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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
-
-
-
?
5-bromouridine + H2O
5-bromouracil + D-ribose
5-fluorouridine + H2O
5-fluorouracil + D-ribose
5-iodouridine + H2O
5-iodouracil + D-ribose
-
-
-
-
?
5-methyluridine + H2O
5-methyluracil + D-ribose
-
-
-
-
?
5-methyluridine + H2O
D-ribose + 5-methyluracil
-
-
-
-
?
6-azauridine + H2O
6-azauracil + D-ribose
-
poor substrate
-
?
6-mercaptopurine ribonucleoside + H2O
6-mercaptopurine + D-ribose
-
-
-
?
a pyrimidine nucleoside + H2O
D-ribose + a pyrimidine base
-
-
-
-
?
adenosine + H2O
adenine + D-ribose
adenosine + H2O
D-ribose + adenine
-
-
-
?
cytidine + H2O
cytosine + D-ribose
guanosine + H2O
guanine + 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
-
-
?
inosine + H2O
D-ribose + hypoxanthine
inosine + H2O
hypoxanthine + D-ribose
isopentenyladenine riboside + H2O
?
N-D-ribosylpyrimidine
pyrimidine + D-ribose
N-D-ribosylpyrimidine + H2O
pyrimidine + D-ribose
N-ribosylpurine + H2O
purine + D-ribose
-
-
-
r
N-ribosylpyrimidine + H2O
pyrimidine + D-ribose
preferred substrate
-
-
r
purine D-ribonucleosides + H2O
purine + D-ribose
tubercidin + H2O
1-deazaadenine + D-ribose
-
poor substrate
-
?
uridine + H2O
D-ribose + uracil
-
-
-
?
uridine + H2O
uracil + D-ribose
xanthosine + H2O
xanthine + D-ribose
additional information
?
-
5-bromouridine + H2O
5-bromouracil + D-ribose
-
-
-
-
?
5-bromouridine + H2O
5-bromouracil + D-ribose
-
-
-
?
5-fluorouridine + H2O
5-fluorouracil + D-ribose
-
-
-
-
?
5-fluorouridine + H2O
5-fluorouracil + D-ribose
-
detagged recombinant enzyme
-
-
?
adenosine + H2O
adenine + D-ribose
-
-
-
-
?
adenosine + H2O
adenine + D-ribose
-
-
-
?
adenosine + H2O
adenine + D-ribose
-
-
-
?
adenosine + H2O
adenine + D-ribose
-
-
-
?
adenosine + H2O
adenine + D-ribose
-
-
-
?
cytidine + H2O
cytosine + D-ribose
-
-
-
?
cytidine + H2O
cytosine + D-ribose
-
-
-
-
?
cytidine + H2O
cytosine + D-ribose
-
-
-
?
cytidine + H2O
cytosine + D-ribose
-
detagged recombinant enzyme
-
-
?
cytidine + H2O
cytosine + D-ribose
-
-
-
?
cytidine + H2O
cytosine + D-ribose
-
-
-
?
cytidine + H2O
cytosine + D-ribose
-
-
-
?
cytidine + H2O
cytosine + D-ribose
-
-
-
?
cytidine + H2O
cytosine + D-ribose
-
-
-
?
cytidine + H2O
cytosine + D-ribose
-
-
-
?
guanosine + H2O
guanine + D-ribose
-
-
-
?
guanosine + H2O
guanine + D-ribose
-
-
-
?
guanosine + H2O
guanine + D-ribose
-
-
-
?
inosine + H2O
D-ribose + hypoxanthine
-
-
-
?
inosine + H2O
D-ribose + hypoxanthine
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
poor substrate
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
isopentenyladenine riboside + H2O
?
-
-
-
-
?
isopentenyladenine riboside + H2O
?
-
-
-
?
N-D-ribosylpyrimidine
pyrimidine + D-ribose
-
-
-
?
