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Information on EC 2.7.7.7 - DNA-directed DNA polymerase and Organism(s) Homo sapiens and UniProt Accession P06746

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.7 DNA-directed DNA polymerase
IUBMB Comments
Catalyses DNA-template-directed extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. Requires a primer, which may be DNA or RNA. See also EC 2.7.7.49 RNA-directed DNA polymerase.
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This record set is specific for:
Homo sapiens
UNIPROT: P06746
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
dna polymerase alpha, dna polymerase beta, dna polymerase iii, pol beta, klenow fragment, dna polymerase delta, taq dna polymerase, pol delta, pol alpha, dna polymerase gamma, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DNA polymerase beta
-
deoxynucleate polymerase
-
-
-
-
deoxyribonucleate nucleotidyltransferase
-
-
-
-
deoxyribonucleic acid duplicase
-
-
-
-
deoxyribonucleic acid polymerase
-
-
-
-
deoxyribonucleic duplicase
-
-
-
-
deoxyribonucleic polymerase
-
-
-
-
deoxyribonucleic polymerase I
-
-
-
-
DNA duplicase
-
-
-
-
DNA nucleotidyltransferase
-
-
-
-
DNA nucleotidyltransferase (DNA-directed)
-
-
-
-
DNA Pol lambda
-
-
DNA polmerase beta
-
-
-
-
DNA polymerase
DNA polymerase alpha
DNA polymerase beta
-
-
DNA polymerase delta
-
-
DNA polymerase epsilon
DNA polymerase eta
DNA polymerase gamma
DNA polymerase I
DNA polymerase II
-
-
-
-
DNA polymerase III
-
-
-
-
DNA polymerase iota
DNA polymerase kappa
DNA polymerase lambda
-
-
DNA polymerase mu
DNA polymerase ny
-
-
DNA replicase
-
-
-
-
DNA-dependent DNA polymerase
-
-
-
-
duplicase
-
-
-
-
Klenow fragment
mitochondrial DNA polymerase
-
-
mtDNA replicase
-
nucleotidyltransferase, deoxyribonucleate
-
-
-
-
pol alpha
pol beta
pol delta
POl epsilon
-
isozyme
Pol eta
Pol gamma
Pol I
-
-
pol iota
pol kappa
pol kappaDELTAC
-
truncated form of isozyme pol kappa
Pol lambda
Pol mu
Pol ny
-
-
Pol theta
-
isozyme
Pol zeta
-
isozyme
POLD4
-
smallest subunit of DNA polymerase delta
Polepsilon
Q07864; Q9NR33; P56282; Q9NRF9
-
POLG
-
-
poliota
poly iota
-
-
Rec1
-
-
sequenase
-
-
-
-
Taq DNA polymerase
-
-
-
-
Taq Pol I
-
-
-
-
Tca DNA polymerase
-
-
-
-
translesion DNA synthesis polymerase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn = diphosphate + DNAn+1
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
deoxynucleoside-triphosphate:DNA deoxynucleotidyltransferase (DNA-directed)
Catalyses DNA-template-directed extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. Requires a primer, which may be DNA or RNA. See also EC 2.7.7.49 RNA-directed DNA polymerase.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-90-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
8-oxodGTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
dGTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
r8-oxo-GTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
relative to correct dGTP insertion, r8-oxo-GTP insertion efficiency opposite dC and dA is reduced more than 250000fold and 4000fold, respectively. Insertion of r8-oxo-GTP is less efficient than 8-oxodGTP by 700- and 4300fold opposite dA and dC, respectively
-
-
?
rGTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
2-hydroxy-2'-deoxyadenosine 5'-triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
DNA polymerase eta incorporates 2-hydroxy-2'-deoxyadenosine 5'-triphosphate opposite template G during DNA synthesis
-
-
?
8-hydroxy-2'-deoxyguanosine 5'-triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
DNA polymerase eta incorporates 8-hydroxy-2'-deoxyguanosine 5'-triphosphate opposite template A and slightly opposite template C during DNA synthesis
-
-
?
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
the template-dependent polymerase that can repair non-complementary DNA double strand breaks with unpaired 3' primer termini by nonhomologous end joining. Its role is to fill short gaps arising as intermediates in the process of V(D)J recombination and during processing of accidental double strand breaks
-
-
?
dATP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
with activated calf thymus DNA
-
-
?
dCTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
dGTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
with activated calf thymus DNA
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
the template-dependent polymerase that can repair non-complementary DNA double strand breaks with unpaired 3' primer termini by nonhomologous end joining. Its role is to fill short gaps arising as intermediates in the process of V(D)J recombination and during processing of accidental double strand breaks
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
-
pols beta, iota and zeta exhibit maximal activity under conditions of moderate NaCl concentrations of 20-60 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NSC-666715
potent, small molecular weight inhibitor of DNA polymerase beta, blocks Pol-beta-directed single-nucleotide- and long-patch-base excisison repair
(2E)-2-(3-nitro-4-[[6-(trifluoromethyl)pyridin-3-yl]sulfanyl]benzylidene)-5-thioxo-1,3-thiazolidin-4-one
-
-
(2E)-2-(4-chloro-3-ethylbenzylidene)-5-thioxo-1,3-thiazolidin-4-one
-
-
(2E)-2-(pentafluorobenzylidene)-5-thioxodihydrothiophen-3(2H)-one
-
-
(2E)-2-[4-(2-hydroxyethyl)-3-nitrobenzylidene]-5-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(4-chloro-3-nitrobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[3-bromo-4-[(4-fluorobenzyl)oxy]benzylidene]-1,3-thiazolidine-2,4-dione
-
-
(5Z)-5-[3-bromo-4-[(4-fluorophenyl)sulfanyl]benzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[3-nitro-4-(pyridin-3-ylsulfanyl)benzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-(4-methylphenoxy)-3-nitrobenzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-(cyclohexylsulfanyl)-3-nitrobenzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-[(4-bromophenyl)sulfanyl]-3-nitrobenzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-[(4-chlorophenyl)sulfanyl]-3-nitrobenzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-[(4-fluorobenzyl)oxy]-3-nitrobenzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-[(4-fluorobenzyl)oxy]benzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-[(4-methylphenyl)sulfanyl]-3-nitrobenzylidene]-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(9-adenylmethylcarbonyl)-4-aminobutyl triphosphate
-
fully competitive with respect to the nucleotide substrate dTTP, inhibits wild-type enzyme and mutant enzyme Y505A
