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Information on EC 3.2.2.2 - inosine nucleosidase
for references in articles please use BRENDA:EC3.2.2.2
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EC Tree 3 Hydrolases
3.2 Glycosylases
3.2.2 Hydrolysing N-glycosyl compounds
3.2.2.2 inosine nucleosidase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 3.2.2.2
- trypanosoma
- vivax
-
salvage
-
n-glycosidic
- hypoxanthine
- iminoribitols
-
trypanocidal
- riboside
-
isozyme-specific
-
trypanosomiasis
- ribonucleosides
- anthracis
- xanthosine
- fasciculata
-
crithidia
showSynonyms
purine-specific nucleoside hydrolase, inosine nucleosidase, inosine hydrolase, inosine-adenosine-guanosine nucleoside hydrolase, guanosine-inosine-preferring nucleoside n-ribohydrolase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
inosinase
-
-
-
-
inosine-adenosine-guanosine nucleoside hydrolase
inosine-guanosine nucleosidase
-
-
-
-
nucleosidase, inosine
-
-
-
-
inosine-adenosine-guanosine nucleoside hydrolase
-
purine-specific
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inosine + H2O = D-ribose + hypoxanthine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
adenosine nucleotides degradation I
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SYSTEMATIC NAME
IUBMB Comments
inosine ribohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9030-95-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-methylguanosine + H2O
1-methylguanine + D-ribose
-
Substrates: -
Products: -
Products: -
?
1-N2-ethenoguanosine + H2O
1-N2-ethenoguanine + D-ribose
-
Substrates: -
Products: -
Products: -
?
1-N2-isopropenoguanosine + H2O
1-N2-isopropenoguanine + D-ribose
-
Substrates: -
Products: -
Products: -
?
5-methyluridine + H2O
D-ribose + 5-methyluracil
-
Substrates: -
Products: -
Products: -
?
7-methylguanosine + H2O
7-methylguanine + D-ribose
-
Substrates: -
Products: -
Products: -
?
purine riboside + H2O
purine + D-ribose
-
Substrates: nebularine
Products: -
Products: -
?
6-mercaptopurine riboside + H2O
6-mercaptopurine + D-ribose
-
Substrates: inhibitor and substrate
Products: -
Products: -
?
6-mercaptopurine riboside + H2O
6-mercaptopurine + D-ribose
-
Substrates: -
Products: -
Products: -
?
adenosine + H2O
adenine + D-ribose
-
Substrates: -
Products: -
Products: -
?
adenosine + H2O
D-ribose + adenine
-
Substrates: after 1 h, the rate of adenosine cleavage is about 12.5%
Products: -
Products: -
?
adenosine + H2O
D-ribose + adenine
-
Substrates: after 1 h, the rate of adenosine cleavage is about 12.5%
Products: -
Products: -
?
guanosine + H2O
D-ribose + guanine
-
Substrates: after 1 h, the rate of guanosine cleavage is about 16%
Products: -
Products: -
?
guanosine + H2O
D-ribose + guanine
-
Substrates: after 1 h, the rate of guanosine cleavage is about 16%
Products: -
Products: -
?
guanosine + H2O
guanine + D-ribose
-
Substrates: guanosine is hydrolyzed 12% faster than inosine
Products: -
Products: -
?
guanosine + H2O
guanine + D-ribose
-
Substrates: -
Products: -
Products: -
?
inosine + H2O
D-ribose + hypoxanthine
-
Substrates: -
Products: -
Products: -
?
inosine + H2O
D-ribose + hypoxanthine
-
Substrates: isoform NSH2 shows highest hydrolysis capacity for inosine
Products: -
Products: -
?
inosine + H2O
D-ribose + hypoxanthine
-
Substrates: best substrate
Products: -
Products: -
?
inosine + H2O
D-ribose + hypoxanthine
-
Substrates: best substrate
Products: -
Products: -
?
inosine + H2O
hypoxanthine + D-ribose
-
Substrates: -
Products: -
Products: -
?
inosine + H2O
hypoxanthine + D-ribose
Substrates: -
Products: -
Products: -
?
inosine + H2O
hypoxanthine + D-ribose
-
Substrates: guanosine is hydrolyzed 12% faster than inosine
Products: -
Products: -
?
inosine + H2O
hypoxanthine + D-ribose
-
Substrates: -
Products: -
Products: -
?
inosine + H2O
hypoxanthine + D-ribose
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the pure recombinant protein exhibits highest hydrolase activity for uridine, followed by inosine and adenosine
Products: -
Products: -
?
additional information
?
-
-
Substrates: adenosine and xanthosine are poor substrates. No substrate are: 2'-deoxyguanosine, 2'-deoxyinosine, 2'-methylguanosine, pyrimidine nucleosides and 5'-GMP
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
inosine + H2O
hypoxanthine + D-ribose
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
binds to I1- and I2-site, noncompetitive inhibition, ligand exclusion model
Co2+
-
24.2% residual activity at 0.1 M using inosine as substrate, 25.8% residual activity at 0.1 M using guanosine as substrate, 33.3% residual activity at 0.1 M using adenosine as substrate
Cu2+
-
10.6% residual activity at 0.1 M using inosine as substrate, 9.67% residual activity at 0.1 M using guanosine as substrate, complete inhibition at 0.1 M using adenosine as substrate
Fe2+
-
60.6% residual activity at 0.1 M using inosine as substrate, 54.8% residual activity at 0.1 M using guanosine as substrate, 66.6% residual activity at 0.1 M using adenosine as substrate
Mg2+
-
62.1% residual activity at 0.1 M using inosine as substrate, 74.2% residual activity at 0.1 M using guanosine as substrate, 75% residual activity at 0.1 M using adenosine as substrate
NaCN
-
60.6% residual activity at 0.1 M using inosine as substrate, 38.7% residual activity at 0.1 M using guanosine as substrate, 41.6% residual activity at 0.1 M using adenosine as substrate
nucleoside diphosphates
-
less effective inhibitor compared to nucleoside triphosphates, non competitive inhibition
nucleoside triphosphates
-
most potent inhibitor, non competitive inhibition
Mn2+
-
complete inhibition at 0.1 M using inosine, adenosine or guanosine as substrate
Zn2+
-
57.5% residual activity at 0.1 M using inosine as substrate, 45.2% residual activity at 0.1 M using guanosine as substrate, 41.6% residual activity at 0.1 M using adenosine as substrate
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Structures of purine nucleosidase from Trypanosoma brucei bound to isozyme-specific trypanocidals and a novel metalorganic inhibitor.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.44
methyluridine
-
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105 - 115
-
105°C: maximal activity, 115°C: 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
isoform NSH2 acts during the late phase of senescence and supports inosine breakdown
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). URH1_ARATH
336
0
36086
Swiss-Prot
other Location (Reliability: 2)
URH2_ARATH
322
0
34668
Swiss-Prot
other Location (Reliability: 2)
NSH3_ARATH
890
0
99072
Swiss-Prot
Secretory Pathway (Reliability: 1)
IUNH_CRIFA
315
0
34326
Swiss-Prot
other Location (Reliability: 3)
IUNH_LEIMA
314
0
34310
Swiss-Prot
other Location (Reliability: 2)
A0A2G9FXT6_9LAMI
320
0
34258
TrEMBL
other Location (Reliability: 2)
A0A396JQD2_MEDTR
339
0
36337
TrEMBL
other Location (Reliability: 1)
A0A7S7M5C6_LEIDO
312
0
33980
TrEMBL
other Location (Reliability: 2)
A0A7S7M5D0_LEIDO
312
0
34010
TrEMBL
other Location (Reliability: 2)
A0A7S7RT38_LEIDO
312
0
34011
TrEMBL
other Location (Reliability: 3)
B7FJZ5_MEDTR
322
0
34322
TrEMBL
other Location (Reliability: 2)
A0A7S7M5D6_LEIDO
312
0
34077
TrEMBL
other Location (Reliability: 2)
A0A2P6RHV4_ROSCH
322
0
34392
TrEMBL
other Location (Reliability: 1)
A0A7S7RT81_LEIDO
312
0
33984
TrEMBL
other Location (Reliability: 3)
A0A7S7M6Z8_LEIDO
312
0
34050
TrEMBL
other Location (Reliability: 2)
A7UHH1_BACTK
321
0
36271
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34000
-
2 * 34000 Da, SDS-PAGE, predicted: 34325 Da/subunit, intersubunit disulfide bond
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homodimer
-
2 * 34000 Da, SDS-PAGE, predicted: 34325 Da/subunit, intersubunit disulfide bond
homodimer
-
2 * 34000 Da, SDS-PAGE, predicted: 34325 Da/subunit, intersubunit disulfide bond
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
mutants expressing the Arabidopsis thaliana enzyme or the homologue from Oryza sativa exhibit resistance toward toxic fluorouridine, fluorouracil, and fluoroorotic acid. Mutants with increased and decreased nucleosidase activity are delayed in germination
additional information
-
mutant strains lacking the basal layer protein exsY and devoid of exosporium lack detectable levels of collagen-like glycoprotein BclA and the basal layer proteins BxpB, BxpC, CotY, and inosine-uridine-preferring nucleoside hydrolase. The mutation does not affect spore production and germination efficiencies or spore resistance but does influence the course of spore outgrow
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 60
-
the enzyme shows 68.18%, 45.45% and 28.78% residual activities for inosine hydrolysis after 4 min, 6 min, and 8 min of incubation, respectively, at 50°C. The enzyme is completely inactivated after 10 min at 50°C and 4 min at 60°C