Studies on the Structure and Function of Glucosephosphate Isomerases: Chemical Modifications, Chemical Cleavages and Structural Analyses

Abstract

Human glucosephosphate isomerase was subjected to a series of chemical modifications aimed at identifying residues essential for catalytic activity. Specific lysyl, arginyl, tryptophanyl and histidyl residues were found to react stoichiometrically with pyridoxal-5'-phosphate-NaBH4, 2,3-butadione, N-bromosuccinimide and N-bromoacetylethanolamine phosphate, respectively

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