-PAGE, subunits beta and delta appear to be linked together by disulfide bonds
76000
-
alpha,beta,gamma,delta 1 * 76000 + 1 * 33000 + 1 * 18000 + 1 * 14000, SDS-PAGE, subunits beta and delta appear to be linked together by disulfide bonds
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
heterotetramer
-
alpha,beta,gamma,delta 1 * 76000 + 1 * 33000 + 1 * 18000 + 1 * 14000, SDS-PAGE, subunits beta and delta appear to be linked together by disulfide bonds
heterotetramer
-
alpha,beta,gamma,delta 1 * 76000 + 1 * 33000 + 1 * 18000 + 1 * 14000, SDS-PAGE, subunits beta and delta appear to be linked together by disulfide bonds
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5 - 6
-
stable for 1 h at 37°C
287612
5 - 6.5
-
crude enzyme, stable within
287611
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
60
-
stable below, complete loss of activity at 75°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
to homogeneity, chromatography techniques
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Hoshino, M.; Isono, Y.; Sudo, T.
Production of a new enzyme, nucleoside oxidase, by Pseudomonas maltophilia LB-86
Agric. Biol. Chem.
53
399-403
1989
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia LB-86
-
brenda
Isono, Y.; Sudo, T.; Hoshino, M.
Properties of a new enzyme, nucleoside oxidase, from Pseudomonas maltophilia LB-86
Agric. Biol. Chem.
53
1671-1677
1989
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia LB-86
-
brenda
Isono, Y.; Sudo, T.; Hoshino, M.
Purification and reaction of a new enzyme, nucleoside oxidase
Agric. Biol. Chem.
53
1663-1669
1989
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia LB-86
-
brenda
Isono, Y.; Hoshino, M.
Laccase-like activity of nucleoside oxidase in the presence of nucleosides
Agric. Biol. Chem.
53
2197-2203
1989
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia LB-86
-
brenda
html completed