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Information on EC 2.7.7.7 - DNA-directed DNA polymerase and Organism(s) Escherichia coli and UniProt Accession P00582

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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:
Escherichia coli
UNIPROT: P00582
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
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 I
-
Klenow fragment
the Klenow fragment of Escherichia coli DNA polymerase I houses catalytic centers for both polymerase and 3'-5' exonuclease activities
deoxynucleate polymerase
-
-
-
-
deoxyribonucleate nucleotidyltransferase
-
-
-
-
deoxyribonucleic acid duplicase
-
-
-
-
deoxyribonucleic acid polymerase
-
-
-
-
deoxyribonucleic duplicase
-
-
-
-
deoxyribonucleic polymerase
-
-
-
-
deoxyribonucleic polymerase I
-
-
-
-
DinB DNA polymerase
-
-
DNA duplicase
-
-
-
-
DNA nucleotidyltransferase
-
-
-
-
DNA nucleotidyltransferase (DNA-directed)
-
-
-
-
DNA polmerase beta
-
-
-
-
DNA polymerase
DNA polymerase alpha
-
-
-
-
DNA polymerase gamma
-
-
-
-
DNA polymerase I
DNA polymerase II
-
-
-
-
DNA polymerase III
DNA polymerase III epsilon subunit
-
3'-to-5' proofreading exonuclease of the holoenzyme
DNA polymerase IV
-
-
DNA polymerase V
-
-
DNA polymmerase I
-
-
DNA replicase
-
-
-
-
DNA-dependent DNA polymerase
-
-
-
-
duplicase
-
-
-
-
KF(exo-)
-
3'->5'-exonuclease-deficient Klenow fragment of DNA polymerase I
Klenow fragment
nucleotidyltransferase, deoxyribonucleate
-
-
-
-
Pol gamma
-
-
-
-
Pol I
polymerase III
-
-
sequenase
-
-
-
-
Taq DNA polymerase
-
-
-
-
Taq Pol I
-
-
-
-
Tca DNA polymerase
-
-
-
-
UmuD'2C
-
free DNA polymerase V
UmuD'2C-RecA-ATP
-
active form of DNA polymerase V
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
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
DnaG primase and DNA polymerase III holoenzyme are able to bind concurrently to a primed template during DNA replication
-
-
?
Cy3-dATP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
systematic determination of the single-turnover incorporation kinetics of all four native nucleotides and a set of Cy3-labeled nucleotides by the Klenow fragment of Escherichia coli DNA polymerase I
-
-
?
Cy3-dCTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
systematic determination of the single-turnover incorporation kinetics of all four native nucleotides and a set of Cy3-labeled nucleotides by the Klenow fragment of Escherichia coli DNA polymerase I
-
-
?
Cy3-dGTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
systematic determination of the single-turnover incorporation kinetics of all four native nucleotides and a set of Cy3-labeled nucleotides by the Klenow fragment of Escherichia coli DNA polymerase I
-
-
?
Cy3-dUTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
systematic determination of the single-turnover incorporation kinetics of all four native nucleotides and a set of Cy3-labeled nucleotides by the Klenow fragment of Escherichia coli DNA polymerase I
-
-
?
dATP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
systematic determination of the single-turnover incorporation kinetics of all four native nucleotides and a set of Cy3-labeled nucleotides by the Klenow fragment of Escherichia coli DNA polymerase I
-
-
?
dCTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
systematic determination of the single-turnover incorporation kinetics of all four native nucleotides and a set of Cy3-labeled nucleotides by the Klenow fragment of Escherichia coli DNA polymerase I
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
dGTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
systematic determination of the single-turnover incorporation kinetics of all four native nucleotides and a set of Cy3-labeled nucleotides by the Klenow fragment of Escherichia coli DNA polymerase I
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
systematic determination of the single-turnover incorporation kinetics of all four native nucleotides and a set of Cy3-labeled nucleotides by the Klenow fragment of Escherichia coli DNA polymerase I
-
-
?
nucleotide + DNAn
?
