BRENDA - Enzyme Database
show all sequences of 3.6.1.25

A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism

Delvaux, D.; Murty, M.R.; Gabelica, V.; Lakaye, B.; Lunin, V.V.; Skarina, T.; Onopriyenko, O.; Kohn, G.; Wins, P.; De Pauw, E.; Bettendorff, L.; J. Biol. Chem. 286, 34023-34035 (2011)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escherichia coli BL21(DE3) cells
Nitrosomonas europaea
Crystallization (Commentary)
Crystallization (Commentary)
Organism
hanging drop vapor diffusion method, selenomethionine-substituted protein, using 3.5 M sodium formate as a precipitation agent and 0.1 M Bis-Tris propane buffer, pH 7.0, at 20°C
Nitrosomonas europaea
Engineering
Protein Variants
Commentary
Organism
K52R
the His-tagged mutant loses 90-99% of its activity (catalytic efficiency is at least 1000times lower) compared to the wild type enzyme. Mn2+ does not induce a significant activation of this mutant
Nitrosomonas europaea
K85A
the His-tagged mutant is about 10times less active than the wild type enzyme, but the optimal conditions for activity are essentially the same. The mutant is more strongly activated by Mn2+ than by Mg2+, and the inhibitory effects of Ca2+ and Zn2+ are less pronounced
Nitrosomonas europaea
K8A
the His-tagged mutant remains highly active with tripolyphosphate as substrate and Mg2+ as activator, with a catalytic efficiency close to that of the recombinant wild type enzyme
Nitrosomonas europaea
Inhibitors
Inhibitors
Commentary
Organism
Structure
Cd2+
-
Nitrosomonas europaea
Cu2+
-
Nitrosomonas europaea
Zn2+
complete inhibition at 0.005 mM
Nitrosomonas europaea
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.021
-
tripolyphosphate
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.04
-
tripolyphosphate
His-tagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.058
-
tripolyphosphate
His-tagged wild type enzyme, at pH 7.1 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.1
-
tripolyphosphate
untagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.191
-
tripolyphosphate
His-tagged mutant enzyme K52R, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.39
-
tripolyphosphate
His-tagged mutant enzyme K8A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.72
-
tripolyphosphate
His-tagged mutant enzyme K85A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.8
-
ATP
His-tagged wild type enzyme, at pH 8.1 and 50°C, in the presence of 10 mM Mn2+
Nitrosomonas europaea
1.2
-
ATP
His-tagged mutant enzyme K8A, at pH 10.1 and 50°C, in the presence of 10 mM Mn2+
Nitrosomonas europaea
2.6
-
tripolyphosphate
His-tagged mutant enzyme K85A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
74
-
tripolyphosphate
His-tagged mutant enzyme K8A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
Co2+ is a better activator than Mn2+, although the maximum activity is less than 10% that measured in the presence of 5 mM Mg2+
Nitrosomonas europaea
Mg2+
the enzyme hydrolyzes tripolyphosphate with high catalytic efficiency in the presence of 5 mM Mg2+
Nitrosomonas europaea
Mn2+
very poor substituent for Mg2+ in the pH range 7.0-10, but there is a significant Mn2+-dependent activity at pH 10.0-10.5. Half-maximum activation is obtained at 0.4 mM
Nitrosomonas europaea
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
19000
-
2 * 19000, SDS-PAGE
Nitrosomonas europaea
Organism
Organism
UniProt
Commentary
Textmining
Nitrosomonas europaea
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
His-Trap column chromatography, gel filtration
Nitrosomonas europaea
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ATP + H2O
low affinity
719965
Nitrosomonas europaea
?
-
-
-
?
additional information
the enzyme has low affinity for CTP, ATP or thiamine triphosphate. Nucleoside triphosphatase activity is negligible in the presence of 5 mM Mg2+, but a small activity is observed in the presence of 1 mM Mn2+, in particular with GTP. Guanosine 5’-tetraphosphate and long chain polyphosphate (containing about 65 phosphate residues) are not hydrolyzed. The enzyme has no adenylyl cyclase activity
719965
Nitrosomonas europaea
?
