BRENDA - Enzyme Database
show all sequences of 2.7.4.8

Molecular cloning, expression, characterization and mutation of Plasmodium falciparum guanylate kinase

Kandeel, M.; Nakanishi, M.; Ando, T.; El-Shazly, K.; Yosef, T.; Ueno, Y.; Kitade, Y.; Mol. Biochem. Parasitol. 159, 130-133 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
DNA and amino acid sequence determination and analysis, sequence comparison
Plasmodium falciparum
Engineering
Amino acid exchange
Commentary
Organism
D74A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Plasmodium falciparum
E101D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Plasmodium falciparum
N103D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Plasmodium falciparum
Y76F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Plasmodium falciparum
Inhibitors
Inhibitors
Commentary
Organism
Structure
AMP
10-15% inhibition at 5 mM
Plasmodium falciparum
CMP
10-15% inhibition at 5 mM
Plasmodium falciparum
dAMP
10-15% inhibition at 5 mM
Plasmodium falciparum
dCMP
10-15% inhibition at 5 mM
Plasmodium falciparum
dGMP
competitive versus GMP and mixed-type versus ATP
Plasmodium falciparum
EDTA
85% inhibition at 3 mM
Plasmodium falciparum
additional information
no inhibition by TMP and by 2-mercaptoethanol up to 5 mM
Plasmodium falciparum
UMP
10-15% inhibition at 5 mM
Plasmodium falciparum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics of wild-type and mutant enzymes
Plasmodium falciparum
0.0222
-
GMP
wild-type enzyme
Plasmodium falciparum
0.0592
-
GMP
mutant Y76F
Plasmodium falciparum
0.0616
-
GMP
mutant E101D
Plasmodium falciparum
0.0731
-
dGMP
mutant Y76F
Plasmodium falciparum
0.0746
-
dGMP
wild-type enzyme
Plasmodium falciparum
0.1816
-
dGMP
mutant D74A
Plasmodium falciparum
0.1894
-
dGMP
mutant E101D
Plasmodium falciparum
0.1933
-
GMP
mutant D74A
Plasmodium falciparum
0.2265
-
GMP
mutant N103D
Plasmodium falciparum
0.2364
-
dGMP
mutant N103D
Plasmodium falciparum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + GMP
Plasmodium falciparum
-
ADP + GDP
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Plasmodium falciparum
-
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
30
-
with substrates ATP and dGMP
Plasmodium falciparum
750
-
with substrate ATP and GMP
Plasmodium falciparum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + AMP
very low activity with AMP
700079
Plasmodium falciparum
ADP + ADP
-
-
-
?
ATP + dGMP
low activity, dGMP acts also as inhibitor
700079
Plasmodium falciparum
ADP + dGDP
-
-
-
?
ATP + GMP
-
700079
Plasmodium falciparum
ADP + GDP
-
-
-
?
additional information
no activity with CMP, dTMP, dAMP, dCMP, and UMP
700079
Plasmodium falciparum
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2
8
dGMP
mutant Y76F
Plasmodium falciparum
26.5
-
dGMP
mutant E101D
Plasmodium falciparum
26.8
-
dGMP
mutant N103D
Plasmodium falciparum
33.1
-
dGMP
mutant D74A
Plasmodium falciparum
43
-
dGMP
wild-type enzyme
Plasmodium falciparum
848
-
GMP
mutant E101D
Plasmodium falciparum
946
-
GMP
wild-type enzyme
Plasmodium falciparum
1032
-
GMP
mutant Y76F
Plasmodium falciparum
1080
-
GMP
mutant N103D
Plasmodium falciparum
1121
-
GMP
mutant D74A
Plasmodium falciparum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
7.8
-
Plasmodium falciparum
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
9
-
Plasmodium falciparum
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.148
-
dGMP
versus GMP
Plasmodium falciparum
0.4
-
dGMP
versus ATP
Plasmodium falciparum
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, sequence comparison
Plasmodium falciparum
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D74A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Plasmodium falciparum
E101D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Plasmodium falciparum
N103D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Plasmodium falciparum
Y76F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Plasmodium falciparum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
AMP
10-15% inhibition at 5 mM
Plasmodium falciparum
CMP
10-15% inhibition at 5 mM
Plasmodium falciparum
dAMP
10-15% inhibition at 5 mM
Plasmodium falciparum
dCMP
10-15% inhibition at 5 mM
Plasmodium falciparum
dGMP
competitive versus GMP and mixed-type versus ATP
Plasmodium falciparum
EDTA
85% inhibition at 3 mM
Plasmodium falciparum
additional information
no inhibition by TMP and by 2-mercaptoethanol up to 5 mM
Plasmodium falciparum
UMP