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
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
2-(4-azidophenacyl)thio-2'-deoxyadenosine 5'-triphosphate
-
template-competitive DNA polymerase inhibitor
-
alpha-(4-azidophenyl)-1,N6-etheno-dATP
-
template-competitive DNA polymerase inhibitor
Ara-CTP
-
pol II
Benzyloxycarbonyl-Leu-Leu-al
-
-
Dansyl-Leu-Leu-Leu-CH2Cl
-
inhibition of pol I
Halenaquinol sulfate
-
potential inhibitor of DNA polymerase alpha and epsilon, less effective against Escherichia coli DNA polymerase
lysophosphatidic acid
-
weak inhibitor
N-ethylmaleimide
-
abolishes polymerase III activity at 10 mM
Oosporein
-
50% inhibition at 0.7 mM
pyranicin
-
-
RecA
-
exonuclease activity of pol II can be inhibited by the presence of RecA protein and single-strand binding protein
-
SH-blocking agents
-
pol II and III
-
sulfoquinovosyl diacylglycerol
-
significant inhibition of activity at 0.1 mg/ml in strain JM109, but not in strains TOP10, TOP10F, or DH5alpha
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
Auxiliary subunits
-
pol III can repair short gaps created by nuclease in duplex DNA, for efficient replication of the long, single-stranded templates pol III requires auxiliary subunits beta, gamma and delta
-
RecA
-
DNA polymerase V is activated by a RecA nucleoprotein filament, RecA transfers a single RecA-ATP stoichiometrically from its DNA 3'-end to free pol V (UmuD'2C) to form an active mutasome with the composition UmuD'2C-RecA-ATP
-
single-stranded-binding protein
-
SSB protein, Pol V has intrinsically weak DNA polymerase activity, but its catalytic activity can be stimulated in vitro in the presence the beta-processivity clamp, RecA protein bound to ssDNA, and single-stranded-binding protein
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0014 - 0.0037
deoxynucleoside triphosphate
0.00623
Cy3-dATP
-
pH 8.0, 25°C
-
0.003
Cy3-dCTP
-
pH 8.0, 25°C
-
0.0112
Cy3-dGTP
-
pH 8.0, 25°C
-
0.00893
Cy3-dUTP
-
pH 8.0, 25°C
-
0.00028
dATP
-
pH 8.0, 25°C
0.00027
dCTP
-
pH 8.0, 25°C
0.00022
dGTP
-
pH 8.0, 25°C
0.00035
dTTP
-
pH 8.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.16
Cy3-dATP
-
pH 8.0, 25°C
-
1.75
Cy3-dCTP
-
pH 8.0, 25°C
-
1.64
Cy3-dGTP
-
pH 8.0, 25°C
-
1.57
Cy3-dUTP
-
pH 8.0, 25°C
-
1.69
dATP
-
pH 8.0, 25°C
1.75
dCTP
-
pH 8.0, 25°C
6.48
dGTP
-
pH 8.0, 25°C
6.57
dTTP
-
pH 8.0, 25°C
4.17 - 250
Nucleotide
additional information
additional information
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
186
Cy3-dATP
-
pH 8.0, 25°C
-
583
Cy3-dCTP
-
pH 8.0, 25°C
-
146
Cy3-dGTP
-
pH 8.0, 25°C
-
176
Cy3-dUTP
-
pH 8.0, 25°C
-
6004
dATP
-
pH 8.0, 25°C
6480
dCTP
-
pH 8.0, 25°C
29500
dGTP
-
pH 8.0, 25°C
18800
dTTP
-
pH 8.0, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.41
alpha-(4-azidophenyl)-1,N6-etheno-dATP
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
pyranicin
Escherichia coli
-
IC50 above 0.2 mM, DNA polymerase I, in 50 mM Tris-HCl (pH 7.5), 1 mM dithiothreitol, 50% (v/v) glycerol, 0.1 mM EDTA, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.066
-
polymerase II
2.4
-
polymerase III
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
-
the DNA polymerase V is comprised by the UmuD'2C protein complex. Pol V activity depends on the beta-clamp and gamma-clamp loaders UmuC and UmuD'2, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10000
130000
-
gel filtration
140000
160000
-
pol III
25000
32000
-
x * 140000 (alpha) + x * 37000 (beta) + x * 52000 (gamma) + x * 32000 (delta) + x * 25000 (epsilon) + x * 10000 (theta) + x * 78000 (tau)
37000
-
x * 140000 (alpha) + x * 37000 (beta) + x * 52000 (gamma) + x * 32000 (delta) + x * 25000 (epsilon) + x * 10000 (theta) + x * 78000 (tau)
52000
-
x * 140000 (alpha) + x * 37000 (beta) + x * 52000 (gamma) + x * 32000 (delta) + x * 25000 (epsilon) + x * 10000 (theta) + x * 78000 (tau)
78000
-
x * 140000 (alpha) + x * 37000 (beta) + x * 52000 (gamma) + x * 32000 (delta) + x * 25000 (epsilon) + x * 10000 (theta) + x * 78000 (tau)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 109000, pol I
additional information
-
