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Expression, crystallization and structure elucidation of γ‐terpinene synthase from Thymus vulgaris
Author(s) -
Rudolph Kristin,
Parthier Christoph,
EgererSieber Claudia,
Geiger Daniel,
Muller Yves A.,
Kreis Wolfgang,
MüllerUri Frieder
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15023043
Subject(s) - atp synthase , lamiaceae , thymol , stereochemistry , chemistry , enzyme , biosynthesis , biochemistry , terpenoid , biology , essential oil , botany , chromatography
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 ( Tv TPS), 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 Tv TPS is reported at 1.65 Å resolution, confirming the dimeric structure of the enzyme. The putative active site of Tv TPS 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 (4 S )‐limonene synthase from Mentha spicata .