Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein.

Cystathionine beta-synthase (CBS) is a unique heme- containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Here we present the X-ray crystal structure of a truncated form of the enzyme. CBS shares the same fold with O-acetylserine sulfhydrylase but it contains an additional N-terminal heme binding site. This heme binding motif together with a spatially adjacent oxidoreductase active site motif could explain the regulation of its enzyme activity by redox changes.

Pubmed ID: 11483494


  • Meier M
  • Janosik M
  • Kery V
  • Kraus JP
  • Burkhard P


The EMBO journal

Publication Data

August 1, 2001

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cystathionine beta-Synthase
  • Heme
  • Hemeproteins
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis
  • Oxidoreductases
  • Protein Structure, Secondary
  • Pyridoxal Phosphate
  • Rabbits