Thiorphan, tiopronin, and related analogs as substrates and inhibitors of peptidylglycine alpha-amidating monooxygenase (PAM).
FEBS Lett
; 580(2): 521-32, 2006 Jan 23.
Article
en En
| MEDLINE
| ID: mdl-16405966
ABSTRACT
Peptidyglycine alpha-amidating monooxygenase is a copper- and zinc-dependent, bifunctional enzyme that catalyzes the cleavage of glycine-extended peptides or N-acylglycines to the corresponding amides and glyoxylate. This reaction is a key step in the biosynthesis of bioactive alpha-amidated peptides and, perhaps, the primary fatty acids amides also. Two clinically useful N-acylglycines are thiorphan and tiopronin, each with a thiol moiety attached to the acyl group. We report here that thiorphan and tiopronin are substrates for PAM, exhibiting relatively low K(M,app) and V(MAX,app) values. The low V(MAX,app) values result, most likely, from a decrease in active PAM.2Cu(II) as the enzyme competes ineffectively with thiorphan and tiopronin for free copper.
Buscar en Google
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Inhibidores de Proteasas
/
Tiorfan
/
Oxigenasas de Función Mixta
/
Tiopronina
/
Complejos Multienzimáticos
Límite:
Animals
Idioma:
En
Revista:
FEBS Lett
Año:
2006
Tipo del documento:
Article
País de afiliación:
Estados Unidos