2.7.1.B20: broad specificity nucleoside kinase
This is an abbreviated version!
For detailed information about broad specificity nucleoside kinase, go to the full flat file.
Word Map on EC 2.7.1.B20
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2.7.1.B20
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deoxycytidine
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deoxyadenosine
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deoxyguanosine
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deoxyribonucleoside
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dm-dnk
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e-5-2-bromovinyl-2'-deoxyuridine
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prpp-amido
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2.7.1.74
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antiherpetic
- 2.7.1.B20
- deoxycytidine
- deoxyadenosine
- deoxyguanosine
- deoxyribonucleoside
- dm-dnk
-
e-5-2-bromovinyl-2'-deoxyuridine
-
prpp-amido
-
2.7.1.74
-
antiherpetic
Reaction
Synonyms
BTH_I1158, MJ0406, MjNK, NTP:nucleoside kinase, nucleoside kinase, PFK-B sugar kinase, Ta0880
ECTree
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Metals Ions
Metals Ions on EC 2.7.1.B20 - broad specificity nucleoside kinase
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Co2+
Mg2+
Mn2+
Ni2+
enzyme activity requires the presence of divalent cations. Mn2+ is the most efficient, followed by Mg2+, Ni2+ and Co2+
Co2+
enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%)
Co2+
kinase activity is observed with Mg2+ and Co2+ and to a lesser degree with Mn2+
enzyme activity requires the presence of divalent cations. Mn2+ is the most efficient, followed by Mg2+, Ni2+ and Co2+. Maximum activity is attained when the ATP/Mg2+ concentration ratio is 0.5
Mg2+
enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%)
Mg2+
there are two magnesium-binding sites per subunit: one Mg2+ (MO6) is coordinated octahedrally by six water molecules and is located between adenosine and AMPPNP in the active site and one Mg2+ (MO5) is coordinated by five water molecules and is positioned in the interface between the dimers in the crystal
Mg2+
kinase activity is observed with Mg2+ and Co2+ and to a lesser degree with Mn2+
enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%)
Mn2+
kinase activity is observed with Mg2+ and Co2+ and to a lesser degree with Mn2+
enzyme activity requires the presence of divalent cations. Mn2+ is the most efficient, followed by Mg2+, Ni2+ and Co2+
Ni2+
enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%)