multipolypeptide complex in prokaryotes and eukaryotes, three structural levels can be distinguished: 1. core polymerase (responsible for basic polymerization step), 2. DNA polymerase holoenzyme (composed of the core polymerase, which is responsible for the basic polymerization step and associated accessory proteins, a complex which is fully active on naturally occuring DNA templates), 3. holoenzyme embedded in a higher order structure, such as an asymmetric dimer or other complex which acts in concert with other known replication enzymes
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and diphosphate, combined equilibrium dialysis and vapor diffusion method
crystal structure of the catalytic alpha subunit of DNA polymerase III is determined at 2.3 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F771A
the mutation shows 30% decreased polymerase activity compared to the wild type enzyme
L823A
the mutation shows 3% decreased polymerase activity compared to the wild type enzyme
N678A
no change in polymerase activity, increased mismatch-directed exonuclease activity
P680G
reduced kcat, no change in relative DNA binding affinity or Km, nearly complete loss in the processive mode of DNA synthesis
P680Q
reduced kcat, no change in relative DNA binding affinity or Km, nearly complete loss in the processive mode of DNA synthesis
Q667A
polymerase defective, no change in exonuclease activity
R821A
the mutation shows 19% increased polymerase activity compared to the wild type enzyme
R822A
the mutation shows 5% increased polymerase activity compared to the wild type enzyme
R822A/Y824A
the mutation shows 36% increased polymerase activity compared to the wild type enzyme
Y824A
the mutation shows 25% increased polymerase activity compared to the wild type enzyme
F12A
-
mutant enzyme shows disproportionately reduced activity on the damaged template
F13V
-
mutant enzyme is almost unable to carry out translesion synthesis over N2-furfuryl-dG, although its activity on undamaged DNA is unaffected. The F13V mutation has a modest effect on the ability of DinB to discriminate against ribonucleotides, increasing the frequency of their misincorporation from less than 0.00001 to 0.001
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
30 min, 75% inactivation
60
-
10 min, inactivation
80
-
3 min, inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-12°C, stable for several weeks without loss of activity
-
0°C, 3 months, 50% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
-
polymerase I
-
polymerase II
-
polymerase III
-
recombinant His-tagged proteins from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the recombinant subunits including alpha, epsilon, theta, gamma, delta', delta, and beta are purified separately, followed by in vitro reconstitution of the pol III core and clamp loader, or purified by copurification of the subunits of the pol III core and the clamp loader. Pol III core, clamp loader and sliding clamp can be reconstituted effectively to perform DNA polymerization
-
recombinnat His-tagged pol V from Escherichia coli B strain RW644 by nickel affinity chromatography, gel filtration, and hydroxyapatite chromatography, and of His-tagged gamma complex from Escherichia coli strain DV38(lambdaDE3) by nickel affinity chromatography, gel filtration, and anion exxchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Klenow fragment
mutants are expressed in Escherichia coli
expressed in Escherichia coli strain M15
-
expression of subunits including alpha, epsilon, theta, gamma, delta', delta, and beta separately or coexpression of the subunits of the pol III core and the clamp loader, as His-tagged proteins in Escherichia coli strain BL21(DE3)
-
pol V is encoded in the umuDC operon, expression of His-tagged pol V in Escherichia coli B strain RW644, and expression as His-tagged gamma complex in Escherichia coli strain DV38(lambdaDE3), methd development for co-expression of the UmuD'2C protein complex, modules separately or combined with expression of chaperones DnaK-DnaJ-GrpE (DnaKJE), or DnaKJE with GroESL, overview. His-tagged pol V is highly active in vivo
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kornberg, T.; Kornberg, A.
Bacterial DNA polymerases
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
10
119-144
1974
Bacillus subtilis, Bacteria, Escherichia coli, Micrococcus luteus
-
Manually annotated by BRENDA team
Lehman, R.