10-15% inhibition at 5 mM
Plasmodium falciparum
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.148
-
dGMP
versus GMP
Plasmodium falciparum
0.4
-
dGMP
versus ATP
Plasmodium falciparum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics of wild-type and mutant enzymes
Plasmodium falciparum
0.0222
-
GMP
wild-type enzyme
Plasmodium falciparum
0.0592
-
GMP
mutant Y76F
Plasmodium falciparum
0.0616
-
GMP
mutant E101D
Plasmodium falciparum
0.0731
-
dGMP
mutant Y76F
Plasmodium falciparum
0.0746
-
dGMP
wild-type enzyme
Plasmodium falciparum
0.1816
-
dGMP
mutant D74A
Plasmodium falciparum
0.1894
-
dGMP
mutant E101D
Plasmodium falciparum
0.1933
-
GMP
mutant D74A
Plasmodium falciparum
0.2265
-
GMP
mutant N103D
Plasmodium falciparum
0.2364
-
dGMP
mutant N103D
Plasmodium falciparum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + GMP
Plasmodium falciparum
-
ADP + GDP
-
-
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
30
-
with substrates ATP and dGMP
Plasmodium falciparum
750
-
with substrate ATP and GMP
Plasmodium falciparum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + AMP
very low activity with AMP
700079
Plasmodium falciparum
ADP + ADP
-
-
-
?
ATP + dGMP
low activity, dGMP acts also as inhibitor
700079
Plasmodium falciparum
ADP + dGDP
-
-
-
?
ATP + GMP
-
700079
Plasmodium falciparum
ADP + GDP
-
-
-
?
additional information
no activity with CMP, dTMP, dAMP, dCMP, and UMP
700079
Plasmodium falciparum
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2
8
dGMP
mutant Y76F
Plasmodium falciparum
26.5
-
dGMP
mutant E101D
Plasmodium falciparum
26.8
-
dGMP
mutant N103D
Plasmodium falciparum
33.1
-
dGMP
mutant D74A
Plasmodium falciparum
43
-
dGMP
wild-type enzyme
Plasmodium falciparum
848
-
GMP
mutant E101D
Plasmodium falciparum
946
-
GMP
wild-type enzyme
Plasmodium falciparum
1032
-
GMP
mutant Y76F
Plasmodium falciparum
1080
-
GMP
mutant N103D
Plasmodium falciparum
1121
-
GMP
mutant D74A
Plasmodium falciparum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
7.8
-
Plasmodium falciparum
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
9
-
Plasmodium falciparum
Other publictions for EC 2.7.4.8
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
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)
738145
Jain
Insights into open/closed conf ...
Homo sapiens
Eur. Biophys. J.
45
81-89
2016
-
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1
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1
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1
1
1
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2
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1
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1
1
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1
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1
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1
1
1
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1
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3
3
-
-
-
739667
Zhang
Mechanistic insight into the f ...
Saccharomyces cerevisiae
Sci. Rep.
5
8405
2015
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1
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1
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2
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1
1
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738614
Nomura
Diversity in guanosine 3,5-bis ...
Arabidopsis thaliana, Bacillus subtilis, Escherichia coli, Oryza sativa Japonica Group, Oryza sativa Japonica Group Nipponbare, Pisum sativum, Saccharomyces cerevisiae, Synechococcus elongatus
J. Biol. Chem.
289
15631-15641
2014
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7
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9
4
9
7
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11
-
20
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7
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3
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11
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7
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4
7
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7
1
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1
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9
9
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1
9
1
4
9
9
-
11
-
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-
9
-
5
-
-
11
-
9
-
-
4
9
-
-
-
-
10
14
-
4
4
739240
Gupta
Purification and characterizat ...
