Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate.

@article{Nakai1999StructureOT,
  title={Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate.},
  author={Takehiro Nakai and Kengo Okada and Shigeto Akutsu and Ikuko Miyahara and Souta Kawaguchi and Ryohei Kato and Seiki Kuramitsu and Ken Hirotsu},
  journal={Biochemistry},
  year={1999},
  volume={38 8},
  pages={2413-24}
}
The three-dimensional structures of pyridoxal 5'-phosphate-type aspartate aminotransferase (AspAT) from Thermus thermophilus HB8 and pyridoxamine 5'-phosphate type one in complex with maleate have been determined by X-ray crystallography at 1.8 and 2.6 A resolution, respectively. The enzyme is a homodimer, and the polypeptide chain of the subunit is folded into one arm, one small domain, and one large domain. AspATs from many species were classified into aminotransferase subgroups Ia and Ib… CONTINUE READING

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