(biphenylcarbonyl)-4-oxobutyl triphosphate
(E)-enedione
-
-
1,2,3,4-tetrahydro-5-methoxynaphthalene-1,4-diol
-
i.e. nodulisporol. Strong inhibition of pol lambda, but does not influence the activities of mammalian pols alpha to kappa, and shows no effect on the activities of plant pols alpha and beta, prokaryotic pols, and other DNA metabolic enzymes such as calf terminal deoxynucleotidyl transferase, human immunodeficiency virus type-1 (HIV-1) reverse transcriptase, human telomerase, T7 RNA polymerase, and bovine deoxyribonuclease I
1,3-bis[2-chloroethyl]-2-nitrosourea
-
-
1-deoxyrubralactone
-
potent inhibitor of isozymes pol kappa, pol lambda, pol iota, and pol eta, but does not inhibit DNA polymerase isozymes pol delta, pol epsilon, and pol gamma
10-epi-pyragonicin
-
-
19-epi-jimenezin
-
-
2',3'-dideoxy-ATP
-
poor inhibitor
2-(p-n-Butylanilino)-2'-deoxyadenosine 5'-triphosphate
2-butylanilino-dATP
-
potent and highly selective inhibitor
2-methoxy-4-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl 2,4-dichlorobenzoate
-
-
2-methoxy-4-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl 3-bromobenzoate
-
-
2-thiomethyl-6-phenyl-4-(4'-hydroxybutyl)-1,2,4,-triazole (5,1-C)(1,2,4)triazine-7-one triphosphate
3,4-dihydro-4-hydroxy-8-methoxynaphthalen-1(2H)-one
-
i.e. nodulisporone. Strong inhibition of pol lambda, but does not influence the activities of mammalian pols alpha to kappa, and shows no effect on the activities of plant pols alpha and beta, prokaryotic pols, and other DNA metabolic enzymes such as calf terminal deoxynucleotidyl transferase, human immunodeficiency virus type-1 (HIV-1) reverse transcriptase, human telomerase, T7 RNA polymerase, and bovine deoxyribonuclease I
3,5-dimethyl-8-methoxy-3,4-dihydroisocoumarin
-
-
4-chloromercuribenzoic acid
-
-
4-chlorophenyl 2,4-dinitrophenyl sulfide
-
-
4-hydroxy-5-methyl-3-tetradecyl-dihydrofuran-2(3H)-one
-
-
4-[(4-methylphenyl)sulfanyl]-3-nitrobenzaldehyde
-
-
4-[(Z)-(2,4-dioxo-1,3-thiazolidin-5-ylidene)methyl]-2-methoxyphenyl 3-bromobenzoate
-
-
4-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl 2-chlorobenzoate
-
-
5-(5-nitro-2-[[6-(trifluoromethyl)pyridin-3-yl]sulfanyl]benzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-[2-(cyclohexylsulfanyl)-5-nitrobenzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
5-[2-[(4-chlorophenyl)sulfanyl]-5-nitrobenzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
5-[2-[(4-methylphenyl)sulfanyl]-5-nitrobenzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
adefovir diphosphate
-
-
Allicin
-
-
alliin
-
-
aphidicolin
ara-ATP
-
-
aurintricarboxylic acid
-
potent nanomolar inhibitor of pol beta, pol iota, and pol zeta
Ca2+
-
polymerase alpha
Carbonyldiphosphonate
cholesterol hemisuccinate
cloretazine
-
i.e. 1,2-bis[methylsulfonyl]-1-[2-chloroethyl]-2-[(methylamino)carbonyl]hydrazine
diallyl pentasulfide
-
-
diallyl tetrasulfide
-
-
diallyl trisulfide
-
-
Dideoxynucleoside 5'-triphosphate
Dideoxythymidine triphosphate
dimethyl sulfoxide
-
stimulates DNA polymerase alpha and delta, inhibits human DNA polymerase epsilon
ellagic acid
-
potent nanomolar inhibitor of pol beta, pol iota, and pol zeta
epigallocatechin gallate
-
-
gemcitabine
-
i.e. 2'-deoxy-2',2'-difluorocytidine, when gemcitabine is encountered as a template base DNA polymerase gamma pauses at the lesion and one downstream position but eventually elongates the primer to full-length product, these pauses are because of a 1000fold decrease in nucleotide incorporation efficiency
hymenoic acid
-
specific inhibitor of human DNA polymerase lambda, non-competitive inhibition with respect to both the DNA template-primer and the dNTP, i.e trans-4-[(1'E,5'S)-5'-carboxy-1'-methyl-1'-hexenyl]cyclohexanecarboxylic acid, does not influence the activities of the other mammalian pols alpha, gamma, delta, epsilon, eta, iota, and kappa, and also shows no effect even on the activity of pol beta
jimenezin
-
-
lamivudine triphosphate
-
-
Li+
-
polymerase alpha
Mg2+
-
DNA polymerase alpha: free Mg2+ competes with primer for enzyme binding, dramatic inhibition at Mg2+ concentration above the optimum
muconin
-
-
N-(2,4-dinitro-5-fluorophenyl)-2-aminoethyl triphosphate
-
inhibition of mutant enzyme Y505A, inactive against wild-type enzyme
N-(2,4-dinitro-5-fluorophenyl)-4-aminobutyl triphosphate
-
fully competitive with respect to the nucleotide substrate dTTP, inhibits wild-type enzyme and mutant enzyme Y505A
N-(2,4-dinitro-5-imidazolylphenyl)-2-aminoethyl triphosphate
-
inhibition of mutant enzyme Y505A, inactive against wild-type enzyme
N-(2,4-dinitro-5-imidazolylphenyl)-4-aminobutyl triphosphate
-
inhibition of mutant enzyme Y505A, inactive against wild-type enzyme
N-(2,4-dinitrophenyl)-4-aminobutyl triphosphate
-
fully competitive with respect to the nucleotide substrate dTTP, inhibits wild-type enzyme and mutant enzyme Y505A
N-(benzyloxycarbonyl)-4-aminobutyl triphosphate
N-ethylmaleimide
N-[6-N-(2,4-dinitrophenyl)aminohexanoyl]-2-aminoethyl triphosphate
-
inhibition of mutant enzyme Y505A, inactive against wild-type enzyme
N2-(p-n-butylphenyl)-2'-deoxyguanosine 5'-triphosphate
N2-CH2(6-benzo[a]pyrenyl)guanine
-
severely blocks activity
N2-CH2(9-anthracenyl)guanine
-
severely blocks activity, frequencies of dATP misinsertion and extension beyond mispairs are proportionally increased, great decrease in pre-steady-state kinetic burst rate. 2.6fold decrease in dCTP binding affinity and increased DNA substrate binding affinity
Oosporein
-
50% inhibition at 0.61 mM
pamoic acid
-
pol beta inhibitor
plakevulin A
-
-
pyragonicin
-
-
pyranicin
-
potent inhibitor
rhodanines
-
most potent inhibitors for DNA Pol lambda, they are up to 10times less active against the highly similar DNA polymerase beta, structure-activity relationships, overview. 5-Arylidene-2,4-thiazolidinediones are class I rhodanines, rhodanine class II has members of carbohydrazides, and class III contains a common 2,4-pentadione substructure element
-
Salt
-
concentrations above 50 mM inhibit: human KB cell polymerase alpha
single-stranded DNA
-
inhibition of polymerase alpha, competitive with respect to activated DNA substrate
stavudine triphosphate
-
-
talaroflavone
-
-
tenofovir diphosphate
-
-
untenone A
-
-
vitamin K3
-
more than 80% inhibition of pol gamma at 0.03 mM, does not affect other human DNA polymerase isozymes
zidovudine triphosphate
-
-
[3-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenoxy]acetic acid
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dimethyl sulfoxide
-
