Exploring the pyridoxal 5'-phosphate-dependent enzymes.

作者: Andrea Mozzarelli , Stefano Bettati

DOI: 10.1002/TCR.20094

关键词: EnzymeEnzyme catalysisStereochemistryBiochemistryPyridoxalChemistryCysteine synthaseCofactorPyridoxal phosphateEnzyme Commission numberTryptophan 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

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