5C05

Crystal Structure of Gamma-terpinene Synthase from Thymus vulgaris

5C05 の概要

• エントリーDOI: 10.2210/pdb5c05/pdb
• 分子名称: Putative gamma-terpinene synthase, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: terpenoid synthesis, gamma-terpinene, plant, terpene, plant protein, biosynthetic protein
• 由来する生物種: Thymus vulgaris (Thyme)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 131196.11

構造登録者

Parthier, C.P.,Rudolph, K.,Muller, Y.A.,Mueller-Uri, F. (登録日: 2015-06-12, 公開日: 2016-01-13, 最終更新日: 2024-01-10)

主引用文献

Rudolph, K.,Parthier, C.,Egerer-Sieber, C.,Geiger, D.,Muller, Y.A.,Kreis, W.,Muller-Uri, F.
Expression, crystallization and structure elucidation of gamma-terpinene synthase from Thymus vulgaris.
Acta Crystallogr.,Sect.F, 72:16-23, 2016

PubMed Abstract: The biosynthesis of γ-terpinene, a precursor of the phenolic isomers thymol and carvacrol found in the essential oil from Thymus sp., is attributed to the activitiy of γ-terpinene synthase (TPS). Purified γ-terpinene synthase from T. vulgaris (TvTPS), the Thymus species that is the most widely spread and of the greatest economical importance, is able to catalyze the enzymatic conversion of geranyl diphosphate (GPP) to γ-terpinene. The crystal structure of recombinantly expressed and purified TvTPS is reported at 1.65 Å resolution, confirming the dimeric structure of the enzyme. The putative active site of TvTPS is deduced from its pronounced structural similarity to enzymes from other species of the Lamiaceae family involved in terpenoid biosynthesis: to (+)-bornyl diphosphate synthase and 1,8-cineole synthase from Salvia sp. and to (4S)-limonene synthase from Mentha spicata.

PubMed: 26750479
DOI: 10.1107/S2053230X15023043

実験手法

X-RAY DIFFRACTION (1.65 Å)