stimulates DNA polymerase alpha and delta, inhibits human DNA polymerase epsilon
FEN1
-
stimulates strand displacement activity, DEN1 processes nicked DNA, thus removing a barrier to Pol lambda DNA synthesis. It results in a one-nucleotide gapped DNA molecule that is a favorite substrate of Pol lambda
-
PCNA
-
stimulates strand displacement activity
-
Polymerase alpha accessory factors
-
overview
-
proliferating cell nuclear antigen
-
Replication factor A
-
RF-A, multisubunit single-stranded DNA-binding protein, functions as an auxiliary protein for both polymerases alpha and delta, required for initiation and elongation stages of in vitro SV40 DNA replication
-
Replication factor C
-
RF-C, multisubunit protein complex with primer/template binding and DNA-dependent ATPase activity, has a profound effect on leading-strand DNA synthesis
-
spermidine
-
up to 10 mM, polymerase beta
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00249 - 0.00792
dCTP
0.00118
deoxynucleoside triphosphate
-
DNA polymerase lambda, in 50 mM Tris-HCl (pH 7.5), 1 mM dithiothreitol, 50% (v/v) glycerol, and 0.1 mM EDTA, at 37°C
0.175 - 0.211
dTTP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0028 - 0.0038
(9-adenylmethylcarbonyl)-4-aminobutyl triphosphate
0.0004 - 0.0048
(biphenylcarbonyl)-4-oxobutyl triphosphate
0.0188
2',3'-dideoxy-ATP
-
-
0.001
2-butylanilino-dATP
-
-
0.0018 - 0.068
2-thiomethyl-6-phenyl-4-(4'-hydroxybutyl)-1,2,4,-triazole (5,1-C)(1,2,4)triazine-7-one triphosphate
0.00271
adefovir diphosphate
-
-
0.00065
aphidicolin
-
-
0.0506
lamivudine triphosphate
-
-
0.0144
N-(2,4-dinitro-5-fluorophenyl)-2-aminoethyl triphosphate
-
mutant enzyme Y505A
0.0031 - 0.0065
N-(2,4-dinitro-5-fluorophenyl)-4-aminobutyl triphosphate
0.0005
N-(2,4-dinitro-5-imidazolylphenyl)-2-aminoethyl triphosphate
-
mutant enzyme Y505A
0.0154
N-(2,4-dinitro-5-imidazolylphenyl)-4-aminobutyl triphosphate
-
mutant enzyme Y505A
0.0012 - 0.0035
N-(2,4-dinitrophenyl)-4-aminobutyl triphosphate
0.0016 - 0.07
N-(benzyloxycarbonyl)-4-aminobutyl triphosphate
0.0091
N-[6-N-(2,4-dinitrophenyl)aminohexanoyl]-2-aminoethyl triphosphate
-
mutant enzyme Y505A
0.0569
stavudine triphosphate
-
-
0.00618
tenofovir diphosphate
-
-
additional information
additional information
-
Allium sativum extract has an KI value of 0.0112 mM using DNA polymerase lambda, in 50 mM Tris-HCl (pH 7.5), 1 mM dithiothreitol, 50% (v/v) glycerol, and 0.1 mM EDTA, at 37°C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011 - 0.1
(2E)-2-(3-nitro-4-[[6-(trifluoromethyl)pyridin-3-yl]sulfanyl]benzylidene)-5-thioxo-1,3-thiazolidin-4-one
0.0083 - 0.08
(5Z)-5-[3-bromo-4-[(4-fluorophenyl)sulfanyl]benzylidene]-2-thioxo-1,3-thiazolidin-4-one
0.0093 - 0.1
(5Z)-5-[4-(4-methylphenoxy)-3-nitrobenzylidene]-2-thioxo-1,3-thiazolidin-4-one
0.0059 - 0.0644
(5Z)-5-[4-[(4-fluorobenzyl)oxy]benzylidene]-2-thioxo-1,3-thiazolidin-4-one
0.0037 - 0.0088
(E)-enedione
0.092 - 0.307
1,2-bis[methylsulfonyl]-1-[(methylamino)carbonyl]hydrazine
0.271 - 1.435
1,3-bis[2-chloroethyl]-2-nitrosourea
0.0598
1-deoxyrubralactone
Homo sapiens
-
in 50 mM Tris-HCl (pH 7.5) containing 1 mM dithiothreitol, 50% (v/v) glycerol, and 0.1 mM EDTA, at 37°C
0.049
3,5-dimethyl-8-methoxy-3,4-dihydroisocoumarin
Homo sapiens
-
-
0.0124 - 0.0888
4-[(Z)-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenyl 2-chlorobenzoate
0.0081 - 0.0429
5-[2-[(4-chlorophenyl)sulfanyl]-5-nitrobenzylidene]-2-thioxo-1,3-thiazolidin-4-one
0.01 - 0.0455
5-[2-[(4-methylphenyl)sulfanyl]-5-nitrobenzylidene]-2-thioxo-1,3-thiazolidin-4-one
0.0063 - 0.148
cholesterol hemisuccinate
0.074 - 0.387
cloretazine
0.146
diallyl trisulfide
Homo sapiens
-
DNA polymerase lambda, in 50 mM Tris-HCl (pH 7.5), 1 mM dithiothreitol, 50% (v/v) glycerol, and 0.1 mM EDTA, at 37°C
0.0038
epigallocatechin gallate
Homo sapiens
-
pH and temperature not specified in the publication
0.0917
hymenoic acid
Homo sapiens
-
-
0.0049 - 0.06
pamoic acid
0.066 - 0.179
plakevulin A
0.0023 - 0.0158
pyranicin
0.0043 - 0.057
untenone A
0.006
vitamin K3
Homo sapiens
-
isozyme pol gamma, in 50 mM Tris-HCl (pH 7.5) containing 1 mM dithiothreitol, 50% (v/v) glycerol, and 0.1 mM EDTA, at 37°C
additional information
additional information
Homo sapiens
-
Allium sativum extract has an IC50 of 0.0345 mM, using DNA polymerase lambda in 50 mM Tris-HCl (pH 7.5), 1 mM dithiothreitol, 50% (v/v) glycerol, and 0.1 mM EDTA, at 37°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.968
-
polymerase beta
3.43
-
polymerase alpha
5.33
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.9
-
assay at
7.5 - 8.5
-
KB cell DNA polymerase alpha
8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 9
-
pH 7.2: about 65% of maximal activity, pH 9.0: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
polymerase alpha
5.6 - 5.9
-
polymerase C, sucrose gradient, ampholytes pH 3-11
8.5
-
polymerase beta
9.3
-
polymerase N1, sucrose gradient, ampholytes pH 3-11
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug target
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DPOLB_HUMAN
335
0
38178
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
full-length Pol ny
100000 - 110000
-
mitochondrial enzyme
110000
120000
125000
-
1 * 125000 catalytic subunit + 1 * 48000 subunit of unknown function, DNA polymerase delta
140000
170000
190000
215000
-
DNA polymerase epsilon
265000 - 280000
-
dimeric form, polymerase alpha
40000
-
vertebrates, DNA polymerase beta
45000
-
1 * 45000 + 1 * 60000, SDS-PAGE, mitochondrial enzyme
48000
-
1 * 125000 catalytic subunit + 1 * 48000 subunit of unknown function, DNA polymerase delta
54000
-
1 * 54000 + 1 * 140000
60000
-
1 * 45000 + 1 * 60000, SDS-PAGE, mitochondrial enzyme
66000
-
1 * 66000 + 1 * 76000, DNA polymerase alpha, SDS-PAGE
76000
-
1 * 66000 + 1 * 76000, DNA polymerase alpha, SDS-PAGE
77100
-
N-terminally His6-tagged enzyme fragment Pol ny-77, gel filtration
78410
estimated from amino acid sequence
87000
-
1 * 155000-175000 + 1 * 87000, SDS-PAGE, polymerase alpha
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 140000, catalytic subunit, + 55000, accessory subunit, SDS-PAGE
dimer
heterotetramer
Q07864; Q9NR33; P56282; Q9NRF9
the human DNA polymerase epsilon holoenzyme is comprised of the catalytic p261 subunit and the noncatalytic p59, p17, and p12 small subunits. The presence of the p261 C-terminal domain (p261C) and the three small subunits increased the DNA binding affinity and the base substitution fidelity
monomer
tetramer
-
-