N-D-ribosylpyrimidine
pyrimidine + D-ribose
-
-
-
?
N-D-ribosylpyrimidine
pyrimidine + D-ribose
-
-
-
?
N-D-ribosylpyrimidine
pyrimidine + D-ribose
-
-
-
?
N-D-ribosylpyrimidine
pyrimidine + D-ribose
-
-
-
?
N-D-ribosylpyrimidine + H2O
pyrimidine + D-ribose
-
-
-
?
N-D-ribosylpyrimidine + H2O
pyrimidine + D-ribose
-
-
-
?
N-D-ribosylpyrimidine + H2O
pyrimidine + D-ribose
-
-
-
?
N-D-ribosylpyrimidine + H2O
pyrimidine + D-ribose
-
-
-
?
N-D-ribosylpyrimidine + H2O
pyrimidine + D-ribose
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
uridine + H2O
uracil + D-ribose
-
-
-
-
?
uridine + H2O
uracil + D-ribose
-
-
-
?
uridine + H2O
uracil + D-ribose
-
-
-
?
uridine + H2O
uracil + D-ribose
-
detagged recombinant enzyme
-
-
?
uridine + H2O
uracil + D-ribose
-
-
-
?
uridine + H2O
uracil + D-ribose
-
cleaves uridine most efficiantly
-
?
uridine + H2O
uracil + D-ribose
-
cleaves uridine most efficiantly
-
?
uridine + H2O
uracil + D-ribose
-
-
-
?
uridine + H2O
uracil + D-ribose
-
-
-
?
uridine + H2O
uracil + D-ribose
-
-
-
?
uridine + H2O
uracil + D-ribose
-
-
-
?
xanthosine + H2O
xanthine + D-ribose
-
high hydrolytic efficiency, xanthosine is a better substrate for isoform NSH1 compared to inosine and adenosine
-
-
?
xanthosine + H2O
xanthine + D-ribose
-
-
-
?
xanthosine + H2O
xanthine + D-ribose
-
second best cleavage
-
?
xanthosine + H2O
xanthine + D-ribose
-
-
-
?
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
?
-
-
no substrate: deazouridine
-
-
?
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
-
-
?
additional information
?
-
-
not: adenosine and guanosine
-
-
?
additional information
?
-
-
not: deoxyribothymidine
-
-
?
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3,4-diaminophenyl-D-iminoribitol
-
competitive, the ligand can bind at the active site in two distinct orientations, binding structure, overview
4,6-Dihydroxy-1-beta-D-ribofuranosylpyrazolo-(3,4-d) pyrimidine
-
-
4-Hydroxyl-1-beta-D-ribofuranosylpyrazolo-(3,4-d) pyrimidine
-
-
4-Methylthio-1-beta-D-ribofuranosylpyrazolo-(3,4-d)pyrimidine
-
-
4-Thio-1-beta-D-ribofuranosylpyrazolo-(3,4-d)pyrimidine
-
-
AgCl
-
at 1 mM: inhibition less than 10%
CaCl2
-
at 1 mM, inhibition less than 10%
CdCl2
-
at 1 mM: inhibition ranging from 40-95%, at 0.01 mM: inhibition less than 10%
CoCl2
-
at 1 mM: inhibition ranging from 40-95%, at 0.01 mM: inhibition less than 10%
CuCl2
-
at 1 mM: inhibition less than 10%
cytidine
-
at 6.25 mM, competitive inhibitor for uridine hydrolysis
EDTA
-
at 1 mM: inhibits uridine hydrolysis by 50%
FeCl3
-
at 1 mM: inhibition ranging from 40-95%, at 0.01 mM: inhibition less than 10%
FeSO4
-
at 1 mM: inhibition less than 10%
HgCl2
-
at 1 mM: inhibition ranging from 40-95%, at 0.01 mM: inhibition less than 10%
Inosine
-
at 6.25 mM, competitive inhibitor for uridine hydrolysis
MgCl2
-
at 1 mM: inhibition less than 10%
MnSO4
-
at 1 mM: inhibition ranging from 40-95%, at 0.01 mM: inhibition less than 10%
NH4Cl
-
at 1 mM: inhibition less than 10%
ZnCl2
-
at 1 mM: inhibition ranging from 40-95%, at 0.01 mM: inhibition less than 10%
additional information
-
poor inhibitors
-
adenosine
-
-
adenosine
-
at 6.25 mM, competitive inhibitor for uridine hydrolysis
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Acanthamoeba Keratitis
Production of a polyclonal antibody against inosine-uridine preferring nucleoside hydrolase of Acanthamoeba castellanii and its access to diagnosis of Acanthamoeba keratitis.
