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Information on EC 3.2.2.1 - purine nucleosidase
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3.2.2.1 purine nucleosidaseIUBMB Comments
The enzyme from the bacterium Ochrobactrum anthropi specifically catalyses the irreversible N-riboside hydrolysis of purine nucleosides. Pyrimidine nucleosides, purine and pyrimidine nucleotides, NAD+, NADP+ and nicotinaminde mononucleotide are not substrates .
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Word Map
- 3.2.2.1
-
salvage
- trypanosoma
- pyrimidine
- hydrolases
- fasciculata
-
crithidia
- vivax
- ribose
- brucei
-
pyrimidine-specific
-
n-glycosidic
-
schramm
- parkin
- iminoribitols
- formycin
-
trypanocidal
-
horenstein
- drug development
- pharmacology
- analysis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
6-oxopurine nucleosidase, CELE_Y43F8C.13, IAG nucleoside hydrolase, IAG-NH, IAG-nucleoside hydrolase, IAGNH, IG-NH, inosine-adenosine-guanosine nucleoside hydrolase, inosine-adenosine-guanosine-preferring nucleoside hydrolase, inosine-guanosine nucleoside hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IAG nucleoside hydrolase
-
-
-
-
IAG-NH
IAGNH
inosine-adenosine-guanosine nucleoside hydrolase
inosine-adenosine-guanosine-preferring nucleoside hydrolase
-
IU-nucleoside hydrolase
-
-
-
-
IunH
IunH is important in moderating inosine- or adenosine-induced germination of Bacillus thuringiensis spores
N-ribosyl purine ribohydrolase
-
-
-
-
N-ribosyl-purine ribohydrolase
-
-
-
-
nucleosidase
-
-
-
-
nucleosidase g
-
-
-
-
nucleoside hydrolase
-
-
-
-
PpNRH1
purine beta-ribosidase
-
-
-
-
purine NRH
Purine nucleosidase
-
-
-
-
purine nucleoside hydrolase
-
-
-
-
purine nucleoside N-ribohydrolase
purine ribonucleosidase
-
-
-
-
purine-preferring nucleoside hydrolase
purine-specific hydrolase
-
-
-
-
purine-specific inosine-adenosine-guanosine nucleoside hydrolase
purine-specific inosineadenosine-guanosine nucleoside hydrolase
-
-
purine-specific NH
purine-specific nucleoside hydrolase
purine-specific ribonucleoside hydrolase
ribonucleoside hydrolase
-
-
-
-
RihC
SsIAG-NH
SSO2243
Tb927.3.2960
IAG-NH
-
the enzyme is specific for adenosine, guanosine and inosine
IAG-NH
-
the enzyme is specific for adenosine, guanosine and inosine
-
purine-specific inosine-adenosine-guanosine nucleoside hydrolase
-
purine-specific inosine-adenosine-guanosine nucleoside hydrolase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a purine nucleoside + H2O = D-ribose + a purine base
-
-
-
-
a purine nucleoside + H2O = D-ribose + a purine base
main features of transition state are activation of the heterocyclic base by protonation of/or hydrogen bonding to O2, an extensively broken C-N-glycosysic bond, formation of an oxocarbenium ion in the ribose ring, C3’-exo ribose ring conformation, and almost no bond formation to the attacking nucleophile
-
a purine nucleoside + H2O = D-ribose + a purine base
mechanism couples loop closure to the positioning of active site residues. Relationship between the dimeric form of the enzyme and its catalytic activity
-
a purine nucleoside + H2O = D-ribose + a purine base
ordered bi-bi kinetic mechanism and high forward commitment with inosine as substrate. The dominant energetic contribution towards catalysis comes from ribosyl and water activation, leaving group activation also makes a considerable contribution. The leaving group is unlikely to be protonated prior to N-glycosidic bond cleavage and active site binding interactions to the purine leaving group are required for efficient ribosyl and/or water activation
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
hydrolysis of N-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
purine-nucleoside ribohydrolase
The enzyme from the bacterium Ochrobactrum anthropi specifically catalyses the irreversible N-riboside hydrolysis of purine nucleosides. Pyrimidine nucleosides, purine and pyrimidine nucleotides, NAD+, NADP+ and nicotinaminde mononucleotide are not substrates [6].
