Purification and characterization of alpha-3 ',4 '-anhydrovinblastine synthase (peroxidase-like) from Catharanthus roseus (L) G. Don

• Tipo: Artigo em Revista Científica Internacional
• Data: 1998

Autores

Sottomayor, M (Autor) FCUP; Lopez Serrano, M (Autor) Outra; DiCosmo, F (Autor) Outra; Barcelo, AR (Autor) Outra

Revista

Título: FEBS Letters

Vol. 428

Páginas: 299-303

ISSN: 0014-5793

Editora: Wiley-Blackwell

Indexação

ISI Web of Knowledge - 58 Citações

Scopus - 82 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

Outras Informações

ID Authenticus: P-001-7WR

DOI: 10.1016/s0014-5793(98)00551-1

Abstract (EN): An H2O2-dependent enzyme capable of coupling catharanthine and vindoline into alpha-3',4'-anhydrovinblastine (AVLB) was purified to apparent homogeneity from Catharanthus roseus leaves. The enzyme shows a specific AVLB synthase activity of 1.8 nkat/mg, and a molecular weight of 45.40 kDa (SDS-PAGE), In addition to AVLB synthase activity, the purified enzyme shows peroxidase activity, and the VIS spectrum of the protein presents maxima at 404, 501 and 633 nm, indicating that it is a high spin ferric heme protein, belonging to the plant peroxidase superfamily, Kinetic studies revealed that both catharanthine and vindoline were substrates of the enzyme, AVLB being the major coupling product. (C) 1998 Federation of European Biochemical Societies.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 5