Anthrax
Analysis of Bacillus anthracis nucleoside hydrolase via in silico docking with inhibitors and molecular dynamics simulation.
Anthrax
Combined virtual screening, MMPBSA, molecular docking and dynamics studies against deadly anthrax: An in silico effort to inhibit Bacillus anthracis nucleoside hydrolase.
Anthrax
Design of new chemotherapeutics against the deadly anthrax disease. Docking and molecular dynamics studies of inhibitors containing pyrrolidine and riboamidrazone rings on nucleoside hydrolase from Bacillus anthracis.
Bacterial Infections
Analysis of Bacillus anthracis nucleoside hydrolase via in silico docking with inhibitors and molecular dynamics simulation.
Infections
A Chimera Containing CD4+ and CD8+ T-Cell Epitopes of the Leishmania donovani Nucleoside Hydrolase (NH36) Optimizes Cross-Protection against Leishmania amazonesis Infection.
Infections
Druggability of the guanosine/adenosine/cytidine nucleoside hydrolase from Trichomonas vaginalis.
Infections
Evaluation of immune responses and protection induced by A2 and nucleoside hydrolase (NH) DNA vaccines against Leishmania chagasi and Leishmania amazonensis experimental infections.
Infections
Leishmania donovani Nucleoside Hydrolase Terminal Domains in Cross-Protective Immunotherapy Against Leishmania amazonensis Murine Infection.
Infections
The F1F3 Recombinant Chimera of Leishmania donovani-Nucleoside Hydrolase (NH36) and Its Epitopes Induce Cross-Protection Against Leishmania (V.) braziliensis Infection in Mice.
Leishmaniasis
F1 Domain of the Leishmania (Leishmania) donovani Nucleoside Hydrolase Promotes a Th1 Response in Leishmania (Leishmania) infantum Cured Patients and in Asymptomatic Individuals Living in an Endemic Area of Leishmaniasis.
Leishmaniasis, Cutaneous
Expression, purification, immunogenicity and protective efficacy of a recombinant nucleoside hydrolase from Leishmania donovani, a vaccine candidate for preventing cutaneous leishmaniasis.
Leishmaniasis, Cutaneous
Isoenzyme characterization of Leishmania isolated from human cases with localized cutaneous leishmaniasis from the State of Campeche, Yucatan Peninsula, Mexico.
Leishmaniasis, Visceral
Cross-protective efficacy of a prophylactic Leishmania donovani DNA vaccine against visceral and cutaneous murine leishmaniasis.
Leishmaniasis, Visceral
Expression, purification and spectrophotometric analysis of nucleoside hydrolase from Leishmania chagasi (LcNH).
Leishmaniasis, Visceral
F1 Domain of the Leishmania (Leishmania) donovani Nucleoside Hydrolase Promotes a Th1 Response in Leishmania (Leishmania) infantum Cured Patients and in Asymptomatic Individuals Living in an Endemic Area of Leishmaniasis.
Leishmaniasis, Visceral
Nucleoside hydrolase DNA vaccine against canine visceral leishmaniasis.
Leishmaniasis, Visceral
Nucleoside hydrolase from Leishmania (L.) donovani is an antigen diagnostic for visceral leishmaniasis.