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CAS REGISTRY NUMBER
COMMENTARY
9025-44-9
-
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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
2,6-diamino-9-beta-D-ribofuranosylpurine + H2O
2,6-diaminopurine + D-ribose
-
76% of the activity with inosine
-
-
ir
2,8-diamino-9-beta-D-ribofuranosyladenine + H2O
2,8-diaminoadenine + D-ribose
-
38% of the activity with inosine
-
-
ir
2-hydroxy-9-beta-D-ribofuranosyladenine + H2O
2-hydroxyadenine + D-ribose
-
10% of the activity with inosine
-
-
ir
3'-AMP + H2O
adenine + D-ribose 3-phosphate
E15229
0.67% of the activity with adenosine
-
-
?
4-nitrophenyl beta-D-ribofuranoside + H2O
4-nitrophenol + beta-D-ribofuranose
-
-
-
-
?
4-nitrophenyl beta-D-ribofuranoside + H2O
4-nitrophenol + D-ribose
-
-
-
-
?
5,6-dimethyl-1-beta-D-ribofuranosylbenzimidazole + H2O
5,6-dimethylbenzimidazole + D-ribose
-
200% of the activity with inosine
-
-
ir
6-dimethylamino-9-beta-D-ribofuranosylbenzimidazole + H2O
6-dimethylaminobenzimidazole + D-ribose
-
30% of the activity with inosine
-
-
ir
6-mercaptopurine ribonucleoside + H2O
6-mercaptopurine + ribose
-
-
-
-
?
9-beta-D-ribofuranosylpurine + H2O
purine + D-ribose
-
47% of the activity with inosine
-
-
ir
imidazoleacetic acid riboside + H2O
imidazoleacetate + D-ribose
-
5% of the activity with inosine
-
-
ir
nicotinamide riboside + H2O
nicotinamide + D-ribose
-
150% of the activity with inosine
-
-
ir
adenosine + H2O
D-ribose + adenine
-
15% of the activity with inosine
-
-
?
adenosine + H2O
D-ribose + adenine
-
103% of the activity with inosine
-
-
ir
adenosine + H2O
D-ribose + adenine
-
IAG-NH shows higher affinity for adenosine with respect to inosine and guanosine, but the catalytic efficiency of these substrates is comparable
-
-
?
adenosine + H2O
D-ribose + adenine
-
substrate for inosine-adenosine-guanosine nucleoside hydrolase
-
-
?
adenosine + H2O
D-ribose + adenine
-
3.6% of the activity with xanthosine
-
-
?
cytidine + H2O
cytosine + D-ribose
-
about 20% of the rate with adenosine
-
-
?
cytidine + H2O
D-ribose + cytosine
-
54% of the activity with inosine
-
-
ir
guanosine + H2O
D-ribose + guanine
-
33% of the activity with inosine
-
-
?
guanosine + H2O
D-ribose + guanine
-
about 80% of the rate with adenosine
-
-
?
guanosine + H2O
D-ribose + guanine
-
90% of the activity with inosine
-
-
ir
guanosine + H2O
D-ribose + guanine
-
1.4% of the activity with xanthosine
-
-
?
guanosine + H2O
guanine + D-ribose
E15229
29.5% of the activity with adenosine
-
-
?
inosine + H2O
D-ribose + hypoxanthine
87% of the activity with xanthosine
-
-
?
inosine + H2O
D-ribose + hypoxanthine
87% of the activity with xanthosine
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
kinetic mechanism is rapid equilibrium with random product release
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
rate of hydrolysis similar to adenosine
-
-
?
inosine + H2O
hypoxanthine + D-ribose
E15229
78.9% of the activity with adenosine
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
kinetic mechanism is rapid equilibrium with random product release
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
25% of the activity with xanthosine
-
-
?
uridine + H2O
D-ribose + uracil
-
substrate for isoform URH1, but nor URH2
-
-
?
uridine + H2O
D-ribose + uracil
-
about 15% of the rate with adenosine
-
-
?
xanthosine + H2O
D-ribose + xanthine
best substrate
-
-
?
xanthosine + H2O
xanthine + D-ribose
E15229
63.5% of the activity with adenosine
-
-
?
additional information
?
-
-
no hydrolysis of the pyrimidines uridine and cytidine
-
-
-
additional information
?
