Information on EC 2.7.1.B20 - broad specificity nucleoside kinase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.7.1.B20
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
broad specificity nucleoside kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NTP + nucleoside = NDP + nucleoside 5'-phosphate
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
NTP:nucleoside 5'-phosphotransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2'-deoxyadenosine
ADP + 2'-deoxyadenosine 5'-phosphate
show the reaction diagram
ATP + adenosine
ADP + adenosine 5'-phosphate
show the reaction diagram
ATP + cytidine
ADP + CMP
show the reaction diagram
ATP + cytidine
ADP + cytidine 5'-phosphate
show the reaction diagram
catalytic efficiency with cytidine is 45% relative to guanosine
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-
?
ATP + guanosine
ADP + GMP
show the reaction diagram
ATP + guanosine
ADP + guanosine 5'-phosphate
show the reaction diagram
ATP + inosine
ADP + IMP
show the reaction diagram
ATP + inosine
ADP + inosine 5'-phosphate
show the reaction diagram
ATP + mizoribine
ADP + mizoribine 5'-phosphate
show the reaction diagram
i.e. 5-hydroxy-1-beta-D-ribofuranosyl-1H-imidazole-4-carboxamide. Phosphate donor specificity in the order of relaltive velocity: ITP (200%), TTP (130%), GTP (125%), ATP (100%), CTP (45%), UTP (40%)
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-
?
ATP + ribavirin
ADP + ribavirin 5'-phosphate
show the reaction diagram
ATP + uridine
ADP + uridine 5'-phosphate
show the reaction diagram
CTP + inosine
CDP + inosine 5'-phosphate
show the reaction diagram
phosphate donor specificity in the order of relaltive velocity: ITP (200%), TTP (130%), GTP (125%), ATP (100%), CTP (45%), UTP (40%)
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-
?
GTP + cytidine
GDP + CMP
show the reaction diagram
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relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
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-
?
GTP + guanosine
GDP + GMP
show the reaction diagram
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relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
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-
?
GTP + guanosine
GDP + guanosine 5'-phosphate
show the reaction diagram
phosphoryl donor specificity in order of decreasing Vmax: GTP > ATP > ITP. The catalytic efficiency of GTP is 39% compared to that of ATP
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-
?
GTP + inosine
GDP + IMP
show the reaction diagram
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relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
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-
?
GTP + inosine
GDP + inosine 5'-phosphate
show the reaction diagram
phosphate donor specificity in the order of relaltive velocity: ITP (200%), TTP (130%), GTP (125%), ATP (100%), CTP (45%), UTP (40%)
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-
?
ITP + cytidine
IDP + CMP
show the reaction diagram
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relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
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-
?
ITP + guanosine
IDP + GMP
show the reaction diagram
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relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
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-
?
ITP + guanosine
IDP + guanosine 5'-phosphate
show the reaction diagram
phosphoryl donor specificity in order of decreasing Vmax: GTP > ATP > ITP
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-
?
ITP + inosine
IDP + IMP
show the reaction diagram
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relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
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-
?
ITP + inosine
IDP + inosine 5'-phosphate
show the reaction diagram
phosphate donor specificity in the order of relaltive velocity: ITP (200%), TTP (130%), GTP (125%), ATP (100%), CTP (45%), UTP (40%)
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-
?
TTP + inosine
TDP + inosine 5'-phosphate
show the reaction diagram
phosphate donor specificity in the order of relaltive velocity: ITP (200%), TTP (130%), GTP (125%), ATP (100%), CTP (45%), UTP (40%)
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-
?
UTP + inosine
UDP + inosine 5'-phosphate
show the reaction diagram
phosphate donor specificity in the order of relaltive velocity: ITP (200%), TTP (130%), GTP (125%), ATP (100%), CTP (45%), UTP (40%)
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine
concentrations above 0.1 mM lead to reduction in enzyme activity
Inosine
concentrations above 0.1 mM lead to reduction in enzyme activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
2'-deoxyadenosine
pH 7.0, 37°C
0.001 - 0.02
adenosine
0.0469 - 3
ATP
0.000411 - 0.017
cytidine
0.185
GTP
pH 8.0, 22°C
0.000208 - 0.46
guanosine
0.000712 - 0.15
Inosine
0.87
mizoribine
pH 7.0, 37°C
0.79
ribavirin
pH 7.0, 37°C
1.7
uridine
pH 7.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.084
adenosine
Thermoplasma acidophilum
Q9HJT3
pH 8.0, 22°C
0.17
ATP
Thermoplasma acidophilum
Q9HJT3
pH 8.0, 22°C, cosubstrate: inosine
0.064
cytidine
Thermoplasma acidophilum
Q9HJT3
pH 8.0, 22°C
0.27
GTP
Thermoplasma acidophilum
Q9HJT3
pH 8.0, 22°C
0.072
guanosine
Thermoplasma acidophilum
Q9HJT3
pH 8.0, 22°C
0.16
Inosine
Thermoplasma acidophilum
Q9HJT3
pH 8.0, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.84
2'-deoxyadenosine
Burkholderia thailandensis
Q2SZE4
pH 7.0, 37°C
357
6.05 - 74.9
adenosine
122
3.7 - 16
ATP
4
156
cytidine
Thermoplasma acidophilum
Q9HJT3
pH 8.0, 22°C
372
1.4
GTP
Thermoplasma acidophilum
Q9HJT3
pH 8.0, 22°C
37
0.24 - 345
guanosine
296
80 - 215
Inosine
167
0.04
mizoribine
Burkholderia thailandensis
Q2SZE4
pH 7.0, 37°C
5001
0.08
ribavirin
Burkholderia thailandensis
Q2SZE4
pH 7.0, 37°C
1304
0.28
uridine
Burkholderia thailandensis
Q2SZE4
pH 7.0, 37°C
261
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1 - 8.2
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50% of maximal activity at pH 6.1 and at pH 8.2
6.2 - 7.8
pH 6.2: about 60% of maximal activity, pH 7.8: about 75% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32804
2 * 32804, calculated from sequence
33000
2 * 33000, SDS-PAGE, crystal structure
68000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 32804, calculated from sequence; 2 * 33000, SDS-PAGE, crystal structure
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized as the apoenzyme as well as in complex with an ATP analogue and Mg2+. The latter crystal form is also soaked with D-fructose 6-phosphate. Synchrotron-radiation data are collected to 1.70 A for the apoenzyme crystals and 1.93 A for the complex crystals. All crystals exhibit orthorhombic symmetry. The apoenzyme crystals contain one monomer per asymmetric unit whereas the complex crystals contain a dimer
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sitting- and hanging-drop vapour diffusion methods, three-dimensional structures of the unliganded enzyme and a complex of the enzyme, an ATP analogue and adenosine are determined to 1.7 and 1.9 A resolution, respectively. In the crystal structure of the MjNK complex, subunit A adopts a closed conformation and subunit B an open conformation. In subunit A all substrates and Mg2+ are observed, whereas in subunit B only the ATP analogue can be clearly identified in the electron density
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sitting nanodroplet vapor diffusion method, crystal structure of Ta0880, determined at 1.91 A resolution reveals a dimer with each monomer composed of an alpha/beta/alpha sandwich domain and a smaller lid domain
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
37°C, 3 h, stable
697882
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
pH 7.0, 20 min, stable
60
pH 7.0, 20 min, 60% loss of activity
70
pH 7.0, 20 min, complete inactivation
90
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melting temperature
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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functionally overexpressed in Rhodococcus erythropolis