The first crystal structure of archaeal aldolase. Unique tetrameric structure of 2-deoxy-d-ribose-5-phosphate aldolase from the hyperthermophilic archaea Aeropyrum pernix.

@article{Sakuraba2003TheFC,
  title={The first crystal structure of archaeal aldolase. Unique tetrameric structure of 2-deoxy-d-ribose-5-phosphate aldolase from the hyperthermophilic archaea Aeropyrum pernix.},
  author={Haruhiko Sakuraba and Hideaki Tsuge and Ikuko Shimoya and Ryushi Kawakami and Shuichiro Goda and Yutaka Kawarabayasi and Nobuhiko Katunuma and Hideo Ago and Masashi Miyano and Toshihisa Ohshima},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 12},
  pages={10799-806}
}
A gene encoding a 2-deoxy-d-ribose-5-phosphate aldolase (DERA) homolog was identified in the hyperthermophilic Archaea Aeropyrum pernix. The gene was overexpressed in Escherichia coli, and the produced enzyme was purified and characterized. The enzyme is an extremely thermostable DERA; its activity was not lost after incubation at 100 degrees C for 10 min. The enzyme has a molecular mass of approximately 93 kDa and consists of four subunits with an identical molecular mass of 24 kDa. This is… CONTINUE READING

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