title: Structural insights into mutations of cystathionine beta-synthase.
abstract: Cystathionine beta-synthase (CBS) is a unique heme-containing enzyme that catalyses 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 amino acid metabolism characterised by increased levels of homocysteine and methionine and decreased levels of cysteine. Presently, more than 100 CBS mutations have been described which lead to homocystinuria with different degrees of severity in the patients. We have recently solved the crystal structure of a truncated form of this enzyme, which enables us to correlate some of these mutations with the structure.
authors.affiliation: M.E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056, Basel, Switzerland.
authors.forename: Markus
authors.initials: M
authors.lastname: Meier
authors.forename: Jana
authors.initials: J
authors.lastname: Oliveriusova
authors.forename: Jan P
authors.initials: JP
authors.lastname: Kraus
authors.forename: Peter
authors.initials: P
authors.lastname: Burkhard
mesh_terms: D001665:Binding Sites; D003541:Cystathionine beta-Synthase / Q000737:chemistry* / Q000235:genetics*; D019281:Dimerization; D006418:Heme / Q000737:chemistry; D006712:Homocystinuria / Q000235:genetics; D006801:Humans; D009154:Mutation
chemical_list: D006418:Heme; D003541:Cystathionine beta-Synthase