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pol beta-DNA complexes dGTP(beta-gamma CF2) and dGTP(beta-gamma CH2) are crystallized by sitting-drop vapor diffusion
sitting drop vapor diffusion, ternary polbeta:DNA:r8-oxo-GTP crystals
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y271G
the mutant is rationally designed to provide flexibility to the steric gate backbone carboxyl of Tyr-271 in pol beta
A329A
not meaningfully associated with breast cancer risk; more likely to respond to Pt-based chemotherapy
A467T
-
naturally occuring mutation, the mutation is the most common POLG mutation and has been found to be associated with all of the disease symptoms analyzed. The A467T pol gamma possesses only 4% of the wild-type DNA polymerase activity and is compromised for its ability to interact with the p55 accessory subunit
A471V
moderate decrease in activity
A957S
-
naturally occuring mutation, involved in autosomal dominant progressive external ophthalmoplegia, the mutation is associated with motiif B in the active site
D115A/E116A
-
catalytically inactive
D189G
impaired for extension step of TLS
D198A/E200A
-
site-directed mutagenesis in the exonuclease domain resulting in loss of exonuclease activity
D275A/E277A/D368A
Q07864; Q9NR33; P56282; Q9NRF9
mutation in the catalytic subunit, exonuclease-deficient variant
E1143G
-
naturally occuring mutation, that is a frequent cause of ataxia-neuropathy syndrome, and found in 4% of European populations
E200A
-
exonuclease-deficient mutant
E292K
E29K
decreased insertion opposite abasic site (2-20)
E419G
20fold decrease in kcat/Km on dG and 670fold decrease on N2-CH2-Anth-dG, extension defect
E430G
low activity on AP site
E449K
low activity on AP site, low fidelity
F155S
decreased activity on model abasic site
F192C
F506G
-
inactive mutant enzyme
F506R
-
complete loss of de novo DNA synthesis
G154E
decreased activity opposite model abasic site, pathogenic
G848S
-
naturally occuring mutation, involved in Alpers syndrome, the mutant shows compromised DNA binding ability that affects its overall functional efficiency
G923D
-
naturally occuring mutation, involved in autosomal dominant progressive external ophthalmoplegia, the mutation is associated with motiif B in the active site
L442F
low activity on AP site
L606G
-
site-directed mutagenesis, the mutant shows increased polymerase activity and slightly reduced exonuclease activity compared to the wild-type enzyme, mutant pol delta L606G is highly error prone, incorporating single noncomplementary nucleotides at a high frequency during DNA synthesis
L606K
-
site-directed mutagenesis, the mutant shows increased polymerase activity and reduced exonuclease activity compared to the wild-type enzyme, mutant pol delta L606K is extremely accurate, with a higher fidelity of single nucleotide incorporation by the active site than that of wild-type pol delta, it does not catalyze detectable nucleotide mis-insertion even with nucleotide concentrations as high as 4 mM, but pol delta L606K mutant is impaired in the bypass of DNA adducts
P169T
R219I
R246X
5-10fold less active with 8-oxo-dG-, N2-CH2-Anth-dG-, O6-Me-dG- and abasic-containing templates
R298H
R512W
decreased activity on undamaged and damaged DNA
R61A
the mutations decreases the ability of the enzyme to distinguish between a thymine-thymine dimer lesion and undamaged DNA. Mutation does not impact the global structure and equilibrium motions of DNA polymerase eta. Only local conformational changes around the mutation sites are observed
R61K
the mutations decreases the ability of the enzyme to distinguish between a thymine-thymine dimer lesion and undamaged DNA. Mutation does not impact the global structure and equilibrium motions of DNA polymerase eta. Only local conformational changes around the mutation sites are observed
R852C
-
naturally occuring mutation, involved in Alpers syndrome, the mutant shows compromised DNA binding ability that affects its overall functional efficiency
R853Q
-
naturally occuring mutation, involved in Alpers syndrome, the mutant shows compromised DNA binding ability that affects its overall functional efficiency
R943H
-
naturally occuring mutation, involved in autosomal dominant progressive external ophthalmoplegia, the mutation is associated with motiif B in the active site, the mutant retains less than 1% of the wild-type polymerase activity and displays a severe decrease in processivity
R964C
S423R
1.6fold more effcient than wild-type, 2fold increased DNA binding affinity, pathogenic
S62A
the mutations decreases the ability of the enzyme to distinguish between a thymine-thymine dimer lesion and undamaged DNA. Mutation does not impact the global structure and equilibrium motions of DNA polymerase eta. Only local conformational changes around the mutation sites are observed
S62L
the mutations decreases the ability of the enzyme to distinguish between a thymine-thymine dimer lesion and undamaged DNA. Mutation does not impact the global structure and equilibrium motions of DNA polymerase eta. Only local conformational changes around the mutation sites are observed
T44M
lesion-specific reduction in activity. Reduced activity with N2-CH2-Anth-dG, O6-Me-dG and abasic sites
T473A
decreased activity on undamaged and damaged DNA
T851A
-
naturally occuring mutation, involved in Alpers syndrome, the mutant shows compromised DNA binding ability that affects its overall functional efficiency
V130I
mutant has relaxed discrimination against the major groove adduct N6-furfuryl-dA
W748S
-
naturally occuring mutation that has intrinsic lower polymerase activity as well as a demonstrated lower affinity for DNA compared to the wild-type enzyme
W748S/E1143G
-
naturally occuring mutation, the E1143G single-nucleotide polymorphism can modulate the deleterious effect of the W748S mutation
Y432S
Y505A
Y955C
-
naturally occuring mutation, involved in autosomal dominant progressive external ophthalmoplegia, the mutation is associated with motiif B in the active site, the mutant retains less than 1% of the wild-type polymerase activity and displays a severe decrease in processivity, the mutation increases nucleotide misinsertion replication errors 10-100 fold in the absence of exonucleolytic proofreading
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
stable for 3 h in an optimized reaction buffer
32
mutant enzyme R298H
36.4
mutant enzyme Y432S
37
-
lifetime below 20 min
40.4
mutant enzyme F192C
41.9
melting temperature, wild-type
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, in concentrated form in the presence of sucrose and potassium phosphate, half-life: 1.5 months, human KB cell DNA polymerase alpha
