Mechanistic studies on carboxypeptidase A from goat pancreas Part I: Role of tyrosine residue at the active site.
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Date
1984-12
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Abstract
Chemical modification of carboxypeptidase Ag1 from goat pancreas with Nacetylimidazole
or iodine led to loss of enzymic activity. This loss in activity could be prevented
when chemical modification was carried out in the presence of β-phenylpropionic acid or
substrate NCbz-glycyl-L-phenylalanine, thus suggesting a tyrosine residue at the active site.
Chemical modification of tyrosine was confirmed by spectral and kinetic studies. While
tyrosine modification destroyed peptidase activity, esterase activity of the enzyme remained
unchanged thus indicating non-involvement of tyrosine residue in ester hydrolysis.
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Keywords
Tyrosine, active site, goat carboxypeptidase, iodine, N-acetylimidazole
Citation
Dua R D, Gupta Kamlesh. Mechanistic studies on carboxypeptidase A from goat pancreas Part I: Role of tyrosine residue at the active site. Journal of Biosciences. 1984 Dec; 6(6): 847-856.