Results 191 to 200 of about 24,101 (229)

A unique inhibitor conformation selectively targets the DNA polymerase PolC of Gram-positive priority pathogens

Smits WK, Urem M, Friggen A, Musch N, Silverman M, Swain C, Barbachyn M, Mortin L, Yu X, DeLuccia R, Lamers M.   +10 more
europepmc   +1 more source

Dynamics and reactivity in Thermus aquaticus N6-adenine methyltransferase. [PDF]

Journal of the American Chemical Society, 2014
M.TaqI is a DNA methyltransferase from Thermus aquaticus that catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the N6 position of an adenine, a process described only in prokaryotes. We have used full atomistic classical molecular
J. Aranda, Kirill Zinovjev, Maite Roca, I. Tuñón   +3 more
semanticscholar   +3 more sources

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Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase.

Biochemistry, 1988
We have determined the fidelity of in vitro DNA synthesis catalyzed at high temperature by the DNA polymerase from the thermophilic bacterium Thermus aquaticus.
Kenneth R. Tindall, T. Kunkel
semanticscholar   +4 more sources

Purification of TaqI endonuclease from Thermus aquaticus

Journal of Chromatography A, 1998
A purification procedure for the thermostable restriction enzyme TaqI was developed using high-performance ion-exchange liquid chromatography. The effects of various operating conditions on the separation behaviour of TaqI endonuclease from the cell extracts were investigated for optimisation and scaling up.
Kutlu O. Ulgen, Mehmet M. Altintas, Nevra Özer   +2 more
openaire   +3 more sources

Crystal structure of Thermus aquaticus DNA polymerase

Nature, 1995
The DNA polymerase from Thermus aquaticus (Taq polymerase), famous for its use in the polymerase chain reaction, is homologous to Escherichia coli DNA polymerase I (pol I) Like pol I, Taq polymerase has a domain at its amino terminus (residues 1-290) that has 5' nuclease activity and a domain at its carboxy terminus that catalyses the polymerase ...
Se Won Suh, Jimin Wang, Dae Sil Lee, Youngsoo Kim, Soo Hyun Eom, Thomas A. Steitz   +5 more
openaire   +3 more sources

A specific l-asparaginase from Thermus aquaticus

Archives of Biochemistry and Biophysics, 1985
The L-asparaginase from an extreme thermophile, Thermus aquaticus strain T351, was highly substrate- and stereospecific, with no activity against glutamine or D-asparagine. It had a high Km of 8.6 mM. In these aspects it closely resembled the corresponding enzymes from thermophilic bacteria.
Graeme Roy Guy, Monique P. Curran, Hugh W. Morgan, Roy M. Daniel   +3 more
openaire   +3 more sources

Safety evaluation of amylomaltase from Thermus aquaticus

Regulatory Toxicology and Pharmacology, 2010
A recombinant amylomaltase, MQ-01, obtained by cultivation of Bacillus subtilis expressing the amylomaltase gene from Thermus aquaticus is to be used in the production of enzymatically-synthesized glycogen; which is intended for use as a food ingredient.
Hiroki Takata, Shahrzad Tafazoli, Tsunehisa Akiyama, Andrea W. Wong, Takashi Kuriki, Iwao Kojima, Eisuke Tomioka, Hideki Kajiura   +7 more
openaire   +3 more sources