HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 3.2.2.1 - purine nucleosidase
for references in articles please use BRENDA:EC3.2.2.1
Word Map on EC 3.2.2.1
- 3.2.2.1
-
salvage
- trypanosoma
- pyrimidine
- fasciculata
-
crithidia
- vivax
- ribose
-
pyrimidine-specific
-
n-glycosidic
-
iminoribitols
-
schramm
- parkin
-
trypanocidal
-
horenstein
- drug development
- pharmacology
- analysis
Please 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: Eukaryota, Bacteria, Archaea
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
3.2.2.1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
purine nucleosidase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
hydrolysis of N-glycosyl bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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].
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.
CAS REGISTRY NUMBER
COMMENTARY
9025-44-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 distinct nucleosidases, one is active on nucleosides, the other on deoxynucleosides
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
changes in the levels of purine, pyrimidine, and cytokinin metabolites in knockout mutants, phenotypes, overview
malfunction
-
changes in the levels of purine, pyrimidine, and cytokinin metabolites in knockout mutants, phenotypes, overview
-
physiological function
-
both isoforms URH1 and URH2 are unimportant for seedling establishment and plant growth, both isoform URH1 and URH2 are required for efficient inosine and xanthosine hydrolytic activity
physiological function
-
isoform NSH3 functions as an extracellular, purine-specific hydrolase that is involved in degradation of extracellular nucleosides and participates in wound and pathogen responses
additional information
-
molecular mechanism underlying the conformational change necessary for enzymatic catalysis, overview
additional information
-
active site structure, homology modelling, overview
additional information
-
regulation mechanisms of key residues and loops 1 and 2 for the base release, molecular dynamics simulations, overview. The base release process is not the rate-limiting step in the entire hydrolysis process, and the very low barrier of about 5.6 kcal/mol can bewashed out easily by the notable exothermicity fromthe substrate hydrolysis step. Glu82/Trp83 in loop 1 and His247/Arg252 in loop 2 are important to modulate the base release. Partial helix-to-coil change of loop 2 occurs along with the base release process
additional information
the presence of a tyrosine at position 249 (PpNRH1 numbering) confers high hydrolase activity for purine ribosides. All plant nucleoside N-ribohydrolases exhibit a conserved sequence motif, DTDPGIDD, at the N-terminus, and the second Asp of the DTDPGIDD conserved motif functions as the active site base
additional information
-
the presence of a tyrosine at position 249 (PpNRH1 numbering) confers high hydrolase activity for purine ribosides. All plant nucleoside N-ribohydrolases exhibit a conserved sequence motif, DTDPGIDD, at the N-terminus, and the second Asp of the DTDPGIDD conserved motif functions as the active site base
additional information
all plant nucleoside N-ribohydrolases exhibit a conserved sequence motif, DTDPGIDD, at the N-terminus, and the second Asp of the DTDPGIDD conserved motif functions as the active site base
additional information
-
the presence of a tyrosine at position 249 (PpNRH1 numbering) confers high hydrolase activity for purine ribosides. All plant nucleoside N-ribohydrolases exhibit a conserved sequence motif, DTDPGIDD, at the N-terminus, and the second Asp of the DTDPGIDD conserved motif functions as the active site base
-
additional information
-
molecular mechanism underlying the conformational change necessary for enzymatic catalysis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-ribofuranosyladenine + H2O
2,6-diaminoadenine + 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
?
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
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
-
N-arylmethyl-substituted iminoribitol derivatives as potential chemotherapeutic agents against trypanosomiasis, validation in an in vivo model of African trypanosomiasis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
50
60
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
-
30°C: about 35% of maximal activity, 70°C: about 20% of maximal activity
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
secreted, activity is much larger in female salivary glands than in male
-
substantial increase in specific activity over root level concomitant with development of effective nodules
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2);
Trypanosoma brucei brucei (strain 927/4 GUTat10.1);
Trypanosoma vivax;
Q97WH6
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2);
Q97ZS5
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2);
Q57X73
Trypanosoma brucei brucei (strain 927/4 GUTat10.1);
Q57ZL6
Trypanosoma brucei brucei (strain 927/4 GUTat10.1);
Q57ZL6
Trypanosoma brucei brucei (strain 927/4 GUTat10.1);
Q57ZL6
Trypanosoma brucei brucei (strain 927/4 GUTat10.1);
Q57ZL6
Trypanosoma brucei brucei (strain 927/4 GUTat10.1);
Q57ZL6
Trypanosoma brucei brucei (strain 927/4 GUTat10.1);
Q57ZL6
Trypanosoma brucei brucei (strain 927/4 GUTat10.1);
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32310
-
x * 35892, isoform rih1, calculated, x * 32310, isoform rih2, calculated
35892
-
x * 35892, isoform rih1, calculated, x * 32310, isoform rih2, calculated
40000