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2.7.1.21: thymidine kinase

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

Word Map on EC 2.7.1.21

Reaction

ATP
+
thymidine
=
ADP
 +
dTMP

Synonyms

2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase, beta-thymidine kinase-1, beta-thymidine kinase-2, calmodulin-binding protein, CaM-binding protein, CaMBP, CHV-TK, dThd kinase-1, dThd kinase-2, EC 2.7.1.75, EHV4-TK, FHV-TK, HSV-1 TK, HSV1-TK, kinase, deoxythymidine (phosphorylating), kinase, thymidine (phosphorylating), LMJF_21_1210, mitochondrial thymidine kinase, More, Mt-TK, TdR kinase, ThyB, thymidine kinase, thymidine kinase 1, thymidine kinase 2, thymidine kinase 2, mitochondrial, thymidine kinase I, thymidine kinase-1, thymidine kinase-2, thymidylate kinase, TK, TK-1, TK-2, TK1, TK1a, TK1b, TK2, type 1 thymidine kinase, type II thymidine kinase 1, UL23, VVTK

ECTree

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

Engineering

Engineering on EC 2.7.1.21 - thymidine kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L143A
-
the mutant shows reduced catalytic efficiency with thymidine compared to the wild type enzyme and exhibits activity towards deoxyguanosine
M42I
-
the mutation has a negative impact on enzyme activity with thymidine as the substrate, affecting both the Km (250fold increase) and the kcat (2fold increase) values
S182A
-
the mutant shows reduced catalytic efficiency with thymidine compared to the wild type enzyme and exhibits activity towards deoxyguanosine
S182T
-
the mutant shows reduced catalytic efficiency with thymidine compared to the wild type enzyme and exhibits activity towards deoxyguanosine
A167Y
Herpes simplex virus
-
heavily reduced ability to phosphorylate pyrimidine nucleosides, ability to phosphorylate ganciclovir and lobucavir is reduced 2fold
C336Y
Herpes simplex virus
-
acyclovir resistant, mutation affects ATP binding site
Q125D
Herpes simplex virus
-
increased Km for thymidine
Q125E
Herpes simplex virus
-
increased Km for thymidine
Q125N
Y101F
Herpes simplex virus
-
12fold increased Km for thymidine
H121N
similar subunit structure to wild-type enzyme, decreased enzyme activity
I212N
similar subunit structure to wild-type enzyme, less than 1% activity compared to wild-type
I59H
-
the mutant shows imcreased Km compared to the wild type enzyme
I59L
-
the mutant shows imcreased Km compared to the wild type enzyme
I59V
-
the mutant shows imcreased Km compared to the wild type enzyme
I59Y
-
the mutant shows decreased Km compared to the wild type enzyme
L124A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
M28A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
M28I
the mutation has a negative impact on enzyme activity with thymidine as the substrate, affecting both the Km (250fold increase) and the kcat (6fold increase) values. The mutant has no activity with deoxycytidine
S13D
-
site-directed mutagenesis, ATP-induced tetramerization is perturbed, mutant is less activated by ATP and shows reduced activity compared to the wild-type enzyme
T163S
the mutation results in a kinase with a 140fold lower Km for 3’-azido-3’-deoxythymidine
V106A
-
site-directed mutagenesis, mutant is similar to the wild-type enzyme in size, conformation and polarity, unaltered activity and oligomerization pattern
V106G
-
site-directed mutagenesis, mutant differs in size, conformation and polarity from the wild-type enzyme, reduced activity, permanent tetrameric form irrespective of the presence of ATP
V106H
-
site-directed mutagenesis, mutant differs in size, conformation and polarity from the wild-type enzyme, reduced activity, permanent tetrameric form irrespective of the presence of ATP
V106I
-
site-directed mutagenesis, mutant is similar to the wild-type enzyme in size, conformation and polarity, unaltered activity and oligomerization pattern
V106K
-
site-directed mutagenesis, mutant differs in size, conformation and polarity from the wild-type enzyme, reduced activity, permanent tetrameric form irrespective of the presence of ATP
V106L
-
site-directed mutagenesis, mutant differs in size, conformation and polarity from the wild-type enzyme, reduced activity, permanent tetrameric form irrespective of the presence of ATP
V106M
V106Q
-
site-directed mutagenesis, mutant differs in size, conformation and polarity from the wild-type enzyme, reduced activity, permanent tetrameric form irrespective of the presence of ATP
V106T
-
site-directed mutagenesis, mutant is similar to the wild-type enzyme in size, conformation and polarity, unaltered activity and oligomerization pattern
A175V
-
site-sirected mutagenesis, inactive mutant, mutation of residue 51 might in vivo be involved into generation of acyclovir resistance of HSV
D77N
-
site-sirected mutagenesis, mutant activity is slightly increased compared to the wild-type enzyme
E83K
-
site-sirected mutagenesis, inactive mutant, mutation of residue 51 might in vivo be involved into generation of acyclovir resistance of HSV
H13I
P03176
the mutant shows strongly increased Km compared to the wild type enzyme
H13I/Y127F
P03176
the mutant shows increased Km compared to the wild type enzyme
P12N
P03176
the mutant shows increased Km compared to the wild type enzyme
P12N/H13I
P03176
the mutant shows decreased Km compared to the wild type enzyme
P12N/H13I/Y127F
P03176
the mutant shows strongly increased Km compared to the wild type enzyme
P12N/Y127F
P03176
the mutant shows strongly increased Km compared to the wild type enzyme
R51W
-
site-sirected mutagenesis, inactive mutant, mutation of residue 51 might in vivo be involved into generation of acyclovir resistance of HSV
G294A
-
site-directed mutagenesis, about 80% reduced activity compared to the wild-type enzyme, no activity with TTP as cofactor
G294V
-
site-directed mutagenesis, nearly inactive mutant, no ATP binding
K297E
-
site-directed mutagenesis, nearly inactive mutant, no ATP binding
K297Q
-
site-directed mutagenesis, nearly inactive mutant, no ATP binding
K297R
-
site-directed mutagenesis, about 90% reduced activity compared to the wild-type enzyme, prefers GTP as cofactor, no activity with TTP as cofactor
T298A
-
site-directed mutagenesis, about 90% reduced activity compared to the wild-type enzyme
T298S
-
site-directed mutagenesis, about 20% reduced activity compared to the wild-type enzyme
H121N
-
the mutant has less than 7% kinase activity compared to the wild type enzyme
additional information