Mutagenesis studies of human cystathionine beta-synthase: residues important for heme binding and substrate interactions

Protein Pept Lett. 2010 Mar;17(3):351-5. doi: 10.2174/092986610790780233.

Abstract

Human cystathionine beta-synthase (CBS) is a pyridoxal 5'-phosphate (PLP) dependent hemoprotein, which catalyzes the condensation of serine and homocysteine. Our mutagenesis studies suggest that Arg-266 is important to sense structural changes in heme-binding site, and that Gln-222 as well as Tyr-223 are involved in interactions with substrates.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain
  • Cystathionine beta-Synthase / chemistry*
  • Cystathionine beta-Synthase / genetics
  • Cystathionine beta-Synthase / metabolism*
  • Heme / chemistry*
  • Heme / genetics
  • Heme / metabolism*
  • Homocysteine / metabolism
  • Humans
  • Hydrogen Sulfide / metabolism
  • Models, Molecular
  • Mutagenesis, Site-Directed / methods*
  • Protein Binding
  • Serine / metabolism
  • Spectrophotometry
  • Structure-Activity Relationship

Substances

  • Homocysteine
  • Heme
  • Serine
  • Cystathionine beta-Synthase
  • Hydrogen Sulfide