An essential tryptophan residue in alkaline phosphatase from pearl oyster (Pinctada fucata).
Biochemistry (Mosc)
; 73(1): 87-91, 2008 Jan.
Article
em En
| MEDLINE
| ID: mdl-18294135
ABSTRACT
Alkaline phosphatases are ubiquitous enzymes found in most species including the pearl oyster, Pinctada fucata, where it is presumably involved in nacreous biomineralization processes. In the present study, we have purified alkaline phosphatases from the pearl oyster and modified the tryptophan residues using N-bromosuccinimide (NBS). We show that the resulting inactivation of purified alkaline phosphatase by NBS is dependent on modification of only one of five tryptophan residues in the enzyme. Substrate protection experiments showed that the tryptophan residue was not located at the substrate-binding site but was involved in the catalytic activity.
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Base de dados:
MEDLINE
Assunto principal:
Triptofano
/
Fosfatase Alcalina
/
Pinctada
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article