DNA polymerase I of Escherichia coli
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
14
15-37
1981
Escherichia coli
-
Manually annotated by BRENDA team
McHenry, C.; Kornberg, A.
DNA polymerase III holoenzyme
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
14
39-65
1981
Escherichia coli
-
Manually annotated by BRENDA team
Setlow, P.
DNA polymerase I from Escherichia coli
Methods Enzymol.
29
3-12
1974
Escherichia coli
Manually annotated by BRENDA team
Moses, R.E.
The isolation and properties of DNA polymerase II from Escherichia coli
Methods Enzymol.
29
13-22
1974
Escherichia coli
Manually annotated by BRENDA team
Kornberg, T.; Gefter, M.L.
Deoxyribonucleic acid polymerase II (Escherichia coli K12)
Methods Enzymol.
29
22-26
1974
Escherichia coli
Manually annotated by BRENDA team
Lehman, I.R.; Bessman, M.J.; Simms, E.S.; Kornberg, A.
Enzymatic synthesis of deoxyribonucleic acid. I. Preparation of substrates and partial purification of an enzyme from Escherichia coli
J. Biol. Chem.
233
163-170
1958
Escherichia coli
Manually annotated by BRENDA team
Hbscher, U.
DNA polymerase holoenzymes
Trends Biochem. Sci.
9
390-393
1984
Bos taurus, Drosophila melanogaster, Escherichia coli
-
Manually annotated by BRENDA team
Beese, L.S.; Friedman, J.M.; Steitz, T.A.
Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate
Biochemistry
32
14095-14101
1993
Escherichia coli (P00582), Escherichia coli
Manually annotated by BRENDA team
Murakami-Murofushi, K.; Shioda, M.; Kaji, K.; Yoshida, S.; Murofushi, H.
Inhibition of eukaryotic DNA polymerase alpha with a novel lysophosphatidic acid (PHYLPA) isolated from myxoamoebae of Physarum polycephalum
J. Biol. Chem.
267
21512-21517
1992
Bos taurus, Escherichia coli, Mammalia
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
Taguchi, T.; Matsukage, A.; Ito, H.; Saito, Y.; Kawashima, S.
Inhibition of DNA polymerases by tripeptide derivative protease inhibitors
Biochem. Biophys. Res. Commun.
185
1133-1140
1992
Escherichia coli, Rattus norvegicus
Manually annotated by BRENDA team
Shioda, M.; Kano, K.; Kobayashi, M.; Kitagawa, I.; Shoji, M.; Yoshida, S.; Ikegami, S.
Differential inhibition of eukaryotic DNA polymerases by halenaquinol sulfate, a p-hydroquinone sulfate obtained from a marine sponge
FEBS Lett.
350
249-252
1994
Escherichia coli, Mammalia
Manually annotated by BRENDA team
Goodman, M.F.; Fygenson, D.K.
DNA polymerase fidelity: from genetics toward a biochemical understanding
Genetics
148
1475-1482
1998
Tequatrovirus T4, Escherichia coli
Manually annotated by BRENDA team
Khare, V.; Eckert, K.A.
The proofreading 3'->5' exonuclease activity of DNA polymerases: a kinetic barrier to translesion DNA synthesis
Mutat. Res.
510
45-54
2002
Tequatrovirus T4, Escherichia coli, Herpes simplex virus
Manually annotated by BRENDA team
Tuske, S.; Singh, K.; Kaushik, N.; Modak, M.J.
The J-helix of Escherichia coli DNA polymerase I (Klenow fragment) regulates polymerase and 3'-5'-exonuclease functions
J. Biol. Chem.
275
23759-23768
2000
Escherichia coli (P00582)
Manually annotated by BRENDA team
Fujii, S.; Gasser, V.; Fuchs, R.P.
The biochemical requirements of DNA polymerase V-mediated translesion synthesis revisited
J. Mol. Biol.
341
405-417
2004
Escherichia coli
Manually annotated by BRENDA team
Sutton, M.D.; Duzen, J.M.; Maul, R.W.
Mutant forms of the Escherichia coli beta sliding clamp that distinguish between its roles in replication and DNA polymerase V-dependent translesion DNA synthesis
Mol. Microbiol.
55
1751-1766
2005
Escherichia coli
Manually annotated by BRENDA team
Doughty, M.B.; Aboudehen, K.; Anderson, G.; Li, K.; Moore, B.II; Poolson, T.