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3 non-mitochondrial enzymes from KB cells: C, N1 and N2
-
DNA polymerase alpha
-
native Pol delta from UV-treated HeLa cells by immunoaffinity chromatography using anti-p125-agarose, recombinant Pol delta subunits from Sf9 insect cells by immunoaffinity and anion exchange chromatography, recombinant His-tagged or GST-tagged subunits from Escherichia coli by nickel affinity and glutathione affinity chromatography, respectively
-
nickel affinity column chromatography and SP column chromatography
polymerase delta
-
polymerase gamma
-
recombinant
-
recombinant C-terminally His6-tagged full-length p55 subunit from Escherichia coli strain BL21(DE3) to homogeneity, by nickel affinity chromatography, recombinant N-terminally His6-tagged wild-type enzyme and mutant R946C from Sf9 insect cells by nickel affinity chromatography, gel filtration, and anion exchange chromatography
-
recombinant refolded N-terminally His6-tagged enzyme fragment Pol ny-77 by gel filtration, dialysis, and heparin affinity chromatography, recombinant soluble His6-tagged enzyme fragment Pol ny-77 from Escherichia coli by nickel affinity chrmatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli
the Y271G mutation is overexpressed in BL21-CodonPlus (DE3)-RP Escherichia coli
catalytic subunit of DNA polymerase delta
catalytic subunits of wild-type and exonuclease-deficient mutant
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Sf9 cells
-
expression in Escherichia coli
-
expression of His-tagged proteins of His-p125, His-p50, His-p68, and Hisp12, in Escherichia coli strain BL21DE3(plys), expression of GST-tagged p12 using pGEX-5X-3 vector in Escherichia coli strain BL21DE3(plys), reconstitution of Pol delta complexes in insect cells infected with a single baculovirus into which one or more subunits are assembled, allowing efficient expression of the tetrameric Pol delta holoenzyme, the p125/p50 core dimer, the core+p68 trimer and the core+p12 trimer, as well as the p125 catalytic subunit
-
gene POLN, expression of N-terminally His6-tagged enzyme fragment Pol ny-77 in Escherichia coli in inclusion bodies
-
overview: genetic structure and predicted functional domains
-
the catalytic subunit is encoded by gene POLG at chromosomal locus 15q2, the accessory subunit is encoded by gene POLG2 at chromosomal locus 17q24.1, expression of polymerase point mutations combined with the D198A/E200A exonuclease mutation, the mutant is also lacking the mitochondrial targeting sequence, expression of N-terminally His6-tagged wild-type enzyme and mutant R946C in Spodoptera frugiperda Sf9 cells, expression of His6-tagged full-length p55 subunit without its mitochondrial targeting sequence in Escherichia coli strain BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
DNA polymerase eta expression is induced by cisplatin, mRNA expression can be up-regulated in a p53-dependent manner following ionizing radiation or camptothecin treatment
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
use of high hydrostatic pressure to refold recombinant N-terminally His6-tagged enzyme fragment Pol ny-77 from inclusion bodies after expression in Escherichia coli, in soluble and active form. The refolded Pol ny fragment has properties comparable to those of the small amount of Pol m that is purified from the soluble fraction, method evaluation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
DNA polymerases are promising drug targets for the treatment of cancer
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murakami, E.; Feng, J.Y.; Lee, H.; Hanes, J.; Johnson, K.A.; Anderson, K.S.
Characterization of novel reverse transcriptase and other RNA-associated catalytic activities by human DNA polymerase gamma: importance in mitochondrial DNA replication
J. Biol. Chem.
278
36403-36409
2003
Homo sapiens
Manually annotated by BRENDA team
Fisher, P.A.
Enzymologic mechanism of replicative DNA polymerases in higher eukaryotes
Prog. Nucleic Acid Res. Mol. Biol.
47
371-397
1994
Drosophila melanogaster, Homo sapiens
Manually annotated by BRENDA team
Wang, T.S.F.
Eukaryotic DNA polymerases
Annu. Rev. Biochem.
60
513-552
1991
Bos taurus, Saccharomyces cerevisiae, Gallus gallus, Drosophila melanogaster, Homo sapiens, Mammalia, Rattus norvegicus, Xenopus laevis
Manually annotated by BRENDA team
Weissbach, A.
Cellular and viral-induced eukaryotic polymerases
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
14
67-86
1981
Bos taurus, Gallus gallus, Herpes simplex virus, Homo sapiens, Mammalia, Mus musculus, Rattus norvegicus, Vaccinia virus
-
Manually annotated by BRENDA team
Sedwick, W.D.; Wang, T.S.F.; Korn, D.
The DNA polymerases of KB cells
Methods Enzymol.
29
89-102
1974
Homo sapiens
Manually annotated by BRENDA team
Lehman, I.R.; Karguni, L.S.
DNA polymerase alpha
J. Biol. Chem.
264
4265-4268
1989
Chlorocebus aethiops, Bos taurus, Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Mammalia, Mus musculus
Manually annotated by BRENDA team
Bambara, R.A.; Jessee, C.B.
Properties of DNA polymerases delta and epsilon, and their roles in eukaryotic DNA replication
Biochim. Biophys. Acta
1088
11-24
1991
Bos taurus, Saccharomyces cerevisiae, Oryctolagus cuniculus, Homo sapiens, Mammalia, Mus musculus
Manually annotated by BRENDA team
Weissbach, A.
The functional roles of mammalian DNA polymerase
Arch. Biochem. Biophys.
198
386-396
1979
Homo sapiens, Mammalia
Manually annotated by BRENDA team
Yang, C.L.; Chang, L.S.; Zhang, P.; Hao, H.; Zhu, L.; Toomey, N.L.; Lee, M.Y.W.T.
Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase delta
Nucleic Acids Res.
20
735-745
1992
Homo sapiens (P28340), Homo sapiens
Manually annotated by BRENDA team
Terry, B.J.; Liu, W.C.; Cianci, C.W.; Proszynski, E.; Fernandes, P.; Bush, K.; Meyers, E.
Inhibition of herpes simplex virus type 1 DNA polymerase by the natural product oosporein
J. Antibiot.
45
286-288
1992
Escherichia coli, Herpes simplex virus, Homo sapiens
Manually annotated by BRENDA team
Gray, H.; Wong T.W.
Purification and identification of subunit structure of the human mitochondrial DNA polymerase
J. Biol. Chem.
267
5835-5841
1992
Homo sapiens
Manually annotated by BRENDA team
Wintersberger E.
DNA-dependent DNA pllymerases from eukaryotes
Trends Biochem. Sci.
1977
58-60
1977
Bos taurus, Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team
Scovassi, A.I.; Plevani, P.; Bertazzoni, U.
Eukaryotic DNA polymerases
Trends Biochem. Sci.