-
-
-
?
tripolyphosphate + H2O
very good substrate with Mg2+ as activator. The enzyme has a strong preference for linear tripolyphosphate compared with cyclic trimetaphosphate and to the linear tetraphosphate
719965
Nitrosomonas europaea
diphosphate + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 19000, SDS-PAGE
Nitrosomonas europaea
Synonyms
Synonyms
Commentary
Organism
inorganic triphosphatase
-
Nitrosomonas europaea
triphosphate tunnel metalloenzyme
-
Nitrosomonas europaea
TTM
-
Nitrosomonas europaea
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
55
-
Nitrosomonas europaea
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.28
-
tripolyphosphate
His-tagged mutant enzyme K8A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.36
-
ATP
His-tagged wild type enzyme, at pH 8.1 and 50°C, in the presence of 10 mM Mn2+
Nitrosomonas europaea
0.98
-
tripolyphosphate
His-tagged mutant enzyme K52R, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
3.96
-
ATP
His-tagged mutant enzyme K8A, at pH 10.1 and 50°C, in the presence of 10 mM Mn2+
Nitrosomonas europaea
10
-
tripolyphosphate
His-tagged mutant enzyme K85A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
21
-
tripolyphosphate
His-tagged mutant enzyme K85A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
60
-
tripolyphosphate
His-tagged wild type enzyme, at pH 7.1 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
76
-
tripolyphosphate
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
288
-
tripolyphosphate
His-tagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
887
-
tripolyphosphate
His-tagged mutant enzyme K8A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
7900
-
tripolyphosphate
untagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.7
-
around pH 9.7
Nitrosomonas europaea
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.0015
-
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
Zn2+
0.01
-
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
Cd2+
0.02
-
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
Cu2+
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Nitrosomonas europaea
Crystallization (Commentary) (protein specific)
Crystallization
Organism
hanging drop vapor diffusion method, selenomethionine-substituted protein, using 3.5 M sodium formate as a precipitation agent and 0.1 M Bis-Tris propane buffer, pH 7.0, at 20°C
Nitrosomonas europaea
Engineering (protein specific)
Protein Variants
Commentary
Organism
K52R
the His-tagged mutant loses 90-99% of its activity (catalytic efficiency is at least 1000times lower) compared to the wild type enzyme. Mn2+ does not induce a significant activation of this mutant
Nitrosomonas europaea
K85A
the His-tagged mutant is about 10times less active than the wild type enzyme, but the optimal conditions for activity are essentially the same. The mutant is more strongly activated by Mn2+ than by Mg2+, and the inhibitory effects of Ca2+ and Zn2+ are less pronounced
Nitrosomonas europaea
K8A
the His-tagged mutant remains highly active with tripolyphosphate as substrate and Mg2+ as activator, with a catalytic efficiency close to that of the recombinant wild type enzyme
Nitrosomonas europaea
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.0015
-
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
Zn2+
0.01
-
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
Cd2+
0.02
-
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
Cu2+
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cd2+
-
Nitrosomonas europaea
Cu2+
-
Nitrosomonas europaea
Zn2+
complete inhibition at 0.005 mM
Nitrosomonas europaea
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.021
-
tripolyphosphate
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.04
-
tripolyphosphate
His-tagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.058
-
tripolyphosphate
His-tagged wild type enzyme, at pH 7.1 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.1
-
tripolyphosphate
untagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.191
-
tripolyphosphate
His-tagged mutant enzyme K52R, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.39
-
tripolyphosphate
His-tagged mutant enzyme K8A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.72
-
tripolyphosphate
His-tagged mutant enzyme K85A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.8
-
ATP
His-tagged wild type enzyme, at pH 8.1 and 50°C, in the presence of 10 mM Mn2+
Nitrosomonas europaea
1.2
-
ATP
His-tagged mutant enzyme K8A, at pH 10.1 and 50°C, in the presence of 10 mM Mn2+
Nitrosomonas europaea
2.6
-
tripolyphosphate
His-tagged mutant enzyme K85A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
74
-
tripolyphosphate
His-tagged mutant enzyme K8A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
Co2+ is a better activator than Mn2+, although the maximum activity is less than 10% that measured in the presence of 5 mM Mg2+
Nitrosomonas europaea
Mg2+
the enzyme hydrolyzes tripolyphosphate with high catalytic efficiency in the presence of 5 mM Mg2+
Nitrosomonas europaea
Mn2+
very poor substituent for Mg2+ in the pH range 7.0-10, but there is a significant Mn2+-dependent activity at pH 10.0-10.5. Half-maximum activation is obtained at 0.4 mM
Nitrosomonas europaea
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
19000
-
2 * 19000, SDS-PAGE
Nitrosomonas europaea
Purification (Commentary) (protein specific)
Commentary
Organism
His-Trap column chromatography, gel filtration
Nitrosomonas europaea
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ATP + H2O
low affinity
719965
Nitrosomonas europaea
?
-
-
-
?
additional information
the enzyme has low affinity for CTP, ATP or thiamine triphosphate. Nucleoside triphosphatase activity is negligible in the presence of 5 mM Mg2+, but a small activity is observed in the presence of 1 mM Mn2+, in particular with GTP. Guanosine 5’-tetraphosphate and long chain polyphosphate (containing about 65 phosphate residues) are not hydrolyzed. The enzyme has no adenylyl cyclase activity
719965
Nitrosomonas europaea
?
