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Kampranis, S.C., Ioannidis, D., Purvis, A., Mahrez, W., Ninga, N., Katerelos, N.A., Ansour, S., Dunwell, J.M., Degenhardt, J., Makris, A.M., Goodenough, P.W. and Johnson, C.B. (2007) Rational conversion of substrate and product specificity in a Salvia monoterpene synthase: Structural insights into the evolution of terpene synthase function. Plant Cell, 19, 1994-2005. doi:10.1105/tpc.106.047779

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• 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.