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E602V/A608V/I614M/E615G
the mutant enzyme is able to incorporate both NTPs and dNTPs with the same catalytic efficiency as the wild-type enzyme incorporates dNTPs. The mutant enzyme allowed the generation of mixed RNADNA amplification products in PCR demonstrating DNA polymerase, RNA polymerase as well as reverse transcriptase activity within the same polypeptide. The mutant displays an expanded substrate spectrum towards other 2'-substituted nucleotides and is able to synthesize nucleic acid polymers in which each base bear a different 2'-substituent
L831N/A814R
truncated enzyme delta413-L813N/A814R has reduced temperature stability
G418K
-
increased exonuclease activity
N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R /S612N/V730L/R736Q/S739N/M747R
-
selection of a polymerase with 15 mutations, mostly located at the template binding interface, by directed evolution of Thermus aquaticus DNA polymerase I, the mutant enzyme is a single variant of the Stoffel fragment of Taq DNA polymerase I, the enzyme shows broad template specificity and is a thermostable DNA-dependent and RNA-dependent DNA-polymerase, see also EC 2.7.7.49
Q507E
-
increased exonuclease activity
additional information
the intervening domain of the thermostable Thermus aquaticus DNA polymerase (TAQ: polymerase), which has no catalytic activity, is exchanged for the 3'-5' exonuclease domain of the homologous mesophile Escherichia coli DNA polymerase I (Escherichia coli pol I) and the homologous thermostable Thermotoga neapolitana DNA polymerase (TNE: polymerase). Three chimeric DNA polymerases are constructed using the three-dimensional (3D) structure of the Klenow fragment of the Escherichia coli pol I and 3D models of the intervening and polymerase domains of the TAQ: polymerase and the TNE: polymerase: chimera TaqEc1 (exchange of residues 292-423 from TAQ: polymerase for residues 327-519 of Escherichia coli pol I), chimera TaqTne1 (exchange of residues 292-423 of TAQ: polymerase for residues 295-485 of TNE: polymerase) and chimera TaqTne2 (exchange of residues 292-448 of TAQ: polymerase for residues 295-510 of TNE: polymerase). The chimera TaqEc1 shows characteristics from both parental polymerases at an intermediate temperature of 50°C: high polymerase activity, processivity, 3'-5' exonuclease activity and proof-reading function The chimeras TaqTne1 and TaqTne2 show no significant 3'-5' exonuclease activity and no proof-reading function. The chimera TaqTne1 shows an optimum temperature at 60°C, decreased polymerase activity compared with the TAQ: polymerase and reduced processivity. The chimera TaqTne2 shows high polymerase activity at 72°C, processivity and less reduced thermostability compared with the chimera TaqTne1
additional information
-
the intervening domain of the thermostable Thermus aquaticus DNA polymerase (TAQ: polymerase), which has no catalytic activity, is exchanged for the 3'-5' exonuclease domain of the homologous mesophile Escherichia coli DNA polymerase I (Escherichia coli pol I) and the homologous thermostable Thermotoga neapolitana DNA polymerase (TNE: polymerase). Three chimeric DNA polymerases are constructed using the three-dimensional (3D) structure of the Klenow fragment of the Escherichia coli pol I and 3D models of the intervening and polymerase domains of the TAQ: polymerase and the TNE: polymerase: chimera TaqEc1 (exchange of residues 292-423 from TAQ: polymerase for residues 327-519 of Escherichia coli pol I), chimera TaqTne1 (exchange of residues 292-423 of TAQ: polymerase for residues 295-485 of TNE: polymerase) and chimera TaqTne2 (exchange of residues 292-448 of TAQ: polymerase for residues 295-510 of TNE: polymerase). The chimera TaqEc1 shows characteristics from both parental polymerases at an intermediate temperature of 50°C: high polymerase activity, processivity, 3'-5' exonuclease activity and proof-reading function The chimeras TaqTne1 and TaqTne2 show no significant 3'-5' exonuclease activity and no proof-reading function. The chimera TaqTne1 shows an optimum temperature at 60°C, decreased polymerase activity compared with the TAQ: polymerase and reduced processivity. The chimera TaqTne2 shows high polymerase activity at 72°C, processivity and less reduced thermostability compared with the chimera TaqTne1
additional information
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generation of a mutated thermostable DNA polymerase, Taq M1, from Thermus aquaticus that exhibits an increased reverse transcriptase activity. The Taq polymerase mutant Taq M1 has similar PCR sensitivity and nuclease activity as the respective Taq wild-type DNA polymerase, but Taq M1 exhibits a significantly increased reverse transcriptase activity especially at high temperatures compared to the wild-type
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Rapid purification of high-activity Taq DNA polymerase
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1993
Thermus aquaticus, Thermus aquaticus INValphaF'
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1992
Thermus aquaticus, Thermus aquaticus YT1
-
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Lawyer, F.C.; Stoffel, S.; Saiki, R.K.; Chang, S.Y.; Landre, P.A.; Abramson, R.D.; Gelfand, D.H.
