S-adenosyl-L-homocysteine hydrolase from a hyperthermophile (Thermotoga maritima) is expressed in Escherichia coli in inactive form - Biochemical and structural studies.

@article{Brzezinski2017SadenosylLhomocysteineHF,
  title={S-adenosyl-L-homocysteine hydrolase from a hyperthermophile (Thermotoga maritima) is expressed in Escherichia coli in inactive form - Biochemical and structural studies.},
  author={Krzysztof Brzezinski and Justyna Czyrko and Joanna Śliwiak and Edyta Nalewajko-Sieliwoniuk and Mariusz Jaskolski and Boguslaw P. Nocek and Zbigniew Dauter},
  journal={International journal of biological macromolecules},
  year={2017},
  volume={104 Pt A},
  pages={
          584-596
        }
}
Thermotoga maritima is a hyperthermophilic bacterium but its genome encodes a number of archaeal proteins including S-adenosyl-L-homocysteine hydrolase (SAHase), which regulates cellular methylation reactions. The question of proper folding and activity of proteins of extremophilic origin is an intriguing problem. When expressed in E.coli and purified (as a homotetramer) at room temperature, the hyperthermophilic SAHase from T.maritima was inactive. ITC study indicated that the protein… CONTINUE READING
BETA
Tweets
This paper has been referenced on Twitter 1 time. VIEW TWEETS