Results 261 to 270 of about 40,909 (278)
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A DNA Methylase from Thermus thermophilus HB8

The Journal of Biochemistry, 1980
A DNA methylase was purified in a homogeneous state from a extremely thermophilic bacterium, Thermus thermophilus HB8, by chromatography on, successively, phosphocellulose, CM-cellulose, and heparin-Sepharose. The molecular weight of the enzyme was determined to be about 44,000 by gel filtration on a Sephadex G-100 column and 41,000 by SDS-poly ...
Kayoko Nakazawa   +2 more
openaire   +3 more sources

In vitro dihydrouridine formation by tRNA dihydrouridine synthase from Thermus thermophilus, an extreme-thermophilic eubacterium.

Journal of Biochemistry (Tokyo), 2015
Dihydrouridine (D) is formed by tRNA dihydrouridine synthases (Dus). In mesophiles, multiple Dus enzymes bring about D modifications at several positions in tRNA.
Hiroaki Kusuba   +8 more
semanticscholar   +1 more source

Inhibitors of Thermus thermophilus Isopropylmalate Dehydrogenase

The Journal of Organic Chemistry, 1994
In an attempt to use mechanism-based design for the discovery of inhibitors of the isopropylmalate dehydrogenase from T. thermophilus, we have prepared and studied a number of potential mimics for an intermediate in the oxidative decarboxylation of isopropyl malate, the enol or enolate of α-ketoisocaproate. Because hydroramate and dicarboxylate enolate
Michael C. Pirrung   +2 more
openaire   +2 more sources

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

Nature Structural Biology, 1995
The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus, solved at 2.9 A resolution, displays (alpha beta)2 subunit organization. Unexpectedly, both the catalytic alpha- and the non-catalytic beta-subunits comprise the characteristic fold of the class II active-site domains.
Mosyak, Lidia   +4 more
openaire   +4 more sources

A hyperthermophilic laccase from Thermus thermophilus HB27

Extremophiles, 2005
A copper-inducible laccase activity was detected in Thermus thermophilus HB27. The enzyme was partially purified and separated by SDS-PAGE. After staining, a gel slice containing a approximately 53-kDa protein was excised and treated with trypsin, and the in-gel digests were analyzed by mass spectrometry. By mass fingerprinting, the peptides were found
openaire   +3 more sources

Biochemical Assays of Gre Factors of Thermus Thermophilus

2003
Publisher Summary This chapter discusses the biochemical assaying of Gre factors of Thermus Thermophilus. The biochemical studies of Escherichia coli Gre factors indicate that they are not nucleases but RNAP co-factors, which activate the same catalytic center involved in both RNA synthesis and RNA hydrolysis reactions.
Sergei Borukhov, Oleg Laptenko
openaire   +3 more sources

Biotechnological Applications of Thermus thermophilus as Host

Current Biotechnology, 2013
Aurelio Hidalgo, Jose Berenguer
openaire   +2 more sources

Genes and Genetic Manipulation in Thermus thermophilus

1995
Nagahari and colleagues (1980) first isolated a gene from Thermus by cloning a HindIII fragment of chromosomal DNA containing the leuCine genes, leuB, leuC, and leuD from Thermus thermophilus strain HB27 into Escherichia coli. Independently, Tanaka et al.
openaire   +2 more sources

Thermus thermophilus HB8

1998
K. M. Borges, P. L. Bergquist
openaire   +2 more sources

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