Symposium ArticlesEsterase-Like Activity of Human Serum Albumin II: Reaction with N-trans-Cinnamoylimidazoles
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Molecular and practical aspects of the enzymatic properties of human serum albumin and of albumin-ligand complexes
2013, Biochimica et Biophysica Acta - General SubjectsCitation Excerpt :This step is followed by a slower and rate limiting one in which the acylated protein is deacylated by general acid or base catalysis with the participation of water. Principally the same mechanism was proposed by Ohta et al. [13], who examined the HSA catalyzed hydrolysis of a series of N-trans-cinnamoylimidazoles (amides) and by Kurono et al. [14], who studied the hydrolysis of ten amino acid p-nitrophenyl esters. The latter authors also found that making the esters more hydrophobic by incorporating an N-carbobenzoxy group accelerated the enzymatic activity of HSA; N-carbobenzoxy-d-alanine p-nitrophenyl ester was the best substrate studied.
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