title: Exploring the pyridoxal 5'-phosphate-dependent enzymes.
abstract: Pyridoxal 5'-phosphate (PLP)-dependent enzymes represent about 4% of the enzymes classified by the Enzyme Commission. The versatility of PLP in carrying out a large variety of reactions exploiting the electron sink effect of the pyridine ring, the conformational changes accompanying the chemical steps and stabilizing distinct catalytic intermediates, and the spectral properties of the different coenzyme-substrate derivatives signaling the reaction progress, are some of the features that have attracted our interest to investigate the structure-dynamics-function relationships of PLP-dependent enzymes. To this goal, an integrated approach combining biochemical, biophysical, computational, and molecular biology methods was used. The extensive work carried out on two enzymes, tryptophan synthase and O-acetylserine sulfhydrylase, is presented and discussed as representative of other PLP-dependent enzymes we have investigated. Finally, perspectives of PLP-dependent enzymes functional genomics and drug targeting highlight the continuous novelty of an "old" class of enzymes.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Parma, 43100 Parma, Italy. andrea.mozzarelli@unipr.it
authors.forename: Andrea
authors.initials: A
authors.lastname: Mozzarelli
authors.forename: Stefano
authors.initials: S
authors.lastname: Bettati
mesh_terms: D002384:Catalysis; D003460:Crystallization; D003547:Cysteine Synthase / Q000737:chemistry / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000378:metabolism; D011487:Protein Conformation; D011732:Pyridoxal Phosphate / Q000378:metabolism*; D014367:Tryptophan Synthase / Q000737:chemistry / Q000378:metabolism*
chemical_list: D004800:Enzymes, Immobilized; D011732:Pyridoxal Phosphate; D003547:Cysteine Synthase; D014367:Tryptophan Synthase