1980
335-337
1980
Bos taurus, Saccharomyces cerevisiae, Dictyostelium discoideum, Euglena gracilis, Homo sapiens, Mammalia, Neurospora crassa, Physarum polycephalum, Tetrahymena pyriformis, Trypanosoma brucei, Ustilago maydis
-
Manually annotated by BRENDA team
Semizarov, D.G.; Arzumanov, A.A.; Dyatkina, N.B.; Meyer, A.; Vichier-Guerre, S.; Gosselin, G.; Rayner, B.; Imbach, J.L.; Krayevsky, A.A.
Stereoisomers of deoxynucleoside 5'-triphosphates as substrates for template-dependent and -independent DNA polymerases
J. Biol. Chem.
272
9556-9560
1997
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Roettger, M.P.; Fiala, K.A.; Sompalli, S.; Dong, Y.; Suo, Z.
Pre-steady-state kinetic studies of the fidelity of human DNA polymerase mu
Biochemistry
43
13827-13838
2004
Homo sapiens
Manually annotated by BRENDA team
Lebedeva, N.A.; Rechkunova, N.I.; Dezhurov, S.V.; Khodyreva, S.N.; Favre, A.; Blanco, L.; Lavrik, O.I.
Comparison of functional properties of mammalian DNA polymerase l and DNA polymerase b in reactions of DNA synthesis related to DNA repair
Biochim. Biophys. Acta
1751
150-158
2005
Homo sapiens
Manually annotated by BRENDA team
Ramadan, K.; Shevelev, I.V.; Maga, G.; Huebscher, U.
De novo DNA synthesis by human DNA polymerase l, DNA polymerase m and terminal deoxyribonucleotidyl transferase
J. Mol. Biol.
339
395-404
2004
Homo sapiens
Manually annotated by BRENDA team
Choi, J.Y.; Guengerich, F.P.
Adduct size limits efficient and error-free bypass across bulky N2-guanine DNA lesions by human DNA polymerase eta
J. Mol. Biol.
352
72-90
2005
Homo sapiens
Manually annotated by BRENDA team
Ray, A.S.; Feng, J.Y.; Murakami, E.; Chu, C.K.; Schinazi, R.F.; Anderson, K.S.
Interaction of 2-deoxyguanosine triphosphate analogue inhibitors of HIV reverse transcriptase with human mitochondrial DNA polymerase gamma
Antiviral Chem. Chemother.
18
25-33
2007
Homo sapiens
Manually annotated by BRENDA team
Ishimaru, C.; Kuriyama, I.; Shimazaki, N.; Koiwai, O.; Sakaguchi, K.; Kato, I.; Yoshida, H.; Mizushina, Y.
Cholesterol hemisuccinate: a selective inhibitor of family X DNA polymerases
Biochem. Biophys. Res. Commun.
354
619-625
2007
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Sucato, C.A.; Upton, T.G.; Kashemirov, B.A.; Batra, V.K.; Martinek, V.; Xiang, Y.; Beard, W.A.; Pedersen, L.C.; Wilson, S.H.; McKenna, C.E.; Florian, J.; Warshel, A.; Goodman, M.F.
Modifying the beta,gamma leaving-group bridging oxygen alters nucleotide incorporation efficiency, fidelity, and the catalytic mechanism of DNA polymerase beta
Biochemistry
46
461-471
2007
Homo sapiens (P06746)
Manually annotated by BRENDA team
Kamisuki, S.; Ishimaru, C.; Onoda, K.; Kuriyama, I.; Ida, N.; Sugawara, F.; Yoshida, H.; Mizushina, Y.
Nodulisporol and Nodulisporone, novel specific inhibitors of human DNA polymerase lambda from a fungus, Nodulisporium sp
Bioorg. Med. Chem.
15
3109-3114
2007
Homo sapiens
Manually annotated by BRENDA team
Doncaster, J.R.; Etchells, L.L.; Kershaw, N.M.; Nakamura, R.; Ryan, H.; Takeuchi, R.; Sakaguchi, K.; Sardarian, A.; Whitehead, R.C.
Synthetic analogues of the manzamenones and plakoridines which inhibit DNA polymerase
Bioorg. Med. Chem. Lett.
16
2877-2881
2006
Homo sapiens
Manually annotated by BRENDA team
Yakubovskaya, E.; Lukin, M.; Chen, Z.; Berriman, J.; Wall, J.S.; Kobayashi, R.; Kisker, C.; Bogenhagen, D.F.
The EM structure of human DNA polymerase gamma reveals a localized contact between the catalytic and accessory subunits
EMBO J.
26
4283-4291
2007
Homo sapiens (Q9UHN1), Homo sapiens
Manually annotated by BRENDA team
Hudson, G.; Chinnery, P.F.
Mitochondrial DNA polymerase-gamma and human disease
Hum. Mol. Genet.
15
R244-R252
2006
Homo sapiens
Manually annotated by BRENDA team
Choi, J.Y.; Guengerich, F.P.
Kinetic evidence for inefficient and error-prone bypass across bulky N2-guanine DNA adducts by human DNA polymerase iota
J. Biol. Chem.
281
12315-12324
2006
Homo sapiens
Manually annotated by BRENDA team
Duym, W.W.; Fiala, K.A.; Bhatt, N.; Suo, Z.
Kinetic effect of a downstream strand and its 5-terminal moieties on single nucleotide gap-filling synthesis catalyzed by human DNA polymerase lambda
J. Biol. Chem.
281
35649-35655
2006
Homo sapiens
Manually annotated by BRENDA team
Frank, E.G.; Woodgate, R.
Increased catalytic activity and altered fidelity of human DNA polymerase iota in the presence of manganese
J. Biol. Chem.
282
24689-24696
2007
Homo sapiens
Manually annotated by BRENDA team
Yamanaka, H.; Gatanaga, H.; Kosalaraksa, P.; Matsuoka-Aizawa, S.; Takahashi, T.; Kimura, S.; Oka, S.
Novel mutation of human DNA polymerase gamma associated with mitochondrial toxicity induced by anti-HIV treatment
J. Infect. Dis.
195
1419-1425
2007
Homo sapiens
Manually annotated by BRENDA team
Johnson, R.E.; Prakash, L.; Prakash, S.
Yeast and human translesion DNA synthesis polymerases: expression, purification, and biochemical characterization
Methods Enzymol.
408
390-407
2006
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Liu, G.; Chen, X.
DNA polymerase eta, the product of the xeroderma pigmentosum variant gene and a target of p53, modulates the DNA damage checkpoint and p53 activation
Mol. Cell. Biol.
26
1398-1413
2006
Homo sapiens
Manually annotated by BRENDA team
Capp, J.P.; Boudsocq, F.; Besnard, A.G.; Lopez, B.S.; Cazaux, C.; Hoffmann, J.S.; Canitrot, Y.
Involvement of DNA polymerase mu in the repair of a specific subset of DNA double-strand breaks in mammalian cells
Nucleic Acids Res.
35
3551-3560
2007
Homo sapiens
Manually annotated by BRENDA team
Crespan, E.; Alexandrova, L.; Khandazhinskaya, A.; Jasko, M.; Kukhanova, M.; Villani, G.; Huebscher, U.; Spadari, S.; Maga, G.