Neoplasms
Crystal structure to 1.7 a of the Escherichia coli pyrimidine nucleoside hydrolase YeiK, a novel candidate for cancer gene therapy.
Neoplasms
Identification of a 2'-O-Methyluridine Nucleoside Hydrolase Using the Metagenomic Libraries.
Parasitic Diseases
Analysis of Bacillus anthracis nucleoside hydrolase via in silico docking with inhibitors and molecular dynamics simulation.
Trypanosomiasis, African
Evaluation of nucleoside hydrolase inhibitors for treatment of African trypanosomiasis.
Tuberculosis
Biochemical characterization of recombinant nucleoside hydrolase from Mycobacterium tuberculosis H37Rv.
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7.5
1-beta-D-ribofuranosylthymine
-
-
0.25
4-nitrophenyl beta-D-ribofuranoside
pH 7.5, 25°C
0.18
4-nitrophenyl ribopyranoside
pH 7.0, 35°C, recombinant enzyme
0.186 - 2.5
5-Bromouridine
0.128
5-fluorouridine
-
pH 7.3, 37°C
0.22
5-iodouridine
-
pH 7.3, 37°C
0.329
5-methyluridine
-
pH 7.3, 37°C
0.33
6-mercaptopurine ribonucleoside
-
-
0.4
isopentenyladenine-riboside
recombinant enzyme expressed in Escherichia coli, in 50 mM Tris-HCl, pH 7.5, at 30°C
0.44
methyluridine
-
isoform NSH1, pH not specified in the publication, at 30°C
0.78
purine ribonucleoside
-
-
additional information
additional information
-
0.186
5-Bromouridine
-
pH 7.3, 37°C
0.5
adenosine
-
pH 8.5
0.6
adenosine
pH 7.5, 25°C
0.648
adenosine
pH 7.0, 35°C, recombinant enzyme
0.7
adenosine
recombinant enzyme expressed in Escherichia coli, in 50 mM Tris-HCl, pH 7.5, at 30°C
0.7
adenosine
-
isoform NSH1, pH not specified in the publication, at 30°C
0.524
cytidine
pH 7.0, 35°C, recombinant enzyme
0.532
cytidine
-
pH 7.3, 37°C
0.7
cytidine
pH 7.5, 25°C
0.97
cytidine
pH 7.4, 80°C
0.363
guanosine
pH 7.0, 35°C, recombinant enzyme
0.2
Inosine
-
pH 8.5
0.239
Inosine
pH 7.0, 35°C, recombinant enzyme
1.16
Inosine
mutant enzyme T223Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
1.4
Inosine
recombinant enzyme expressed in Escherichia coli
1.4
Inosine
recombinant enzyme expressed in Escherichia coli, in 50 mM Tris-HCl, pH 7.5, at 30°C
1.4
Inosine
-
isoform NSH1, pH not specified in the publication, at 30°C
1.77
Inosine
mutant enzyme Q227F, in 50 mM HEPES buffer (pH 7.3), at 37°C
1.93
Inosine
mutant enzyme T223Y/Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
2.14
Inosine
mutant enzyme Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
2.34
Inosine
wild type enzyme, in 50 mM HEPES buffer (pH 7.3), at 37°C
3.29
Inosine
mutant enzyme T223A, in 50 mM HEPES buffer (pH 7.3), at 37°C
4.31
Inosine
mutant enzyme Q227A, in 50 mM HEPES buffer (pH 7.3), at 37°C
4.42
Inosine
mutant enzyme T223F/Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
5.3
Inosine
mutant enzyme T223F, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.083
uridine
pH 7.0, 35°C, recombinant enzyme
0.12
uridine
wild type enzyme, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.142
uridine
-
pH 7.3, 37°C
0.31
uridine
pH 7.4, 80°C
0.31
uridine
mutant enzyme T223F, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.33
uridine
mutant enzyme T223A, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.345
uridine
-
pH 7.3, 37°C, H82N mutant
0.57
uridine
mutant enzyme Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.77
uridine
mutant enzyme Q227A, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.8
uridine
recombinant enzyme expressed in Escherichia coli, in 50 mM Tris-HCl, pH 7.5, at 30°C
0.8
uridine
-
isoform NSH1, pH not specified in the publication, at 30°C
1.06
uridine
mutant enzyme T223Y/Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
1.09
uridine
mutant enzyme T223F/Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
1.13
uridine