-
hydrolase activity could not be detected when uridine or cytidine is used as a substrate
-
-
-
additional information
?
-
-
hydrolase activity could not be detected when uridine or cytidine is used as a substrate
-
-
-
additional information
?
-
IunH can hydrolyse inosine, adenosine and guanosine with the activity order: inosine
-
-
-
additional information
?
-
-
IunH can hydrolyse inosine, adenosine and guanosine with the activity order: inosine
-
-
-
additional information
?
-
-
isoform rih1 shows pyrimidine-specific ribonuclease activity. Activity of isoform rih2 in decreasing order: inosine, adenine, uridine, guanosine, xanthosine, cytidine
-
-
-
additional information
?
-
-
the enzyme prefers ribonucleosides and 2'-O-methylribonucleosides as its hydrolytic substrates, but reacts weakly with 2'-deoxyribonucleosides
-
-
-
additional information
?
-
poor activity with adenosine, uridine, and guanosine, no activity with cytokinin riboside, cytidine, and trans-zeatin riboside. Substrate docking into the active site, overview
-
-
-
additional information
?
-
-
poor activity with adenosine, uridine, and guanosine, no activity with cytokinin riboside, cytidine, and trans-zeatin riboside. Substrate docking into the active site, overview
-
-
-
additional information
?
-
poor activity with adenosine, uridine, and guanosine, no activity with cytokinin riboside, cytidine, and trans-zeatin riboside. Substrate docking into the active site, overview
-
-
-
additional information
?
-
-
IAG-NH does not recognize as substrate nucleosides 5'-phosphates, NAD+ and NADP+
-
-
-
additional information
?
-
-
the enzyme catalyzes the irreversible hydrolysis of the N-glycosidic bond of beta-ribonucleosides forming ribose and purine base, substrate specificity and involved residues, overview
-
-
-
additional information
?
-
-
IAG-NH does not recognize as substrate nucleosides 5'-phosphates, NAD+ and NADP+
-
-
-
additional information
?
-
-
cytidine, uridine, and 4-nitrophenyl-riboside are poor substrates
-
-
-
additional information
?
-
-
inosine-guanosine nucleoside hydrolase does not use adenosine as substrate
-
-
-
additional information
?
-
-
cytidine, uridine, and 4-nitrophenyl-riboside are poor substrates
-
-
-
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NATURAL SUBSTRATE
NATURAL 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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
E15229
3 mM, reactivation after preincubation with 8-hydroxyquinoline
Zn2+
E15229
3 mM, reactivation after preincubation with 8-hydroxyquinoline
Ca2+
-
the active site contains the trademark Ca2+ ion of nucleodide hydrolase enzymes, octacoordinated by residues Asp9, Asp14, Ile121, and Asp238, two solvent molecules, and one glycerol molecule
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3R,4S)-1-[(4-amino-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidine-3,4-diol
-
-
(2R,3R,4S)-1-[(4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidin-3,4-diol
-
nanomolar inhibitor
(2R,3R,4S)-2-(hydroxymethyl)-1-(quinolin-8-ylmethyl)pyrrolidin-3,4-diol
-
nanomolar inhibitor
(2R,3R,4S)-2-(hydroxymethyl)-1-(quinolin-8-ylmethyl)pyrrolidine-3,4-diol
-
-
(2S,3R,4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidine-3,4-diol
-
nanomolar inhibitor
1,4-dideoxy-1,4-imino-N-(1-methyl-1H-1,2,3-benzotriazol-5-yl)methyl-D-ribitol
-
-
1,4-dideoxy-1,4-imino-N-(1-methyl-1H-benzimidazol-2-yl)methyl-D-ribitol
-
-
1,4-dideoxy-1,4-imino-N-(4-amino-2-methylquinolin-8-yl)methyl-D-ribitol
-
-
1,4-dideoxy-1,4-imino-N-(4-aminothieno[3,2-d]pyrimidin-7-yl)-methyl-D-ribitol
-
-
1,4-dideoxy-1,4-imino-N-(4-chloro-2-methylquinolin-8-yl)methyl-D-ribitol
-
-
1,4-dideoxy-1,4-imino-N-(4-methyl-2-phenylpyrimidin-5-yl)methyl-D-ribitol
-
-
1-[2-[(2S,3S,4R,5R)-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-2-yl]ethyl]guanidine
-
-
1-[3-[(2R,3R,4S)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-yl]propyl]guanidine
-
-
7-[[(2R,3R,4S)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
-
cytidine
E15229
0.5 mM, 81% inhibition of activity with adenosine, 92% inhibition of activity with inosine, 91% inhibition of the activity with xanthosine, 94% inhibition of activity with guanosine
Li2SO4
-
inhibits activity with adenosine and guanosine, slight inhibition of activity with inosine
MnSO4
-