Brugia malayi
Parasitology
141
1341-1352
2014
-
-
1
-
-
-
8
2
-
2
2
1
-
3
-
-
1
1
-
-
-
-
6
2
1
1
-
2
1
1
-
1
-
-
-
-
-
1
1
-
-
-
-
8
-
2
-
2
2
1
-
-
-
1
-
-
-
-
6
2
1
1
-
2
1
1
-
-
-
1
1
-
2
2
737590
Mori
Crystal structure of the guany ...
Homo sapiens
Biochem. Biophys. Res. Commun.
435
334-338
2013
-
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1
1
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2
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3
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1
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1
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1
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2
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1
-
-
-
-
-
-
-
-
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-
-
-
-
-
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3
3
-
-
-
723031
Dembowski
Alternative splicing of a nove ...
Homo sapiens
J. Nucleic Acids
2012
816237
2012
-
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-
-
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1
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3
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1
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721551
Mertlikova-Kaiserova
Point mutations in human guany ...
Homo sapiens
Biochem. Pharmacol.
82
131-138
2011
-
-
1
-
1
-
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2
-
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1
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2
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2
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1
1
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1
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1
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2
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1
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2
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-
1
1
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-
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-
1
1
1
1
-
-
722117
Zhu
Guanylate kinase domains of th ...
Homo sapiens, Rattus norvegicus
EMBO J.
30
4986-4997
2011
-
-
2
2
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2
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2
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2
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2
2
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723014
Kandeel
Binding dynamics and energetic ...
Plasmodium falciparum
J. Mol. Recognit.
24
322-332
2011
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1
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2
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700079
Kandeel
Molecular cloning, expression, ...
Plasmodium falciparum
Mol. Biochem. Parasitol.
159
130-133
2008
-
-
1
-
4
-
8
11
-
-
-
1
-
2
-
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-
-
-
-
2
-
4
-
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10
1
1
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2
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1
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4
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8
2
11
-
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1
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2
-
4
-
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10
1
1
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700475
Gardoni
Postsynaptic density-membrane ...
Homo sapiens, Mus musculus, Rattus norvegicus
Neuroscience
158
324-333
2008
-
-
1
-
1
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-
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4
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4
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3
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3
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6
-
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5
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1
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1
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1
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4
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4
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3
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6
-
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5
-
1
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-
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700950
Gonzalez-Gutierrez
The guanylate kinase domain of ...
Rattus norvegicus
Proc. Natl. Acad. Sci. USA
105
14198-14203
2008
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1
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1
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1
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2
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1
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2
2
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672643
Choi
Guanylate kinase, induced fit, ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Biophys. J.
92
1651-1658
2007
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1
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1
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2
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3
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1
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1
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7
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1
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1
1
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1
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2
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1
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7
-
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675510
Sumita
Synaptic scaffolding molecule ...
Rattus norvegicus
J. Neurochem.
100
154-166
2007
-
-
1
-
-
-
-
-
3
-
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1
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2
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-
-
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5
-
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1
1
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1
-
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3
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1
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5
-
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1
1
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-
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-
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-
676138
Reese
The guanylate kinase domain of ...
Rattus norvegicus
Nat. Struct. Mol. Biol.
14
155-163
2007
-
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1
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1
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1
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1
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1
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1
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1
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1
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1
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1
1
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700744
Sugimoto
The rice nuclear gene, VIRESCE ...
Oryza sativa
Plant J.
52
512-527
2007
-
-
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1
-
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6
-
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3
-
5
-
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-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
6
-
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
671155
El Omari
Structure of Staphylococcus au ...
Staphylococcus aureus
Acta Crystallogr. Sect. F
F62
949-953
2006
-
-
-
1
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
672440
Hible
Crystal structures of GMP kina ...
Escherichia coli
Biochimie
88
1157-1164
2006
-
1
-
1
-
-
1
-
-
-
-
2
-
3
-
-
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
1
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
673847
Willmon
A guanylate kinase/HSV-1 thymi ...
