Klentaq

From Thermus aquaticus (aliases:Stoffel fragment)
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Welcome to the Polymerase Page

This page presents all the information in Polbase for Klentaq.

Mutants:

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Structures/Sequence:

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Mutant of: Taq pol I (1-235)

Klentaq is a family A enzyme from Thermus aquaticus.

Selected Properties for Klentaq:

3'-5' exo activity 5'-3' exo activity Frameshift Rate Substitution Rate General Error Rate
no data no data no data no data no data
Year Authors Title Results by property
2013 Paul J Rothwell, William J Allen, Evangelos Sisamakis, Stanislav Kalinin, Suren Felekyan, Jerker Widengren, Gabriel Waksman, Claus A M Seidel dNTP-dependent conformational transit...
2013 Nina Blatter, Konrad Bergen, O Nolte, Wolfgang Welte, Kay Diederichs, J Mayer, M Wieland, Andreas Marx Structure and Function of an RNA-Read...
2013 Samra Obeid, H Bußkamp, Wolfram Welte, Kay Diederichs, Andreas Marx Snapshot of a DNA polymerase while in...
2012 Samra Obeid, Wolfram Welte, Kay Diederichs, Andreas Marx Amino acid templating mechanisms in s... Amino Acids Contacting NTP,All properties
2012 Sarah E Graham, FatimaSultana Syeda, G Andrés Cisneros Computational prediction of residues ...
2012 Konrad Bergen, Anna-Lena Steck, Stefan Strütt, Anna Baccaro, Wolfram Welte, Kay Diederichs, Andreas Marx Structures of KlenTaq DNA polymerase ...
2010 Christian Gloeckner, Ramon Kranaster, Andreas Marx Directed evolution of DNA polymerases...
2003 Milko B Kermekchiev, Anatoly Tzekov, Wayne M Barnes Cold-sensitive mutants of Taq DNA pol...
1999 Yingqian Li, V Mitaxov, Gabriel Waksman Structure-based design of Taq DNA pol...
1998 Yingqian Li, S Korolev, Gabriel Waksman Crystal structures of open and closed...
1995 S Korolev, M Nayal, Wayne M Barnes, E Di Cera, Gabriel Waksman Crystal structure of the large fragme...

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