mutant enzyme T223Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
1.19
uridine
mutant enzyme Q227F, in 50 mM HEPES buffer (pH 7.3), at 37°C
1.9
uridine
-
pH 7.3, 37°C, H239A mutant
2.1
uridine
recombinant enzyme expressed in Saccharomyces cerevisiae, in 50 mM Tris-HCl, pH 7.5, at 30°C
3.6
uridine
positive homotropic cooperativity, Hill coefficient value of 2.4, pH 7.5, 25°C
1.11
Xanthosine
-
-
1.69
Xanthosine
-
isoform NSH1, pH not specified in the publication, at 30°C
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics
-
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344
4-nitrophenyl beta-D-ribofuranoside
pH 7.5, 25°C
39
4-nitrophenyl ribopyranoside
pH 7.0, 35°C, recombinant enzyme
30.8
5-Bromouridine
-
pH 7.3, 37°C
14.7
5-fluorouridine
-
pH 7.3, 37°C
42.7
5-iodouridine
-
pH 7.3, 37°C
25.5
5-methyluridine
-
pH 7.3, 37°C
0.0056
guanosine
pH 7.0, 35°C, recombinant enzyme
0.0154
adenosine
pH 7.0, 35°C, recombinant enzyme
0.039
adenosine
pH 7.5, 25°C
0.066
cytidine
pH 7.5, 25°C
11.6
cytidine
-
pH 7.3, 37°C
11.6
cytidine
pH 7.0, 35°C, recombinant enzyme
39.4
cytidine
pH 7.4, 80°C
0.035
Inosine
mutant enzyme T223Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.043
Inosine
pH 7.0, 35°C, recombinant enzyme
0.086
Inosine
wild type enzyme, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.109
Inosine
mutant enzyme T223F, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.125
Inosine
mutant enzyme Q227F, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.18
Inosine
mutant enzyme T223A, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.182
Inosine
mutant enzyme Q227A, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.382
Inosine
mutant enzyme T223F/Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
0.593
Inosine
mutant enzyme Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
3.62
Inosine
mutant enzyme T223Y/Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
11.2
Inosine
pH 7.5, 25°C
4.4
uridine
-
pH 7.3, 37°C, H239A mutant
4.7
uridine
-
pH 7.3, 37°C
5.4
uridine
wild type enzyme, in 50 mM HEPES buffer (pH 7.3), at 37°C
13.9
uridine
pH 7.0, 35°C, recombinant enzyme
15.1
uridine
mutant enzyme Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
15.5
uridine
-
pH 7.3, 37°C, H82N mutant
18.8
uridine
mutant enzyme T223F, in 50 mM HEPES buffer (pH 7.3), at 37°C
39.8
uridine
mutant enzyme T223A, in 50 mM HEPES buffer (pH 7.3), at 37°C
44.3
uridine
mutant enzyme T223Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
46.9
uridine
mutant enzyme Q227A, in 50 mM HEPES buffer (pH 7.3), at 37°C
52.5
uridine
mutant enzyme Q227F, in 50 mM HEPES buffer (pH 7.3), at 37°C
59.1
uridine
mutant enzyme T223F/Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
72.9
uridine
mutant enzyme T223Y/Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C
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hanging drop vapor diffusion method
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hanging drop vapour diffusion method, using 100 mM Tris (pH 8.5), 200 mM NaCl, and 24% PEG 4000
molecular dynamics simulation. Both in wild-type and mutant T223Y/Q227Y, inosine binding is facilitated by interactions of the ribose moiety with active site residues and Ca2+, and pi-interactions between residues His82 and His239 and the nucleobase. The lack of observed activity toward inosine for wild-type CU-NH is explained by no residue being correctly aligned to stabilize the departing nucleobase. A hydrogen-bonding network between hypoxanthine and a general acid Asp15 is present when the two Tyr mutations are engineered into the active site. This hydrogen-bonding network is only maintained when both Tyr mutations are present due to a pi-interaction between the residues
