Information on EC 1.1.3.28 - nucleoside oxidase

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The expected taxonomic range for this enzyme is: Stenotrophomonas maltophilia

EC NUMBER
COMMENTARY hide
1.1.3.28
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RECOMMENDED NAME
GeneOntology No.
nucleoside oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
inosine + O2 = 9-riburonosylhypoxanthine + H2O
show the reaction diagram
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
82599-71-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxyadenosine + O2
9-(2-deoxy-beta-D-erythro-pentofuranuronosyl)-9H-purin-6-amine + H2O
show the reaction diagram
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81.4% of the activity compared to inosine
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?
adenosine + O2
9-riburonosyladenine + H2O
show the reaction diagram
cytidine + O2
1-riburonosylcytosine + H2O
show the reaction diagram
deoxycytidine + O2
1-riburonosylcytosine + H2O
show the reaction diagram
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77.3% of the activity compared to inosine
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?
deoxyguanosine + O2
9-riburonosyldeoxyguanine + H2O
show the reaction diagram
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92.3% of the activity compared to inosine
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?
deoxyinosine + O2
9-riburonosyldeoxyhypoxanthine + H2O
show the reaction diagram
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80.7% of the activity compared to inosine
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?
guanosine + O2
9-riburonosylguanine + H2O
show the reaction diagram
hydroquinone + inosine + O2
p-quinone + 9-riburonosylhypoxanthine + H2O
show the reaction diagram
inosine + O2
9-riburonosylhypoxanthine + H2O
show the reaction diagram
thymidine + O2
1-riburonosylthymine + H2O
show the reaction diagram
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55.8% of the activity compared to inosine
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?
uridine + O2
1-riburonosyluracil + H2O
show the reaction diagram
xanthosine + O2
9-riburonosylxanthine + H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
inosine + O2
9-riburonosylhypoxanthine + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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1 FAD covalently bound to the alpha subunit
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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2 g non-heme iron per mol of enzyme, contains also a heme component
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HgCl2
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30.8% inhibition at 1 mM
KCN
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65.2% inhibition at 1 mM, complete inhibition at 10 mM
N-bromosuccinimide
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complete inhibition at 1 mM
NaN3
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18.5% inhibition at 1 mM
Pb(CH3COO)2
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18.7% inhibition at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
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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
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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
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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
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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
130000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6
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stable for 1 h at 37°C
287612
5 - 6.5
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crude enzyme, stable within
287611
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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stable below, complete loss of activity at 75°C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to homogeneity, chromatography techniques
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