Conformational properties of nine purified cystathionine β-synthase mutants.

@article{Hnzda2012ConformationalPO,
  title={Conformational properties of nine purified cystathionine β-synthase mutants.},
  author={Ale{\vs} Hn{\'i}zda and Tomas Majtan and Lu Wei Liu and Angel L Pey and John Franklin Carpenter and Milan Kod{\'i}{\vc}ek and Viktor Ko{\vz}ich and Jan P Kraus},
  journal={Biochemistry},
  year={2012},
  volume={51 23},
  pages={
          4755-63
        }
}
Protein misfolding due to missense mutations is a common pathogenic mechanism in cystathionine β-synthase (CBS) deficiency. In our previous studies, we successfully expressed, purified, and characterized nine CBS mutant enzymes containing the following patient mutations: P49L, P78R, A114V, R125Q, E176K, R266K, P422L, I435T, and S466L. These purified mutants exhibited full heme saturation, normal tetrameric assembly, and high catalytic activity. In this work, we used several spectroscopic and… CONTINUE READING
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