Expanding the repertoire of DNA polymerase substrates: template-instructed incorporation of non-nucleoside triphosphate analogues by DNA polymerases beta and lambda
Nucleic Acids Res.
35
45-57
2007
Homo sapiens
Manually annotated by BRENDA team
Naganuma, M.; Nishida, M.; Kuramochi, K.; Sugawara, F.; Yoshida, H.; Mizushina, Y.
1-deoxyrubralactone, a novel specific inhibitor of families X and Y of eukaryotic DNA polymerases from a fungal strain derived from sea algae
Bioorg. Med. Chem.
16
2939-2944
2008
Tequatrovirus T4, Bos taurus, Brassica oleracea, Escherichia coli, Homo sapiens, Rattus norvegicus, Thermus aquaticus
Manually annotated by BRENDA team
Sasaki, R.; Suzuki, Y.; Yonezawa, Y.; Ota, Y.; Okamoto, Y.; Demizu, Y.; Huang, P.; Yoshida, H.; Sugimura, K.; Mizushina, Y.
DNA polymerase gamma inhibition by vitamin K3 induces mitochondria-mediated cytotoxicity in human cancer cells
Cancer Sci.
99
1040-1048
2008
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Nishida, M.; Hada, T.; Kuramochi, K.; Yoshida, H.; Yonezawa, Y.; Kuriyama, I.; Sugawara, F.; Yoshida, H.; Mizushina, Y.
Diallyl sulfides: Selective inhibitors of family X DNA polymerases from garlic (Allium sativum L.)
Food Chem.
108
551-560
2008
Tequatrovirus T4, Bos taurus, Brassica oleracea, Drosophila melanogaster, Escherichia coli, Homo sapiens, Rattus norvegicus, Thermus aquaticus, Oncorhynchus masou
Manually annotated by BRENDA team
Takahashi, S.; Yonezawa, Y.; Kubota, A.; Ogawa, N.; Maeda, K.; Koshino, H.; Nakata, T.; Yoshida, H.; Mizushina, Y.
Pyranicin, a non-classical annonaceous acetogenin, is a potent inhibitor of DNA polymerase, topoisomerase and human cancer cell growth
Int. J. Oncol.
32
451-458
2008
Tequatrovirus T4, Bos taurus, Brassica oleracea, Drosophila melanogaster, Escherichia coli, Homo sapiens, Rattus norvegicus, Thermus aquaticus, Oncorhynchus masou
Manually annotated by BRENDA team
Richartz, A.; Hoeltje, M.; Brandt, B.; Schaefer-Korting, M.; Hoeltje, H.D.
Targeting human DNA polymerase alpha for the inhibition of keratinocyte proliferation. Part 1. Homology model, active site architecture and ligand binding
J. Enzyme Inhib. Med. Chem.
23
94-100
2008
Homo sapiens
Manually annotated by BRENDA team
Yasui, M.; Suenaga, E.; Koyama, N.; Masutani, C.; Hanaoka, F.; Gruz, P.; Shibutani, S.; Nohmi, T.; Hayashi, M.; Honma, M.
Miscoding properties of 2-deoxyinosine, a nitric oxide-derived DNA adduct, during translesion synthesis catalyzed by human DNA polymerases
J. Mol. Biol.
377
1015-1023
2008
Homo sapiens
Manually annotated by BRENDA team
Bailey, C.M.; Kasiviswanathan, R.; Copeland, W.C.; Anderson, K.S.
R964C mutation of DNA polymerase gamma imparts increased stavudine toxicity by decreasing nucleoside analog discrimination and impairing polymerase activity
Antimicrob. Agents Chemother.
53
2610-2612
2009
Homo sapiens
Manually annotated by BRENDA team
Frederick, A.M.; Davis, M.L.; Rice, K.P.
Inhibition of human DNA polymerase beta activity by the anticancer prodrug cloretazine
Biochem. Biophys. Res. Commun.
378
419-423
2009
Homo sapiens
Manually annotated by BRENDA team
Kanao, R.; Hanaoka, F.; Masutani, C.
A novel interaction between human DNA polymerase eta and MutLalpha
Biochem. Biophys. Res. Commun.
389
40-45
2009
Homo sapiens
Manually annotated by BRENDA team
Huang, Q.M.; Akashi, T.; Masuda, Y.; Kamiya, K.; Takahashi, T.; Suzuki, M.
Roles of POLD4, smallest subunit of DNA polymerase delta, in nuclear structures and genomic stability of human cells
Biochem. Biophys. Res. Commun.
391
542-546
2010
Homo sapiens
Manually annotated by BRENDA team
Donny-Clark, K.; Shapiro, R.; Broyde, S.
Accommodation of an N-(deoxyguanosin-8-yl)-2-acetylaminofluorene adduct in the active site of human DNA polymerase iota: Hoogsteen or Watson-Crick base pairing?
Biochemistry
48
7-18
2009
Homo sapiens (Q9UNA4), Homo sapiens
Manually annotated by BRENDA team
Nishida, M.; Ida, N.; Horio, M.; Takeuchi, T.; Kamisuki, S.; Murata, H.; Kuramochi, K.; Sugawara, F.; Yoshida, H.; Mizushina, Y.
Hymenoic acid, a novel specific inhibitor of human DNA polymerase lambda from a fungus of Hymenochaetaceae sp
Bioorg. Med. Chem.
16
5115-5122
2008
Homo sapiens
Manually annotated by BRENDA team
Berdis, A.
Mechanisms of DNA polymerases
Chem. Rev.
109
2862-2879
2009
Geobacillus stearothermophilus, Bacillus subtilis, Tequatrovirus T4, Escherichia phage T7, Escherichia coli, Homo sapiens, Escherichia phage RB69, Thermus aquaticus (P19821)
Manually annotated by BRENDA team
Hidaka, K.; Yamada, M.; Kamiya, H.; Masutani, C.; Harashima, H.; Hanaoka, F.; Nohmi, T.
Specificity of mutations induced by incorporation of oxidized dNTPs into DNA by human DNA polymerase eta
DNA Repair
7
497-506
2008
Homo sapiens
Manually annotated by BRENDA team
Petta, T.B.; Nakajima, S.; Zlatanou, A.; Despras, E.; Couve-Privat, S.; Ishchenko, A.; Sarasin, A.; Yasui, A.; Kannouche, P.
Human DNA polymerase iota protects cells against oxidative stress
EMBO J.
27
2883-2895
2008
Homo sapiens
Manually annotated by BRENDA team
Kirouac, K.N.; Ling, H.
Structural basis of error-prone replication and stalling at a thymine base by human DNA polymerase iota
EMBO J.
28
1644-1654
2009
Homo sapiens (Q9UNA4), Homo sapiens
Manually annotated by BRENDA team
Di Pasquale, F.; Fischer, D.; Grohmann, D.; Restle, T.; Geyer, A.; Marx, A.
Opposed steric constraints in human DNA polymerase beta and E. coli DNA polymerase I
J. Am. Chem. Soc.
130
10748-10757
2008
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Fowler, J.D.; Brown, J.A.; Johnson, K.A.; Suo, Z.