inhibits activity with adenosine and guanosine, very slight inhibition of activity with inosine
(+-)-1-[(9-deazahypoxanthin-9-yl)methyl]azetidine-2-methanol
-
transition state analogue inhibitor, comparison with inhibition of human and Plasmodium falciparum enzyme
(+-)-1-[(9-deazahypoxanthin-9-yl)methyl]azetidine-2-methanol
-
transition state analogue inhibitor, comparison with inhibition of bovine and Plasmodium falciparum enzyme
(+-)-1-[(9-deazahypoxanthin-9-yl)methyl]azetidine-2-methanol
-
transition state analogue inhibitor, comparison with inhibition of human and bovine enzyme
1-[(7-benzyloxymethyl-6-tert-butoxy-9-deazapurin-9-yl)methyl] azetidine-3-methanol
-
transition state analogue inhibitor, comparison with inhibition of human and Plasmodium falciparum enzyme
1-[(7-benzyloxymethyl-6-tert-butoxy-9-deazapurin-9-yl)methyl] azetidine-3-methanol
-
transition state analogue inhibitor, comparison with inhibition of bovine and Plasmodium falciparum enzyme
1-[(7-benzyloxymethyl-6-tert-butoxy-9-deazapurin-9-yl)methyl] azetidine-3-methanol
-
transition state analogue inhibitor, comparison with inhibition of human and bovine enzyme. Ki value above 10 microM
1-[(9-deazahypoxanthin-9-yl)methyl]azetidine-3,3dimethanol
-
transition state analogue inhibitor, comparison with inhibition of human and Plasmodium falciparum enzyme
1-[(9-deazahypoxanthin-9-yl)methyl]azetidine-3,3dimethanol
-
transition state analogue inhibitor, comparison with inhibition of bovine and Plasmodium falciparum enzyme
1-[(9-deazahypoxanthin-9-yl)methyl]azetidine-3,3dimethanol
-
transition state analogue inhibitor, comparison with inhibition of human and bovine enzyme, Ki value above 10 microM
4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin H
-
i.e. DADMe-ImmH, transition state analogue inhibitor, comparison with inhibition of human and Plasmodium falciparum enzyme
4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin H
-
i.e. DADMe-ImmH, transition state analogue inhibitor, comparison with inhibition of bovine and Plasmodium falciparum enzyme
adenosine
-
competitive inhibitor of xanthosine hydrolysis and inosine hydrolysis
EDTA
-
after 1 h incubation with EDTA (5 mM) the enzyme activity is reduced to less than 0.05% and is restored by addition of 20 mM CaCl2
immucillin H
-
transition-state inhibitor, i.e. (1S)-1-(9-deazahypoxanthin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol
immucillin H
-
immucilin H is (1S)-1-(9-deazahypoxanthin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol
immucillin H
-
immucillin H is (1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol
meso-[(9-deazahypoxanthin-9-yl)methyl]azetidine-2,4-dimethanol hydrochloride
-
transition state analogue inhibitor, comparison with inhibition of human and Plasmodium falciparum enzyme
meso-[(9-deazahypoxanthin-9-yl)methyl]azetidine-2,4-dimethanol hydrochloride
-
transition state analogue inhibitor, comparison with inhibition of bovine and Plasmodium falciparum enzyme
meso-[(9-deazahypoxanthin-9-yl)methyl]azetidine-2,4-dimethanol hydrochloride
-
transition state analogue inhibitor, comparison with inhibition of human and bovine enzyme
N-(9-deaza-adenin-9-yl)methyl-1,4-dideoxy-1,4-imino-D-ribitol
-
UAMC-00363, is the only N-arylmethyl-substituted iminoribitol derivative active as chemotherapeutic agent against trypanosomiasis, validation in an in vivo model of African trypanosomiasis. No cross-resistance to the diamidine or the melaminophenyl arsenical classes of trypanocides
UAMC-00363
-
i.e. N-(9-deaza-adenin-9-yl)methyl-1,4-dideoxy-1,4-imino-D-ribitol, significant inhibition of inosine-adenosine-guanosine nucleoside hydrolase and inosine-guanosine nucleoside hydrolase
UAMC-00363
-
i.e. N-(9-deaza-adenin-9-yl)methyl-1,4-dideoxy-1,4-imino-D-ribitol
uridine
E15229
0.5 mM, 38% inhibition of activity with adenosine, 45% inhibition of activity with inosine, 35% inhibition of the activity with xanthosine, 58% inhibition of activity with guanosine
additional information
-
transition state analogue inhibitors of protozoan nucleoside hydrolases
-
additional information
-
high-affinity inhibition of the enzyme by iminoribitol-based compounds. Metallorganic complexes can compete for binding at the active site of nucleoside hydrolase enzymes, mimicking the positively charged transition state of the enzymatic reaction, different modes of iminoribitol ring binding at a conserved active site, overview. Divalent metal ions can act as noncompetitive enzyme inhibitors, stabilizing a nonproductive conformation of the catalytic loop