Homo sapiens, Mus musculus
Gene Ther.
13
1309-1312
2006
-
-
-
-
-
-
-
2
-
-
-
6
-
2
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
6
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
675894
Abergel
Impact of the excision of an a ...
Rickettsia conorii
Mol. Biol. Evol.
23
2112-2122
2006
-
-
-
-
-
-
-
2
-
1
-
-
-
7
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
662657
Hible
Calorimetric and crystallograp ...
Escherichia coli
J. Mol. Biol.
352
1044-1059
2005
-
-
1
1
-
-
-
-
-
-
2
2
-
6
-
-
1
-
1
-
-
1
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
2
-
-
-
1
1
-
-
1
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
660690
Stolworthy
A novel Escherichia coli strai ...
Escherichia coli, Escherichia coli TS202A
Anal. Biochem.
322
40-47
2003
-
1
-
-
-
-
-
-
-
-
-
2
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
662176
Olsen
Functional analysis of the nuc ...
Rattus norvegicus, Saccharomyces cerevisiae
J. Biol. Chem.
278
6873-6878
2003
-
-
2
-
3
-
-
3
-
-
-
2
-
3
-
-
2
-
-
-
2
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
3
-
-
-
-
3
-
-
-
2
-
-
-
2
-
-
2
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642707
Sekulic
Structural characterization of ...
Mus musculus
J. Biol. Chem.
277
30236-30243
2002
-
-
-
1
-
-
-
-
-
-
2
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642705
Blaszczyk
Crystal structure of unligated ...
Saccharomyces cerevisiae
J. Mol. Biol.
307
247-257
2001
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642706
Stolworthy
The mouse guanylate kinase dou ...
Mus musculus
Protein Eng.
14
903-909
2001
-
-
1
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
6
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
745202
Adams
Key role for sulfur in peptid ...
Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
642704
Miller
Phosphorylation of ganciclovir ...
Homo sapiens, Sus scrofa
Nucleosides Nucleotides Nucleic Acids
19
341-356
2000
-
-
-
-
-
-
-
4
-
-
-
-
-
4
-
-
-
-
-
2
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
2
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642703
Prinz
Binding of nucleotides to guan ...
Homo sapiens
J. Biol. Chem.
274
35337-35342
1999
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642702
Zhang
Structural and functional role ...
Saccharomyces cerevisiae
J. Biol. Chem.
272
19343-19350
1997
-
-
-
-
1
-
2
4
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
1
-
-
2
4
4
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642700
Brady
Cloning, characterization, and ...
Homo sapiens, Mus musculus
J. Biol. Chem.
271
16734-16740
1996
-
-
2
-
-
-
-
1
-
-
2
-
-
6
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642701
Li
Kinetic and thermodynamic char ...
Saccharomyces cerevisiae
J. Biol. Chem.
271
28038-28044
1996
-
-
1
-
1
-
4
7
-
1
-
-
-
4
-
-
-
-
-
-
-
-
3
-
-
-
-
3
-
-
-
-
4
-
-
-
-
1
-
-
1
-
-
4
4
7
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
642692
Stehle
-
Temperature-dependent space-gr ...
Saccharomyces cerevisiae
Acta Crystallogr. Sect. B Struct. Sci.
B48
546-548
1992
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642696
Stehle
Refined structure of the compl ...
Saccharomyces cerevisiae
J. Mol. Biol.
224
1127-1141
1992
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642697
NavÚ
9-(Phosphonoalkyl)guanine deri ...
Sus scrofa
Arch. Biochem. Biophys.
295
253-257
1992
-
-
-
-
-
-
3
3
-
1
-
1
-
1
-
-
-
-
-
1
-
-
6
-
1
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
3
2
3
-
1
-
1
-
-
-
-
-
1
-
-
6
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
642693
Stehle
Three-dimensional structure of ...
Saccharomyces cerevisiae
J. Mol. Biol.
211
249-254
1990
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642694
Le Floc'h
-
Purification and properties of ...
Helianthus tuberosus
Plant Physiol. Biochem.
