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Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes.
(31)P NMR studies of O-acetylserine sulfhydrylase-B from Salmonella typhimurium.
Isozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic target.
Molecular basis for the isozymes of bovine glucose-6-phosphate isomerase.
Fine tuning of the active site modulates specificity in the interaction of O-acetylserine sulfhydrylase isozymes with serine acetyltransferase.
Detection of intermediates in reactions catalyzed by PLP-dependent enzymes: O-acetylserine sulfhydrylase and serine-glyoxalate aminotransferase.
Exploring O-acetylserine sulfhydrylase-B isoenzyme from Salmonella typhimurium by fluorescence spectroscopy.
Acid-base chemical mechanism of O-acetylserine sulfhydrylases-A and -B from pH studies.
Crystallization and preliminary X-ray data for the A-isozyme of O-acetylserine sulfhydrylase from Salmonella typhimurium.
Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants.