3.2.2.8: ribosylpyrimidine nucleosidase
This is an abbreviated version!
For detailed information about ribosylpyrimidine nucleosidase, go to the full flat file.
Word Map on EC 3.2.2.8
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3.2.2.8
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purine
-
leishmania
-
salvage
-
inosine
-
leishmaniasis
-
donovani
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crithidia
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fasciculata
-
vivax
-
purine-specific
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n-glycosidic
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ribonucleosides
-
schramm
-
chaga
-
horenstein
-
iminoribitols
-
inosine-adenosine-guanosine
-
ribooxocarbenium
-
xanthosine
-
zymodeme
- 3.2.2.8
- purine
- leishmania
-
salvage
- inosine
- leishmaniasis
- donovani
- crithidia
- fasciculata
- vivax
-
purine-specific
-
n-glycosidic
- ribonucleosides
-
schramm
-
chaga
-
horenstein
- iminoribitols
-
inosine-adenosine-guanosine
-
ribooxocarbenium
- xanthosine
-
zymodeme
Reaction
Synonyms
CU-NH, cytidine-uridine nucleoside hydrolase, cytidine-uridine-preferring nucleoside hydrolase, LBRM_18_1610, More, N-ribohydrolase, N-ribosylpyrimidine nucleosidase, N-ribosylpyrimidine ribohydrolase, NH, NSH1, nucleosidase, pyrimidine, nucleoside hydrolase, pyrimidine nucleosidase, pyrimidine nucleoside hydrolase, pyrimidine-specific nucleoside hydrolase, ribonucleoside hydrolase 1, rih1, RihA, RihB, SsCU-NH, SSO0505, URH1, uridine-ribohydrolase 1, YbeK, YeiK
ECTree
3.2.2.8 ribosylpyrimidine nucleosidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.2.2.8 - ribosylpyrimidine nucleosidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-beta-D-ribofuranosylnicotinamide + H2O
nicotinamide + D-ribose
-
-
-
?
1-beta-D-ribofuranosylthymine + H2O
D-ribose + thymine
-
-
-
?
4-amino-5-imidazolecarboxamide ribonucleotide + H2O
4-amino-5-imidazolecarboxamide + D-ribose
-
-
-
?
4-nitrophenyl beta-D-ribofuranoside + H2O
4-nitrophenol + D-ribose
-
-
-
?
4-nitrophenyl ribopyranoside + H2O
4-nitrophenol + D-ribose
-
-
-
?
6-azauridine + H2O
6-azauracil + D-ribose
-
poor substrate
-
?
6-mercaptopurine ribonucleoside + H2O
6-mercaptopurine + D-ribose
-
-
-
?
imidazoleacetic acid ribonucleotide + H2O
imidazoleacetic acid + D-ribose
-
-
-
?
inosine + H2O
?
catalytic efficiency towards inosine is at least 100-fold below that for uridine
-
-
?
N-ribosylpyrimidine + H2O
pyrimidine + D-ribose
preferred substrate
-
-
r
tubercidin + H2O
1-deazaadenine + D-ribose
-
poor substrate
-
?
5-fluorouridine + H2O
5-fluorouracil + D-ribose
-
detagged recombinant enzyme
-
-
?
purine D-ribonucleosides + H2O
purine + D-ribose
-
appreciable substrate activity if a hydroxyl or thio group is present in the 6-position or if a hydroxyl group is present in the 2- and 6-position, preference for oxo versus amino substituents
-
?
purine D-ribonucleosides + H2O
purine + D-ribose
-
prefers pyrimidines
-
?
purine D-ribonucleosides + H2O
purine + D-ribose
-
prefers pyrimidines
-
?
purine D-ribonucleosides + H2O
purine + D-ribose
-
prefers pyrimidines
-
?
uridine + H2O
uracil + D-ribose
the pure recombinant protein exhibits highest hydrolase activity for uridine, followed by inosine and adenosine
-
-
?
uridine + H2O
uracil + D-ribose
-
cleaves uridine most efficiantly
-
?
uridine + H2O
uracil + D-ribose
-
cleaves uridine most efficiantly
-
?
xanthosine + H2O
xanthine + D-ribose
-
high hydrolytic efficiency, xanthosine is a better substrate for isoform NSH1 compared to inosine and adenosine
-
-
?
additional information
?
-
-
the pure recombinant protein exhibits highest hydrolase activity for uridine, followed by inosine and adenosine
-
-
?
additional information
?
-
the pure recombinant protein exhibits highest hydrolase activity for uridine, followed by inosine and adenosine
-
-
?
additional information
?
-
-
enzyme is pyrimidine specific, purine nucleosides are not hydrolysed, 2'-, 3'- and 5'-deoxynucleosides are no substrates
-
-
?
additional information
?
-
-
catalytic cycles between the open and closed conformations of RihA, stabilization of two flexible active site regions is pivotal to establish the interactions required for substrate discrimination and catalysis, involvement of the Asp10 as general base in the mechanism, role of the conserved His82 residue in modulating product release, structure-function analysis, detailed overview
-
-
?
additional information
?
-
the enzyme is required for recycling of nitrogenous bases
-
-
?
additional information
?
-
-
detagged recombinant enzyme: substrate specificity, no activity with purine nucleosides, and with 2'-, 3'-, and 5'-deoxynucleosides
-
-
?
