Your browser doesn't support javascript.
loading
Characterisation of neprilysin (EC 3.4.24.11) S2' subsite.
Dion, N; Cohen, P; Crine, P; Boileau, G.
Afiliación
  • Dion N; Département de Biochimie, Faculté de Médecine, Université de Montréal, C.P. Succ. Centre-Ville Montréal, Québec, Canada.
FEBS Lett ; 411(1): 140-4, 1997 Jul 07.
Article en En | MEDLINE | ID: mdl-9247159
Neprilysin is a neutral peptidase that cleaves small peptide substrates on the amino-side of hydrophobic amino acid residues. In the present study, we have used inhibition of non-mutated and mutated enzymes with dipeptide inhibitors and hydrolysis of the substrate [Leu5, Arg6]enkephalin in order to evaluate the contribution of the S2' subsite to substrate and inhibitor binding. Our results suggest that (1) Arg-102 and Asn-542 provide major contributions to the interaction of the enzyme with the P2' residue of the substrate, (2) the S2' subsite is vast and can accommodate bulky side chains, and (3) Arg-102 restricts access to the S2' subsite to some side chains such as arginine.
Asunto(s)
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Neprilisina Límite: Animals Idioma: En Revista: FEBS Lett Año: 1997 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Reino Unido
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Neprilisina Límite: Animals Idioma: En Revista: FEBS Lett Año: 1997 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Reino Unido