Side-chain conformational restriction in template-competitive inhibitors of E. coli DNA polymerase I Klenow fragment: synthesis, structural characterization and inhibition activity
Nucleosides Nucleotides Nucleic Acids
23
1751-1765
2004
Escherichia coli
Manually annotated by BRENDA team
Bakhtina, M.; Roettger, M.P.; Kumar, S.; Tsai, M.D.
A unified kinetic mechanism applicable to multiple DNA polymerases
Biochemistry
46
5463-5472
2007
African swine fever virus, Escherichia coli, Rattus norvegicus
Manually annotated by BRENDA team
Lamers, M.H.; Georgescu, R.E.; Lee, S.G.; ODonnell, M.; Kuriyan, J.
Crystal structure of the catalytic alpha subunit of E. coli replicative DNA polymerase III
Cell
126
881-892
2006
Escherichia coli
Manually annotated by BRENDA team
Jarosz, D.F.; Godoy, V.G.; Delaney, J.C.; Essigmann, J.M.; Walker, G.C.
A single amino acid governs enhanced activity of DinB DNA polymerases on damaged templates
Nature
439
225-228
2006
Escherichia coli
Manually annotated by BRENDA team
Bailey, M.F.; Van der Schans, E.J.; Millar, D.P.
Dimerization of the Klenow fragment of Escherichia coli DNA polymerase I is linked to its mode of DNA binding
Biochemistry
46
8085-8099
2007
Escherichia coli
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
Cramer, J.; Rangam, G.; Marx, A.; Restle, T.
Varied active-site constraints in the Klenow fragment of E. coli DNA polymerase I and the lesion-bypass Dbh DNA polymerase
ChemBioChem
9
1243-1250
2008
Escherichia coli
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
Kukreti, P.; Singh, K.; Ketkar, A.; Modak, M.J.
Identification of a new motif required for the 3-5 exonuclease activity of Escherichia coli DNA polymerase I (Klenow fragment): the RRRY motif is necessary for the binding of single-stranded DNA substrate and the template strand of the mismatched duplex
J. Biol. Chem.
283
17979-17990
2008
Escherichia coli (P00582), Escherichia coli
Manually annotated by BRENDA team
Furukawa, T.; Nishida, M.; Hada, T.; Kuramochi, K.; Sugawara, F.; Kobayashi, S.; Iijima, H.; Shimada, H.; Yoshida, H.; Mizushina, Y.
Inhibitory effect of sulfoquinovosyl diacylglycerol on prokaryotic DNA polymerase I activity and cell growth of Escherichia coli
J. Oleo Sci.
56
43-47
2007
Escherichia coli
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
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
Pohlhaus, J.R.; Long, D.T.; OReilly, E.; Kreuzer, K.N.
The epsilon subunit of DNA polymerase III is involved in the nalidixic acid-induced SOS response in Escherichia coli
J. Bacteriol.
190
5239-5247
2008
Escherichia coli, Escherichia coli JH39
Manually annotated by BRENDA team
Jiang, Q.; Karata, K.; Woodgate, R.; Cox, M.M.; Goodman, M.F.
The active form of DNA polymerase V is UmuD(2)C-RecA-ATP
Nature
460
359-363
2009
Escherichia coli
Manually annotated by BRENDA team
Karata, K.; Vaisman, A.; Goodman, M.F.; Woodgate, R.
Simple and efficient purification of Escherichia coli DNA polymerase V: cofactor requirements for optimal activity and processivity in vitro
DNA Repair
11
431-440
2012
Escherichia coli
Manually annotated by BRENDA team
Lin, S.Q.; Bi, L.J.; Zhang, X.E.
A simplified method for reconstituting active E. coli DNA polymerase III
Protein Cell
2
303-307
2011
Escherichia coli
Manually annotated by BRENDA team
Walsh, M.T.; Huang, X.
Measurement of incorporation kinetics of non-fluorescent native nucleotides by DNA polymerases using fluorescence microscopy
Nucleic Acids Res.
45
e175
2017
Escherichia coli
Manually annotated by BRENDA team
Bogutzki, A.; Naue, N.; Litz, L.; Pich, A.; Curth, U.
E. coli primase and DNA polymerase III holoenzyme are able to bind concurrently to a primed template during DNA replication
Sci. Rep.
9
14460
2019
Escherichia coli
Manually annotated by BRENDA team