title: Mode of action of cystathionine beta-lyase.
abstract: Cystathionine beta-lyase (CBL) is a member of the gamma-family of pyridoxal-5'-phosphate (PLP)-dependent enzymes (Alexander et al., 1994) that cleave C(beta,gamma)-S bonds of a broad variety of substrates. Recently, we reported the X-ray crystal structures of CBL and the CBL-trifluoroalanine inactivation complex at 1.83 A and 2.3 A resolution, respectively. The structures explicitly reveal the cofactor and substrate binding pockets. Spectral analysis of substrate turnover indicates a change of hydrophobicity in the microenvironment of the aldimine bond. In combination with further spectroscopic data, crystallographic evidence permits the formulation of a likely reaction mechanism.
authors.affiliation: Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany.
authors.forename: T
authors.initials: T
authors.lastname: Clausen
authors.forename: B
authors.initials: B
authors.lastname: Laber
authors.forename: A
authors.initials: A
authors.lastname: Messerschmidt
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003540:Cystathionine / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008190:Lyases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D013237:Stereoisomerism; D014961:X-Ray Diffraction
chemical_list: D003540:Cystathionine; D008190:Lyases; C019965:cystathionine beta-lyase