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

• Type: Article in International Scientific Journal
• Date: 1998

Authors

Sottomayor, M (Author) FCUP; Lopez Serrano, M (Author) Other; DiCosmo, F (Author) Other; Barcelo, AR (Author) Other

Journal

Title: FEBS Letters

Vol. 428

Pages: 299-303

ISSN: 0014-5793

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 58 Citations

Scopus - 82 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 5