Purification and characterization of a novel enzyme, L-threo-3-hydroxyaspartate dehydratase, from Pseudomonas sp. T62.

@article{Wada1999PurificationAC,
  title={Purification and characterization of a novel enzyme, L-threo-3-hydroxyaspartate dehydratase, from Pseudomonas sp. T62.},
  author={Masaru Usuki-Manshon Wada and Tomohiro Matsumoto and Shigeru Nakamori and Masami Sakamoto and Miyuki Kataoka and June Qingxia Liu and Noriyuki Itoh and Hidetoshi Yamada and Shinnkichi Shimizu},
  journal={FEMS microbiology letters},
  year={1999},
  volume={179 1},
  pages={
          147-51
        }
}
L-threo-3-Hydroxyaspartate dehydratase (L-threo-3-hydroxyaspartate hydro-lyase), which exhibited specificity for L-threo-3-hydroxyaspartate (K(m)=0.74 mM, V(max)=37.5 micromol min(-1) (mg protein)(-1)) but not for D-threo or D, L-erythro-3-hydroxyaspartate, was purified from a cell-free extract of Pseudomonas sp. T62. The activity of the enzyme was inhibited by hydroxylamine and EDTA, which suggests that pyridoxal 5'-phosphate and divalent cations participate in the enzyme reaction. The NH(2… CONTINUE READING
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