-
additional information
in silico docking experiments using flavone, 5-hydroxyflavone, 7-hydroxyflavone, chrysin, apigenin, kaempferol, fisetin, and quercetin. All tested flavonoids show high affinities for the enzyme, the lowest free binding energy ranging from -10.23 to -7.14 kcal/mol
-
additional information
-
in silico docking experiments using flavone, 5-hydroxyflavone, 7-hydroxyflavone, chrysin, apigenin, kaempferol, fisetin, and quercetin. All tested flavonoids show high affinities for the enzyme, the lowest free binding energy ranging from -10.23 to -7.14 kcal/mol
-
additional information
-
N-arylmethyl-substituted iminoribitol derivatives as potential chemotherapeutic agents against trypanosomiasis, validation in an in vivo model of African trypanosomiasis
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Leukemia
Purine Nucleosidase Phosphorylase (PNP): A novel target in leukemias and lymphomas.
Lymphoma
Purine Nucleosidase Phosphorylase (PNP): A novel target in leukemias and lymphomas.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
B6T563
substrate specificity and kinetics, overview
-
0.009
2-aminopurine riboside
-
wild type enzyme, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.0005
7-methyl guanosine
-
wild type enzyme, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.0018
guanosine
-
mutant enzyme D253P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.0023
guanosine
-
wild type enzyme, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.003
guanosine
-
mutant enzyme E249P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.004
guanosine
-
mutant enzyme C248P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.008
guanosine
-
mutant enzyme H247P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.016
guanosine
-
mutant enzyme L250P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.021
guanosine
-
mutant enzyme L251P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.024
guanosine
-
mutant enzyme R252P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.33
Inosine
-
mutant enzyme H79A, pH and temperature not specified in the publication
0.34
Inosine
-
wild-type enzyme, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.57
2-aminopurine riboside
-
wild type enzyme, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
1.07
7-methyl guanosine
-
wild type enzyme, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
1.09
guanosine
-
mutant enzyme C248P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
1.4
guanosine
-
mutant enzyme L250P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
1.7
guanosine
-
mutant enzyme E249P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
2.3
guanosine
-
wild type enzyme, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
2.5
guanosine
-
mutant enzyme L251P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
3.9
guanosine
-
mutant enzyme D253P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
4.1
guanosine
-
mutant enzyme H247P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
13
guanosine
-
mutant enzyme R252P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.85
Inosine
-
mutant enzyme H79A, pH and temperature not specified in the publication
11.6
Inosine
-
wild-type enzyme, pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.6
Inosine
-
mutant enzyme H79A, pH and temperature not specified in the publication
34.1
Inosine
-
wild-type enzyme, pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018
(1S )-1,4-dideoxy-1-(2-guanidinoethyl)-1,4-imino-D-ribitol
-
pH 7.0, 35°C
0.0000041
(2R,3R,4S)-1-[(4-amino-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidine-3,4-diol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0000044
(2R,3R,4S)-1-[(4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidin-3,4-diol
-
-
0.0043
(2R,3R,4S)-2-(hydroxymethyl)-1-(4-iodobenzyl)pyrrolidine-3,4-diol
-
-
0.0075
(2R,3R,4S)-2-(hydroxymethyl)-1-(4-nitrobenzyl)pyrrolidine-3,4-diol
-
-
0.0000108
(2R,3R,4S)-2-(hydroxymethyl)-1-(quinolin-8-ylmethyl)pyrrolidin-3,4-diol
-
-
0.0000108
(2R,3R,4S)-2-(hydroxymethyl)-1-(quinolin-8-ylmethyl)pyrrolidine-3,4-diol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0000041
