A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase.
Science
; 248(4958): 981-7, 1990 May 25.
Article
em En
| MEDLINE
| ID: mdl-2111581
ABSTRACT
An active site, cofactor-containing peptide has been obtained in high yield from bovine serum amine oxidase. Sequencing of this pentapeptide indicates Leu-Asn-X-Asp-Tyr. Analysis of the peptide by mass spectrometry, ultraviolet-visible spectroscopy, and proton nuclear magnetic resonance leads to the identification of X as 6-hydroxydopa. This result indicates that, contrary to previous proposals, pyrroloquinoline quinone is not the active site cofactor in mammalian copper amine oxidases. Although 6-hydroxydopa has been implicated in neurotoxicity, the data presented suggest that this compound has a functional role at an enzyme active site.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Di-Hidroxifenilalanina
/
Amina Oxidase (contendo Cobre)
/
Oxirredutases atuantes sobre Doadores de Grupo CH-NH
Limite:
Animals
Idioma:
En
Revista:
Science
Ano de publicação:
1990
Tipo de documento:
Article