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Thermus aquaticus
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Ma, W.P.; Kaiser, M.W.; Lyamicheva, N.; Schaefer, J.J.; Allawi, H.T.; Takova, T.; Neri, B.P.; Lyamichev, V.I.
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Thermus thermophilus, Thermus aquaticus
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Villbrandt, B.; Sagner, G.; Schomburg, D.
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Protein Eng.
10
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1997
Thermus aquaticus (P19821), Thermus aquaticus
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Influence of DNA aptamer structure on the specificity of binding to Taq DNA polymerase
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68
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2003
Thermus aquaticus
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Thermus aquaticus
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Tequatrovirus T4, Thermus aquaticus
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2007
Thermus aquaticus
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Bailey, S.; Wing, R.A.; Steitz, T.A.
The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases
Cell
126
893-904
2006
Thermus aquaticus (Q9XDH5), Thermus aquaticus
brenda
Ong, J.L.; Loakes, D.; Jaroslawski, S.; Too, K.; Holliger, P.
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361
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2006
Thermus aquaticus (P19821)
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1-deoxyrubralactone, a novel specific inhibitor of families X and Y of eukaryotic DNA polymerases from a fungal strain derived from sea algae
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16
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2008
Tequatrovirus T4, Bos taurus, Brassica oleracea, Escherichia coli, Homo sapiens, Rattus norvegicus, Thermus aquaticus
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Nuclear factor-kappaB activation and differential expression of survivin and Bcl-2 in human grade 2-4 astrocytomas
Cancer
112
2258-2266
2008
Thermus aquaticus
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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.)
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108
551-560
2008
Tequatrovirus T4, Bos taurus, Brassica oleracea, Drosophila melanogaster, Escherichia coli, Homo sapiens, Rattus norvegicus, Thermus aquaticus, Oncorhynchus masou
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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
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32
451-458
2008
Tequatrovirus T4, Bos taurus, Brassica oleracea, Drosophila melanogaster, Escherichia coli, Homo sapiens, Rattus norvegicus, Thermus aquaticus, Oncorhynchus masou
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Berdis, A.
Mechanisms of DNA polymerases
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2862-2879
2009
Geobacillus stearothermophilus, Bacillus subtilis, Tequatrovirus T4, Escherichia phage T7, Escherichia coli, Homo sapiens, Escherichia phage RB69, Thermus aquaticus (P19821)
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Kranaster, R.; Drum, M.; Engel, N.; Weidmann, M.; Hufert, F.T.; Marx, A.
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2010
Thermus aquaticus
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Characterisation of a DNA polymerase highly mutated along the template binding interface
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2010
Thermus aquaticus
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Extremophiles
2
339-345
1998
Pyrococcus sp., Pyrococcus furiosus, Thermus aquaticus, Pyrococcus sp. ES4
brenda
Villbrandt, B.; Sobek, H.; Frey, B.; Schomburg, D.
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Thermus aquaticus (P19821), Thermus aquaticus
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Din, R.U.; Khan, M.I.; Jan, A.; Khan, S.A.; Ali, I.
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202
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2020
Thermus aquaticus (P19821), Thermus aquaticus
brenda
Burke, C.R.; Luptak, A.
DNA synthesis from diphosphate substrates by DNA polymerases
Proc. Natl. Acad. Sci. USA
115
980-985
2018
Thermus aquaticus (P19821), Thermococcus litoralis (P30317), Geobacillus stearothermophilus (P52026), Pyrococcus furiosus (P61875), Bacillus subtilis (P94544), Bacillus subtilis 168 (P94544)
brenda