作者: Andrea Mozzarelli , Stefano Bettati
DOI: 10.1002/TCR.20094
关键词: Enzyme 、 Enzyme catalysis 、 Stereochemistry 、 Biochemistry 、 Pyridoxal 、 Chemistry 、 Cysteine synthase 、 Cofactor 、 Pyridoxal phosphate 、 Enzyme Commission number 、 Tryptophan synthase
摘要: Pyridoxal 5'-phosphate (PLP)-dependent enzymes represent about 4% of the classified by Enzyme Commission. The versatility PLP in carrying out a large variety reactions exploiting electron sink effect pyridine ring, conformational changes accompanying chemical steps and stabilizing distinct catalytic intermediates, spectral properties different coenzyme-substrate derivatives signaling reaction progress, are some features that have attracted our interest to investigate structure-dynamics-function relationships PLP-dependent enzymes. To this goal, an integrated approach combining biochemical, biophysical, computational, molecular biology methods was used. extensive work carried on two enzymes, tryptophan synthase O-acetylserine sulfhydrylase, is presented discussed as representative other we investigated. Finally, perspectives functional genomics drug targeting highlight continuous novelty "old" class