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2.7.1.20: adenosine kinase

This is an abbreviated version!
For detailed information about adenosine kinase, go to the full flat file.

Word Map on EC 2.7.1.20

Reaction

ATP
+
adenosine
=
ADP
 +
AMP

Synonyms

adenosine kinase (phosphorylating), ADK, AdK-L, AdK-S, Ado kinase, AdoK, AK, ATP:adenosine 5'-phosphotransferase, CpAK, hADK, kinase, adenosine (phosphorylating), LdAdK, MGG_06270, Rv2202c, Tb927.6.2360, TbAK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.20 adenosine kinase

Engineering

Engineering on EC 2.7.1.20 - adenosine kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E229A
complete loss of activity, decrease in the alpha-helix content
E229R
complete loss of activity, significant decrease in the alpha-helix content
F303A
complete loss of activity, decrease in the alpha-helix content
G280A
mutation has no significant influence on the enzymatic activity compared with that of wild-type enzyme, slight decrease in the alpha-helix content
G280D
mutation has no significant influence on the enzymatic activity compared with that of wild-type enzyme, slight decrease in the alpha-helix content
G68A
mutation results in significant decrease in activity
S201A
mutation significantly increases the alpha-helix content of BmADK and its activity
S201D
significant decrease in the alpha-helix content
S201R
significant decrease in the alpha-helix content
F338A
mutant displays reduced susceptibility to non-nucleoside inhibitors, while maintaining comparable affinity for nucleoside inhibitors to the wild-type enzyme
H107A
mutant displays reduced susceptibility to non-nucleoside inhibitors, while maintaining comparable affinity for nucleoside inhibitors to the wild-type enzyme
K341A
mutant displays reduced susceptibility to non-nucleoside inhibitors, while maintaining comparable affinity for nucleoside inhibitors to the wild-type enzyme
Q74A
mutant displays reduced susceptibility to non-nucleoside inhibitors, while maintaining comparable affinity for nucleoside inhibitors to the wild-type enzyme
Q74A/F338A
mutant displays reduced susceptibility to non-nucleoside inhibitors, while maintaining comparable affinity for nucleoside inhibitors to the wild-type enzyme
Q78A
mutant displays reduced susceptibility to non-nucleoside inhibitors, while maintaining comparable affinity for nucleoside inhibitors to the wild-type enzyme
D16E
-
specific activity at the highest attainable adenosine concentration is approximately 2.5-fold lower than that of the wild-type enzyme. Non-saturation kinetics of the D16E mutant are indicative of weaker binding
D16N
-
kcat/Km value for adenosine is lowered more than 1000fold. Mutation does not significantly affected the apparent Km for ATP
D16V
-
kcat/Km value for adenosine is lowered more than 1000fold. Mutation does not significantly affected the apparent Km for ATP
D299A
-
site-directed mutagenesis, inactive mutant, slightly reduced AMP binding ability compared to the wild-type enzyme
G62D
-
site-directed mutagenesis, inactive mutant, no AMP binding ability
R131A
R69A
-
site-directed mutagenesis, reduced reduced catalytic activity and AMP binding ability compared to the wild-type enzyme
R69K
-
site-directed mutagenesis, reduced catalytic activity and slightly reduced AMP binding ability compared to the wild-type enzyme
R69K/R131A
-
site-directed mutagenesis, highly reduced catalytic activity and AMP binding ability compared to the wild-type enzyme
D310A
catalytically deficient mutant that looses responsiveness to K+
D310P
catalytically deficient mutant that looses responsiveness to K+
additional information