Substrate specificity of an acylaminopeptidase that catalyzes the cleavage of the blocked amino termini of peptides.
Biochim Biophys Acta
; 953(3): 357-60, 1988 Apr 14.
Article
em En
| MEDLINE
| ID: mdl-3128332
ABSTRACT
An acylaminopeptidase purified from human red cells cleaves acetylated dipeptides in the decreasing order of acetyl-Ala, acetyl-Met, acetyl-Ser, acetyl-Gly and acetyl-Val. In addition, it was also found that the nature of the second amino-acid residue influenced the rate of cleavage of the blocked N-terminus charged residues at the second position lead to reduced rates of cleavage. The possible use of this enzyme for structural studies on blocked peptide or protein substrates is evaluated.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Dipeptídeos
/
Eritrócitos
/
Aminopeptidases
Limite:
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1988
Tipo de documento:
Article