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2.7.1.78: polynucleotide 5'-hydroxyl-kinase

This is an abbreviated version!
For detailed information about polynucleotide 5'-hydroxyl-kinase, go to the full flat file.

Word Map on EC 2.7.1.78

Reaction

ATP
+
5'-dephospho-DNA
=
ADP
 +
5'-phospho-DNA

Synonyms

5' end-specific RNA/DNA kinase, 5' polynucleotide kinase, 5'-hydroxyl polynucleotide kinase, 5'-hydroxyl polyribonucleotide kinase, 5'-hydroxyl RNA kinase, 5'-OH polynucleotide kinase, ATP:5'-dephosphopolynucleotide 5'-phosphatase, cleavage and polyadenylation factor I subunit, CLP1, Clp1-like protein, DNA 5'-hydroxyl kinase, DNA kinase, Grc3, HD-Pnk, HEAB, hPNKP, kinase (phosphorylating), polynucleotide 5'-hydroxyl, More, mPNKP, Nol9, PALF, PhoClp1, PNK, Pnk1, PNKP, polynucleotide 5'-hydroxyl kinase (phosphorylating), polynucleotide 5'-hydroxyl-kinase, polynucleotide kinase, polynucleotide kinase and aprataxin-like forkhead-associated, polynucleotide kinase phosphatase, polynucleotide kinase-phosphatase, polynucleotide kinase/phosphatase, RNA-specific polynucleotide kinase, Rnl1, RPNK, T4 PNK, T4 polynucleotide kinase, T4 polynucleotide kinase/phosphatase, tRNA endonuclease complex, TSEN

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.78 polynucleotide 5'-hydroxyl-kinase

Engineering

Engineering on EC 2.7.1.78 - polynucleotide 5'-hydroxyl-kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D38E
site-directed mutagenesis, the mutant shows 6% of wild-type activity
D38N
site-directed mutagenesis, inactive mutant
H189D
-
mutation transforms enzyme into a Mn2+-dependent phosphodiesterase devoid of monoesterase activity. Phosphodiesterase activity of mutant is strictly specific for 2',3'-cyclic phosphates which it hydrolyzes to yield a 2'-NMP as the sole product
K21Q
site-directed mutagenesis, the mutant shows 100fold reduced activity compared to the wild-type enzyme
K21R
site-directed mutagenesis, the mutant shows 15fold reduced activity compared to the wild-type enzyme
K95A
site-directed mutagenesis, inactive mutant, the phenotype is benign
Q51A
the mutation reduces kinase specific activity about 3fold
R116A
the mutation elicits a 10fold increase in Km for ATP, but has little effect on the turnover number value leading to 83% of wild type activity
R41K
site-directed mutagenesis, the mutant shows about 65% reduced activity compared to the wild-type enzyme
R41Q
site-directed mutagenesis, the mutant shows 100fold reduced activity compared to the wild-type enzyme
S22T
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
S37A/T80A
the double mutation reduces kinase activity 50fold
T54A
the mutation reduces kinase specific activity about 3fold
V129A
the mutation reduces kinase specific activity about 3fold
Q51A
-
the mutation reduces kinase specific activity about 3fold
-
S37A/T80A
-
the double mutation reduces kinase activity 50fold
-
T54A
-
the mutation reduces kinase specific activity about 3fold
-
V129A
-
the mutation reduces kinase specific activity about 3fold
-
D171A
-
complete loss of activity
D173A
-
complete loss of activity
K127A
-
inactive
K138A/R35A
-
the mutant shows impaired nuclear localization as compared to the wild type enzyme
K378A
-
complete loss of activity
R140H
W331F
single mutant, 90% phosphatase activity
W402F
single mutant, 85% phosphatase activity
WFX402
mutant, all tryptophans except 402 are replaced by phenylalanine, 85% phosphatase activity
D169A
Kostyavirus CJW1
-
50% of wild-type activity with 37-mer oligodeoxyribonucleotide substrate, no reverse reaction
K15A
Kostyavirus CJW1
-
no enzymic activity in kinase reaction, 58% of wild-type activity in 3’-phosphates reaction
D175A
Omegavirus omega
-
60% of wild-type activity with 37-mer oligodeoxyribonucleotide substrate, 68% of wild-type activity with CMP substrate
K16A
Omegavirus omega
-
no enzymic activity
D73A
mutation abolishes activity
K49A
mutation reduces activity to 1% of the wild-type value
D254A
-
inactive
H73A
-
the mutant shows wild type activity
R257A
-
inactive
D254A
-
inactive
-
H73A
-
the mutant shows wild type activity
-
R257A
-
inactive
-
D165A
Tequatrovirus T4
-
site-directed mutagenesis, increased activity compared to the wild-type, no 3'-phosphatase activity remaining
D180A
Tequatrovirus T4
-
site-directed mutagenesis, slightly higher activity than the wild-type, reduced 3'-phosphatase activity
D250A
Tequatrovirus T4
-
site-directed mutagenesis, increased activity compared to the wild-type , reduced 3'-phosphatase activity
D254A
Tequatrovirus T4
-
site-directed mutagenesis, increased activity compared to the wild-type, nearly no 3'-phosphatase activity remaining
D278A
Tequatrovirus T4
-
site-directed mutagenesis, increased activity compared to the wild-type, no 3'-phosphatase activity remaining
G14D
Tequatrovirus T4
-
the mutation impairs the 5`-kinase activity of the enzyme in vivo as well as in vitro and leads to diminished processing at secondary sites of several RegB-cleaved transcripts
K125A
Tequatrovirus T4
-
site-directed mutagenesis, slightly higher activity than the wild-type
R122A
Tequatrovirus T4
-
site-directed mutagenesis, slightly higher activity than the wild-type, reduced 3'-phosphatase activity
R126A
Tequatrovirus T4
-
site-directed mutagenesis, highly reduced activity
R176A
Tequatrovirus T4
-
site-directed mutagenesis, increased activity compared to the wild-type, highly reduced 3'-phosphatase activity
R213A
Tequatrovirus T4
-
site-directed mutagenesis, increased activity compared to the wild-type, no 3'-phosphatase activity remaining
R229H
Tequatrovirus T4
-
the mutant shows slightly reduced wild type activity
R246A
Tequatrovirus T4
-
site-directed mutagenesis, increased activity compared to the wild-type, highly reduced 3'-phosphatase activity
R279A
Tequatrovirus T4
-
site-directed mutagenesis, increased activity compared to the wild-type, highly reduced 3'-phosphatase activity
R36A
Tequatrovirus T4
-
site-directed mutagenesis, similar activity than the wild-type
R38A
Tequatrovirus T4
-
site-directed mutagenesis, highly reduced activity, reduced 3'-phosphatase activity
S84A
Tequatrovirus T4
-
site-directed mutagenesis, slightly lower activity than the wild-type, reduced 3'-phosphatase activity
G14D
Tequatrovirus T4 K10
-
the mutation impairs the 5`-kinase activity of the enzyme in vivo as well as in vitro and leads to diminished processing at secondary sites of several RegB-cleaved transcripts
-
R229H
Tequatrovirus T4 K10
-
the mutant shows slightly reduced wild type activity
-
additional information