Results 191 to 200 of about 14,614 (212)
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Crystal structure of Thermus aquaticus DNA polymerase
Nature, 1995The 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 +5 more
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A specific l-asparaginase from Thermus aquaticus
Archives of Biochemistry and Biophysics, 1985The 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 +3 more
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Safety evaluation of amylomaltase from Thermus aquaticus
Regulatory Toxicology and Pharmacology, 2010A 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 +7 more
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The growth behaviour of Thermus aquaticus in continuous cultivation
European Journal of Applied Microbiology and Biotechnology, 1982The growth of the yellow pigmented non-sporulating caldoactive bacterium Thermus aquaticus was investigated in different culture vessels and using differnt culture techniques. Each combination of these two variables led to very specific characteristic behaviour of the culture. A synthetic medium for a white cell type of T.
S. Cometta +2 more
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Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase
Biochemistry, 1988We have determined the fidelity of in vitro DNA synthesis catalyzed at high temperature by the DNA polymerase from the thermophilic bacterium Thermus aquaticus. Using a DNA substrate that contains a 3'-OH terminal mismatch, we demonstrate that the purified polymerase lacks detectable exonucleolytic proofreading activity.
Thomas A. Kunkel, Kenneth R. Tindall
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Thermal stability of ribosomes and RNA from Thermus aquaticus
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1970Abstract This paper presents data on the physical and chemical properties of the ribosomes and RNA of Thermus aquaticus, an organism able to grow at temperatures up to 79°. Ultracentrifugal analysis of purified ribosomes in 0.01 M Mg2+ demonstrated components sedimenting at 50 S, 70 S and 100 S.
Thomas D. Brock +2 more
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Cloning and Sequencing of the Thermus aquaticus Glycerol Facilitator Gene
DNA Sequence, 2002The gene glpK, encoding glycerol kinase of Thermus aquaticus has been identified [Biosci. Biotechnol. Biochem., 62 (1998) 2375-2381]. In the present work, the nucleotide sequence of glpFK operon and the gene glpF encoding glycerol facilitator were determined. T.
Tadashi Yoshimoto +2 more
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Recombinant Thermus aquaticus RNA Polymerase for Structural Studies
Journal of Molecular Biology, 2006Advances in the structural biology of bacterial transcription have come from studies of RNA polymerases (RNAPs) from the thermophilic eubacteria Thermus aquaticus (Taq) and Thermus thermophilus (Tth). These structural studies have been limited by the fact that only endogenous Taq or Tth RNAP, laboriously purified from large quantities of Taq or Tth ...
Konstantin Kuznedelov +5 more
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Purification and Properties of Malate Dehydrogenase from Thermus Aquaticus
1976The extreme thermophile Thermus aquaticus 1 grows optimally at 70° to a high cell density with a mean generation time of about one hour. The type strain YT1, and several strains of similar genera and species have been used for the purification of enzymes for comparison with those of mesophiles2. We have purified and investigated malate dehydrogenase (E.
J. H. F. Biffen, R. A. D. Williams
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Preliminary crystallographic study ofThermus aquaticusglycerol kinase
Acta Crystallographica Section D Biological Crystallography, 2001Glycerol kinase (GlpK) is an important enzyme which catalyzes the rate-limiting step in a central biochemical pathway involving glycerol metabolism. GlpK from the thermophile Thermus aquaticus has been overexpressed in glpK-deficient Escherichia coli and crystallized by the hanging-drop method.
Hua-Shan Huang +3 more
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