-
-
-
?
tripolyphosphate + H2O
very good substrate with Mg2+ as activator. The enzyme has a strong preference for linear tripolyphosphate compared with cyclic trimetaphosphate and to the linear tetraphosphate
719965
Nitrosomonas europaea
diphosphate + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 19000, SDS-PAGE
Nitrosomonas europaea
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
55
-
Nitrosomonas europaea
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.28
-
tripolyphosphate
His-tagged mutant enzyme K8A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
0.36
-
ATP
His-tagged wild type enzyme, at pH 8.1 and 50°C, in the presence of 10 mM Mn2+
Nitrosomonas europaea
0.98
-
tripolyphosphate
His-tagged mutant enzyme K52R, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
3.96
-
ATP
His-tagged mutant enzyme K8A, at pH 10.1 and 50°C, in the presence of 10 mM Mn2+
Nitrosomonas europaea
10
-
tripolyphosphate
His-tagged mutant enzyme K85A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
21
-
tripolyphosphate
His-tagged mutant enzyme K85A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
60
-
tripolyphosphate
His-tagged wild type enzyme, at pH 7.1 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
76
-
tripolyphosphate
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
288
-
tripolyphosphate
His-tagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
887
-
tripolyphosphate
His-tagged mutant enzyme K8A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
7900
-
tripolyphosphate
untagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.7
-
around pH 9.7
Nitrosomonas europaea
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.45
-
ATP
His-tagged wild type enzyme, at pH 8.1 and 50°C, in the presence of 10 mM Mn2+
Nitrosomonas europaea
3.3
-
ATP
His-tagged mutant enzyme K8A, at pH 10.1 and 50°C, in the presence of 10 mM Mn2+
Nitrosomonas europaea
4
-
tripolyphosphate
His-tagged mutant enzyme K85A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
5.1
-
tripolyphosphate
His-tagged mutant enzyme K52R, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
29
-
tripolyphosphate
His-tagged mutant enzyme K85A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
190
-
tripolyphosphate
His-tagged mutant enzyme K8A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
2300
-
tripolyphosphate
His-tagged mutant enzyme K8A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
3300
-
tripolyphosphate
His-tagged wild type enzyme, at pH 7.1 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
3600
-
tripolyphosphate
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
7200
-
tripolyphosphate
His-tagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
79000
-
tripolyphosphate
untagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.45
-
ATP
His-tagged wild type enzyme, at pH 8.1 and 50°C, in the presence of 10 mM Mn2+
Nitrosomonas europaea
3.3
-
ATP
His-tagged mutant enzyme K8A, at pH 10.1 and 50°C, in the presence of 10 mM Mn2+
Nitrosomonas europaea
4
-
tripolyphosphate
His-tagged mutant enzyme K85A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
5.1
-
tripolyphosphate
His-tagged mutant enzyme K52R, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
29
-
tripolyphosphate
His-tagged mutant enzyme K85A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
190
-
tripolyphosphate
His-tagged mutant enzyme K8A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
2300
-
tripolyphosphate
His-tagged mutant enzyme K8A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
3300
-
tripolyphosphate
His-tagged wild type enzyme, at pH 7.1 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
3600
-
tripolyphosphate
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
7200
-
tripolyphosphate
His-tagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
79000
-
tripolyphosphate
untagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Nitrosomonas europaea
Other publictions for EC 3.6.1.25
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
719965
Delvaux
A specific inorganic triphosph ...
Nitrosomonas europaea
J. Biol. Chem.
286
34023-34035
2011
-
-
1
1
3
-
3
11
-
3
1
-
-
7
-
-
1
-
-
-
-
-
3
1
3
1
-
-
11
1
-
-
-
-
-
3
-
-
1
-
1
3
-
3
3
-
11
-
3
1
-
-
-
-
1
-
-
-
-
3
1
1
-
-
11
1
-
-
-
-
-
-
-
11
11
669193
Perez Mato
Biochemical basis for the domi ...
Rattus norvegicus
J. Biol. Chem.
276
13803-13809
2001
-
-
1
-
2
-
-
6
-
-
2
-
-
3
-
-
1
-
-
1
12
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
6
-
-
2
-
-
-
-
1
-
1
12
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
210003
Yu
Structure-function analysis of ...
Vaccinia virus
J. Virol.
71
9837-9843
1997
-
-
-
-
-
-
-
-
-
-
1
1
-
8
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
210002
Trilisenko
Subcellular localization of en ...
Kitasatospora aureofaciens
Folia Microbiol. (Praha)
32
402-410
1987
-
-
-
-
-
-
1
-
1
-
-
1
-
4
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
210001
Kulalev
-
A comparative characterization ...
Neurospora crassa
Biochemistry (Moscow)
39
309-312
1974
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210000
Kulaev
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Localization of polyphosphatas ...
Neurospora crassa
Biochemistry (Moscow)
37
190-194
1972
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