Affordable Access

A novel hydroxylase from Catharanthus roseus participating in the hydroxylation of 2-hydroxybenzoic acid.

Authors
  • Shimoda, Kei
  • Kubota, Naoji
  • Sano, Takayuki
  • Hirakawa, Hidetada
  • Hirata, Toshifumi
Type
Published Article
Journal
Journal of Bioscience and Bioengineering
Publisher
Elsevier
Publication Date
Jan 01, 2004
Volume
98
Issue
2
Pages
67–70
Identifiers
PMID: 16233668
Source
Medline
License
Unknown

Abstract

A novel 55-kDa hydroxylase was isolated from cultured cells of Catharanthus roseus by a three-step procedure: anion exchange chromatography, affinity chromatography and hydroxylapatite adsorption chromatography. The enzyme specifically catalyzed the hydroxylation of 2-hydroxybenzoic acid to give 2,5-dihydroxybenzoic acid. The enzyme activity was optimal at pH 7.8 and was completely inhibited by divalent cations, such as Cu(2+) and Hg(2+). The enzyme showed sequence similarity to certain plant flavonoid 3'-hydroxylases.

Report this publication

Statistics

Seen <100 times