Structural insights into pathogenic mutations in heme-dependent cystathionine-beta-synthase.

@article{Yamanishi2006StructuralII,
  title={Structural insights into pathogenic mutations in heme-dependent cystathionine-beta-synthase.},
  author={Mamoru Yamanishi and Omer Kabil and Suvajit Sen and Ruma Banerjee},
  journal={Journal of inorganic biochemistry},
  year={2006},
  volume={100 12},
  pages={1988-95}
}
Human cystathionine beta-synthase plays a key role in maintaining low intracellular levels of homocysteine and is unique in being a pyridoxal phosphate-dependent enzyme that is a hemeprotein. It catalyzes the beta-replacement of serine and homocysteine to generate the condensation product, cystathionine. While the structure of a truncated catalytic core of the protein has been determined by crystallography, a model for the full-length enzyme has been developed guided by hydrogen-deuterium… CONTINUE READING