28
191-201
1990
-
-
-
-
-
-
6
2
1
4
1
-
-
1
-
-
1
-
-
1
-
1
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
2
1
4
1
-
-
-
-
1
-
1
-
1
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
642691
Berger
Guanylate kinase from Saccharo ...
Saccharomyces cerevisiae
Eur. J. Biochem.
184
433-443
1989
-
-
-
1
-
-
-
-
-
1
2
-
-
2
-
-
1
-
-
-
1
2
5
1
1
-
-
-
1
1
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
1
2
-
-
-
-
1
-
-
1
2
5
1
1
-
-
-
1
1
-
1
-
-
-
-
-
-
642561
Hall
Purification and properties of ...
Bos taurus
Eur. J. Biochem.
161
551-556
1986
-
-
-
-
-
-
1
2
1
5
2
1
-
2
-
-
1
-
-
3
2
-
10
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
1
5
2
1
-
-
-
1
-
3
2
-
10
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
642698
Boehme
Phosphorylation of the antivir ...
Homo sapiens
J. Biol. Chem.
259
12346-12349
1984
-
-
-
-
-
1
2
1
-
1
-
-
-
2
-
-
1
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
1
-
2
8
1
-
1
-
-
-
-
-
1
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642690
Moriguchi
Purification and properties of ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
662
165-167
1981
-
-
-
-
-
1
-
2
-
3
1
-
-
2
-
-
1
-
-
-
1
3
5
-
1
-
2
-
1
1
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
2
-
3
1
-
-
-
-
1
-
-
1
3
5
-
1
-
2
-
1
1
2
-
-
-
-
-
-
-
642687
Oeschger
Guanylate kinase from Escheric ...
Escherichia coli, Escherichia coli B / ATCC 11303
Methods Enzymol.
51
473-482
1978
-
-
-
-
-
1
-
6
-
5
1
-
-
178
-
-
1
-
-
-
1
1
8
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
6
-
5
1
-
-
-
-
1
-
-
1
1
8
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
642688
Agarwal
Guanylate kinases from human e ...
Homo sapiens, Rattus norvegicus, Sus scrofa
Methods Enzymol.
51
483-490
1978
-
-
-
-
-
-
12
14
-
20
-
-
-
3
-
-
3
-
-
4
1
3
37
-
3
-
2
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
12
-
14
-
20
-
-
-
-
-
3
-
4
1
3
37
-
3
-
2
-
-
-
1
2
-
-
-
-
-
-
642695
Agarwal
Inhibition of rat hepatic guan ...
Rattus norvegicus
Biochem. Pharmacol.
24
791-795
1975
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
1
-
-
2
-
-
4
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
2
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
642685
Shimono
Metabolism of deoxyribonucleot ...
Bos taurus, Rattus norvegicus
Eur. J. Biochem.
19
256-263
1971
-
-
-
-
-
3
4
2
-
22
-
-
-
2
-
-
1
-
-
8
-
3
27
-
-
-
1
-
2
2
-
-
2
-
-
-
-
-
-
-
-
3
-
4
2
2
-
22
-
-
-
-
-
1
-
8
-
3
27
-
-
-
1
-
2
2
-
-
-
-
-
-
-
-
642686
Buccino
Partial purification and prope ...
Rattus norvegicus
Arch. Biochem. Biophys.
132
49-61
1969
1
-
-
-
-
2
10
-
-
8
1
-
-
1
-
-
1
-
-
2
1
2
15
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
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2
-
10
-
-
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8
1
-
-
-
-
1
-
2
1
2
15
-
1
-
-
-
-
-
-
-
-
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-
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-
642699
Hiraga
Nucleoside monophosphokinases ...
Escherichia coli, Escherichia coli JE24F+
Biochim. Biophys. Acta
114
416-418
1966
-
-
-
-
-
-
-
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1
-
-
-
-
3
-
-
1
-
-
-
-
1
4
-
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-
-
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-
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1
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-
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1
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1
4
-
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642684
Griffith
The partial purification of de ...
Mus musculus
Biochim. Biophys. Acta
108
114-124
1965
1
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3
3
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8
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1
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1
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1
1
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4
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1
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1
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2
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1
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3
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3
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8
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1
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1
1
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4
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1
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1
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2
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