(2S,3R,4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidine-3,4-diol
-
-
0.00075
1,4-dideoxy-1,4-imino-N-(1-isoquinolinyl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00072
1,4-dideoxy-1,4-imino-N-(1-methyl-1H-1,2,3-benzotriazol-5-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0021
1,4-dideoxy-1,4-imino-N-(1-methyl-1H-benzimidazol-2-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.187
1,4-dideoxy-1,4-imino-N-(2(1H)-quinolon-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00004
1,4-dideoxy-1,4-imino-N-(2-amino-4-benzothiazoyl)-methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.12
1,4-dideoxy-1,4-imino-N-(2-aminopyridin-3-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00836
1,4-dideoxy-1,4-imino-N-(2-aminoquinolin-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000314
1,4-dideoxy-1,4-imino-N-(2-chloroquinolin-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.001258
1,4-dideoxy-1,4-imino-N-(2-methoxyquinolin-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.002
1,4-dideoxy-1,4-imino-N-(2-naphthyl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00018
1,4-dideoxy-1,4-imino-N-(2-quinolinyl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0038
1,4-dideoxy-1,4-imino-N-(3-cyanobenzyl)-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.012
1,4-dideoxy-1,4-imino-N-(3-indolyl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0023
1,4-dideoxy-1,4-imino-N-(3-nitrobenzyl)-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.02
1,4-dideoxy-1,4-imino-N-(3-quinolinyl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0131
1,4-dideoxy-1,4-imino-N-(4(1H)-quinolon-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0713
1,4-dideoxy-1,4-imino-N-(4-amino-2-methylquinolin-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000015
1,4-dideoxy-1,4-imino-N-(4-aminoquinazolin-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00005
1,4-dideoxy-1,4-imino-N-(4-aminoquinolin-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000019
1,4-dideoxy-1,4-imino-N-(4-aminothieno[3,2-d]pyrimidin-7-yl)-methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000369
1,4-dideoxy-1,4-imino-N-(4-chloro-2-methylquinolin-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000014
1,4-dideoxy-1,4-imino-N-(4-chloroquinolin-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.026
1,4-dideoxy-1,4-imino-N-(4-cyanobenzyl)-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000029
1,4-dideoxy-1,4-imino-N-(4-methoxyquinolin-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.043
1,4-dideoxy-1,4-imino-N-(4-methyl-2-phenylpyrimidin-5-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.02
1,4-dideoxy-1,4-imino-N-(4-pyridinyl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.029
1,4-dideoxy-1,4-imino-N-(4-quinolinyl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.032
1,4-dideoxy-1,4-imino-N-(6-methoxypyridin-3-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0023
1,4-dideoxy-1,4-imino-N-(7-methoxy-indol-3-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00072
1,4-dideoxy-1,4-imino-N-(7-quinolinyl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00002
1,4-dideoxy-1,4-imino-N-(7-thieno[3,2-d]pyrimidonyl)-methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.001
1,4-dideoxy-1,4-imino-N-(8-hydroxyquinolin-2-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0000108
1,4-dideoxy-1,4-imino-N-(8-quinolinyl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000058
1,4-dideoxy-1,4-imino-N-(quinazolin-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000109
1,4-dideoxy-1,4-imino-N-(quinazolon-8-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000139
1,4-dideoxy-1,4-imino-N-(quinoxalin-5-yl)-methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000042
1,4-dideoxy-1,4-imino-N-(thieno[3,2-d]pyrimidin-7-yl)methyl-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0034
1,4-dideoxy-1,4-imino-N-[3-(1H-pyrrol-1-yl)benzyl]-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0012
1,4-dideoxy-1,4-imino-N-[4-(1H-pyrazol-1-yl)benzyl]-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.001
1,4-dideoxy-1,4-imino-N-[4-(1H-pyrrol-1-yl)benzyl]-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00000048 - 0.0000063
1-[(7-benzyloxymethyl-6-tert-butoxy-9-deazapurin-9-yl)methyl] azetidine-3-methanol
0.018
