The Key Role of Phloroglucinol O-Methyltransferase in the Biosynthesis of Rosa chinensis Volatile 1,3,5-Trimethoxybenzene | Zendy

Shuiqin Wu | Zendy; Naoharu Watanabe | Zendy; Satoru Mita | Zendy; Hideo Dohra | Zendy; Yoshihiro Ueda | Zendy; Masaaki Shibuya | Zendy; Yutaka Ebizuka | Zendy

Open Access

The Key Role of Phloroglucinol O-Methyltransferase in the Biosynthesis of Rosa chinensis Volatile 1,3,5-Trimethoxybenzene

Author(s) -

Shuiqin Wu,

Naoharu Watanabe,

Satoru Mita,

Hideo Dohra,

Yoshihiro Ueda,

Masaaki Shibuya,

Yutaka Ebizuka

Publication year - 2004

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.103.037051

Subject(s) - phloroglucinol , orcinol , enzyme , o methyltransferase , chemistry , methyltransferase , biochemistry , escherichia coli , petal , biosynthesis , stereochemistry , methylation , substrate (aquarium) , biology , organic chemistry , botany , gene , ecology

1,3,5-Trimethoxybenzene is a key component of the Chinese rose odor. This compound is synthesized in three successive methylation steps from phloroglucinol, the initial precursor. A novel, to our knowledge, phloroglucinol O-methyltransferase (POMT) characterized here methylates the first step to produce the intermediate 3,5-dihydroxyanisole, while two previously described orcinol O-methyltransferases catalyze the subsequent steps. We isolated POMT from rose petals and determined partial amino acid sequences of the purified enzyme. The full-length POMT cDNA was isolated and expressed in Escherichia coli. Both the native and recombinant POMT exhibited substrate specificity for phloroglucinol. POMT was expressed specifically in floral organs, in accordance with its role as a key enzyme in the synthesis of rose floral scent compounds.

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