TITLE:
Determination of amino-acidic positions important for Ocimum basilicum geraniol synthase activity
AUTHORS:
Marc J. C. Fischer, Sophie Meyer, Patricia Claudel, Damien Steyer, Marc Bergdoll, Philippe Hugueney
KEYWORDS:
Geraniol Synthase; Heterologous Expression; Monoterpenols; Point Mutations; Yeast
JOURNAL NAME:
Advances in Bioscience and Biotechnology,
Vol.4 No.2,
February
28,
2013
ABSTRACT: Terpenes are one of the largest and most diversified
families of natural compounds. Although they have found numerous industrial applications,
the molecular basis of their synthesis in plants has, until now, not been fully
understood. Plant genomes have been shown to contain dozens of terpene synthase
(TPS) genes, however knowledge of their amino-acidic protein sequence in not sufficient
to predict which terpene(s) will be produced by a particular enzyme. In order
to investigate the structural basis of a TPS specificity, we performed site directed
mutations in the geraniol synthase from Ocimum
basilicum. The results obtained suggest that a specific region on the catalytic
site plays an important role in GPP transformation, either by stabilizing the
GPP substrate on the catalytic site, or by enabling its transformation into a monoterpenol via an intermediate carbocation.