1-[2-[(2S,3S,4R,5R)-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-2-yl]ethyl]guanidine
-
-
0.04
1-[3-[(2R,3R,4S)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-yl]propyl]guanidine
-
-
0.0000044
7-[[(2R,3R,4S)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
1.2
8-aza-immucillin H
-
mutant R252A, pH 7.0, 35°C; wild-type, pH 7.0, 35°C
0.0000129 - 0.000016
meso-[(9-deazahypoxanthin-9-yl)methyl]azetidine-2,4-dimethanol hydrochloride
0.0000044
N-(9-deazahypoxanthin-9-yl)methyl-1,4-dideoxy-1,4-imino-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000063
1,4-dideoxy-1,4-imino-N-[4-(1H-1,2,4-triazol-1-yl)benzyl]-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0012
1,4-dideoxy-1,4-imino-N-[4-(1H-1,2,4-triazol-1-yl)benzyl]-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00000048
1-[(7-benzyloxymethyl-6-tert-butoxy-9-deazapurin-9-yl)methyl] azetidine-3-methanol
-
pH 7.0
0.0000063
1-[(7-benzyloxymethyl-6-tert-butoxy-9-deazapurin-9-yl)methyl] azetidine-3-methanol
-
pH 7.0
0.0000009
immucillin A
-
inosine-adenosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.0000044
immucillin A
-
inosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.0000062
immucillin A
-
pH and temperature not specified in the publication
0.0000062
immucillin H
-
pH and temperature not specified in the publication
0.000009
immucillin H
-
inosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.000024
immucillin H
-
inosine-adenosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.0000129
meso-[(9-deazahypoxanthin-9-yl)methyl]azetidine-2,4-dimethanol hydrochloride
-
pH 7.0
0.000016
meso-[(9-deazahypoxanthin-9-yl)methyl]azetidine-2,4-dimethanol hydrochloride
-
pH 7.0
0.0000041
N-(9-deaza-adenin-9-yl)methyl-1,4-dideoxy-1,4-imino-D-ribitol
-
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.59
N-(9-deaza-adenin-9-yl)methyl-1,4-dideoxy-1,4-imino-D-ribitol
-
-
0.00003
UAMC-00109
-
inosine-adenosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.138
UAMC-00109
-
inosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.000446
UAMC-00115
-
inosine-adenosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.011
UAMC-00115
-
inosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.00056
UAMC-00311
-
inosine-adenosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.014
UAMC-00311
-
inosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.00019
UAMC-00312
-
inosine-adenosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.12
UAMC-00312
-
inosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.000018
UAMC-00363
-
inosine-adenosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.032
UAMC-00363
-
inosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.000056
UAMC-00375
-
inosine-adenosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
0.031
UAMC-00375
-
inosine-guanosine nucleoside hydrolase, pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.034
UAMC-00312
Trypanosoma brucei brucei
-
pH and temperature not specified in the publication
0.00049
UAMC-00363
Trypanosoma brucei brucei
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
pH 5.0: about 55% of maximal activity, pH 8.0: about 40% of maximal activity
5 - 10
inosine hydrolase activity of the purified recombinant IunH is detected over a wide range of pH values, the highest activity being obtained at pH 6
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
50
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
40 - 70
-
40°C: about 55% of maximal activity with inosine, about 45% of maximal activity with guanosine, about 40% of maximal activity with adenosine, 70°C: about 30% of maximal activity with inosine, about 35% of maximal activity with guanosine, about 25% of maximal activity with adenosine
40 - 100
the activity is stable over a wide temperature range, the highest activity being at 80°C with high activity being maintained up to 100°C
60 - 115
-
the enzyme is highly thermoactive, its activity increases sharply up to the optimal temperature of 105°C and 50% activity is still observed at 115°C
30 - 70
-
30°C: about 35% of maximal activity, 70°C: about 20% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 distinct nucleosidases, one is active on nucleosides, the other on deoxynucleosides
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
secreted, activity is much larger in female salivary glands than in male
brenda