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Updated: Aug 15, 2026

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Published on: August 14, 2019
A novel hydroxylase from Catharanthus roseus participating in the hydroxylation of 2-hydroxybenzoic acid
Kei Shimoda1, Naoji Kubota, Takayuki Sano
1Department of Pharmacology and Therapeutics, Faculty of Medicine, Oita University, 1-1 Hasama-machi, Oita 879-5593, Japan. shimoda@med.oita-u.ac.jp
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.
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