Kinetic investigation of the inhibitory effect of gemcitabine on DNA polymerization catalyzed by human mitochondrial DNA polymerase
J. Biol. Chem.
283
15339-15348
2008
Homo sapiens
Manually annotated by BRENDA team
Cavanaugh, N.A.; Kuchta, R.D.
Initiation of new DNA strands by the herpes simplex virus-1 primase-helicase complex and either herpes DNA polymerase or human DNA polymerase alpha
J. Biol. Chem.
284
1523-1532
2009
Human alphaherpesvirus 1, Homo sapiens
Manually annotated by BRENDA team
Jaiswal, A.S.; Banerjee, S.; Panda, H.; Bulkin, C.D.; Izumi, T.; Sarkar, F.H.; Ostrov, D.A.; Narayan, S.
A novel inhibitor of DNA polymerase beta enhances the ability of temozolomide to impair the growth of colon cancer cells
Mol. Cancer Res.
7
1973-1983
2009
Homo sapiens (P06746)
Manually annotated by BRENDA team
Betous, R.; Rey, L.; Wang, G.; Pillaire, M.J.; Puget, N.; Selves, J.; Biard, D.S.; Shin-ya, K.; Vasquez, K.M.; Cazaux, C.; Hoffmann, J.S.
Role of TLS DNA polymerases eta and kappa in processing naturally occurring structured DNA in human cells
Mol. Carcinog.
48
369-378
2009
Homo sapiens
Manually annotated by BRENDA team
Rey, L.; Sidorova, J.M.; Puget, N.; Boudsocq, F.; Biard, D.S.; Monnat, R.J.; Cazaux, C.; Hoffmann, J.S.
Human DNA polymerase eta is required for common fragile site stability during unperturbed DNA replication
Mol. Cell. Biol.
29
3344-3354
2009
Homo sapiens
Manually annotated by BRENDA team
Loeb, L.A.; Monnat, R.J.
DNA polymerases and human disease
Nat. Rev. Genet.
9
594-604
2008
Homo sapiens
Manually annotated by BRENDA team
Donny-Clark, K.; Broyde, S.
Influence of local sequence context on damaged base conformation in human DNA polymerase iota: molecular dynamics studies of nucleotide incorporation opposite a benzo[a]pyrene-derived adenine lesion
Nucleic Acids Res.
37
7095-7109
2009
Homo sapiens (Q9UNA4), Homo sapiens
Manually annotated by BRENDA team
Dorjsuren, D.; Wilson, D.M.; Beard, W.A.; McDonald, J.P.; Austin, C.P.; Woodgate, R.; Wilson, S.H.; Simeonov, A.
A real-time fluorescence method for enzymatic characterization of specialized human DNA polymerases
Nucleic Acids Res.
37
e128
2009
Homo sapiens
Manually annotated by BRENDA team
Cruet-Hennequart, S.; Gallagher, K.; Sokol, A.M.; Villalan, S.; Prendergast, A.M.; Carty, M.P.
DNA polymerase eta, a key protein in translesion synthesis in human cells
Subcell. Biochem.
50
189-209
2010
Homo sapiens (Q9Y253), Homo sapiens
Manually annotated by BRENDA team
Strittmatter, T.; Bareth, B.; Immel, T.A.; Huhn, T.; Mayer, T.U.; Marx, A.
Small molecule inhibitors of human DNA polymerase lambda
ACS Chem. Biol.
6
314-319
2011
Homo sapiens
Manually annotated by BRENDA team
Johnson, K.A.
The kinetic and chemical mechanism of high-fidelity DNA polymerases
Biochim. Biophys. Acta
1804
1041-1048
2010
Escherichia phage T7, Homo sapiens
Manually annotated by BRENDA team
Schmitt, M.W.; Venkatesan, R.N.; Pillaire, M.J.; Hoffmann, J.S.; Sidorova, J.M.; Loeb, L.A.
Active site mutations in mammalian DNA polymerase delta alter accuracy and replication fork progression
J. Biol. Chem.
285
32264-32272
2010
Homo sapiens
Manually annotated by BRENDA team
Kasiviswanathan, R.; Longley, M.J.; Young, M.J.; Copeland, W.C.
Purification and functional characterization of human mitochondrial DNA polymerase gamma harboring disease mutations
Methods
51
379-384
2010
Homo sapiens
Manually annotated by BRENDA team
Zhou, Y.; Meng, X.; Zhang, S.; Lee, E.Y.; Lee, M.Y.
Characterization of human DNA polymerase delta and its subassemblies reconstituted by expression in the MultiBac system
PLoS ONE
7
e39156
2012
Homo sapiens
Manually annotated by BRENDA team
Arana, M.; Powell, G.; Edwards, L.; Kunkel, T.; Petrovich, R.
Refolding active human DNA polymerase ny from inclusion bodies
Protein Expr. Purif.
70
163-171
2010
Homo sapiens
Manually annotated by BRENDA team
Antczak, N.M.; Walker, A.R.; Stern, H.R.; Leddin, E.M.; Palad, C.; Coulther, T.A.; Swett, R.J.; Cisneros, G.A.; Beuning, P.J.
Characterization of nine cancer-associated variants in human DNA polymerase kappa
Chem. Res. Toxicol.
31
697-711
2018
Homo sapiens (Q9UBT6)
Manually annotated by BRENDA team
Kaminski, A.M.; Bebenek, K.; Pedersen, L.C.; Kunkel, T.A.
DNA polymerase mu An inflexible scaffold for substrate flexibility
DNA Repair
93
102932
2020
Homo sapiens (Q9NP87)
Manually annotated by BRENDA team
Genna, V.; Vidossich, P.; Ippoliti, E.; Carloni, P.; De Vivo, M.
A self-activated mechanism for nucleic acid polymerization catalyzed by DNA/RNA polymerases
J. Am. Chem. Soc.
138
14592-14598
2016
Homo sapiens (Q9Y253)
Manually annotated by BRENDA team
Smith, M.R.; Alnajjar, K.S.; Hoitsma, N.M.; Sweasy, J.B.; Freudenthal, B.D.
Molecular and structural characterization of oxidized ribonucleotide insertion into DNA by human DNA polymerase beta
J. Biol. Chem.
295
1613-1622
2020
Homo sapiens (P06746)
Manually annotated by BRENDA team
Zahurancik, W.J.; Suo, Z.
Kinetic investigation of the polymerase and exonuclease activities of human DNA polymerase epsilon holoenzyme
J. Biol. Chem.
295
17251-17264
2020
Homo sapiens (Q07864 AND Q9NR33 AND P56282 AND Q9NRF9), Homo sapiens
Manually annotated by BRENDA team
Ucisik, M.N.; Hammes-Schiffer, S.
Effects of active site mutations on specificity of nucleobase binding in human DNA polymerase eta
J. Phys. Chem. B
121
3667-3675
2017
Homo sapiens (Q9Y253)
Manually annotated by BRENDA team
Stern, H.R.; Sefcikova, J.; Chaparro, V.E.; Beuning, P.J.
Mammalian DNA polymerase kappa activity and specificity
Molecules
24
2805
2019
Homo sapiens (Q9UBT6)
Manually annotated by BRENDA team