Mechanistic studies on carboxypeptidase A from goat pancreas Part I: Role of tyrosine residue at the active site.
J Biosci
;
1984 Dec; 6(6): 847-856
Artigo
em Inglês
| IMSEAR
| ID: sea-160432
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.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Idioma:
Inglês
Revista:
J Biosci
Ano de publicação:
1984
Tipo de documento:
Artigo
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