QM/MM simulations. The relatively stronger hydrogen-bond interactions between uridine and the active-site residues Gln227 and Tyr231 play an important role in enhancing the substrate binding and thus promoting the N-glycosidic bond cleavage, in comparison with inosine. The estimated energy barrier is 30 kcal/mol for the hydrolysis of inosine and 22 kcal/mol for uridine. The uridine binding is exothermic by about 23 kcal/mol, and inosine binding by 12 kcal/mol
RihA bound to inhibitor 3,4-diaminophenyl-D-iminoribitol, hanging drop vapour diffusion method, 8 mg/ml RihA in 50 mM HEPES, pH 7.2, 150 mM NaCl is mixed with a 5:1 molar excess of 3,4-diaminophenyl-D-iminoribitol, solubilized in 50 mM HEPES, pH 7.2, and incubated at 4°C for 3 hours, the protein/inhibitor complex is mixed with an equal volume of a precipitant solution containing 25% PEG 4000, 0.1 M sodium acetate, pH 5.0, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement
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purified detagged recombinant enzyme, hanging drop vapour diffusion method, 10 mg/ml protein in 20 mM HEPES, pH 7.4, 150 mM NaCl, is mixed with precipitant solution, 25°C, equilibration versus reservoir solution containing 100 mM Tris-HCl, pH 8.5, 200 mM NaCl, 25% w/v PEG 3350, cryoprotection by 25% glycerol, X-ray diffraction structure determination and analysis at 1.7 A resolution
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purified recombinant enzyme in complex with D-ribose, hanging drop vapour diffusion method, 10 mg/ml protein in 10 mM Tris, pH 7.0, 25 mM NaCl, and 500 mM D-ribose, is mixed with an equal volume of precipitant solution containing 24% 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, pH 5.0, and 500 mM D-ribose, 20°C, 1 week, X-ray diffraction structure determination and analysis at 1.78 A resolution
to 1.53 A resolution, orthorhombic space group I222
crystal structure is determined at 1.6 A resolution. The enzyme is crystallized using the hanging drop vapor diffusion method by mixing an equal amount of protein and a precipitant solution, composed of 100 mM bicine (pH 9) and 1.5 M ammonium sulfate
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H239A
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dramatic increase in Km for uridine, unchanged kcat
H82N
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small increase in Km, increase in kcat
Q227A
the mutation causes an increase of kcat for uridine and inosine
Q227F
the mutation causes an increase of kcat for uridine and inosine
Q227Y
the mutation has a strong, enhancing effect on the hydrolysis of inosine, and the catalytic efficiency for the purinic substrate is increased by a factor of 7.6
T223A
the mutation does not improve significantly the catalytic efficiency of YeiK toward inosine
T223F
the mutation does not improve significantly the catalytic efficiency of YeiK toward inosine
T223F/Q227Y
the mutant shows a 2fold increase in catalytic efficiency toward inosine
T223Y
the mutation does not affect the specificity of the enzyme toward inosine or uridine
T227A
the mutation does not improve significantly the catalytic efficiency of YeiK toward inosine
T227F
the mutation does not improve significantly the catalytic efficiency of YeiK toward inosine
T223Y/Q227Y
the mutant displays a catalytic efficiency toward inosine that is more than 50fold increased compared to that of wild type enzyme
T223Y/Q227Y
contrary to wild-type, mutant is able to process inosine
additional information
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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
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
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