Clarkia breweri methyltransferase: A QM/MM study

DEFELIPE, LUCAS ALFREDO; MARTI, MARCELO ADRIÁN; TURJANSKI, ADRIAN GUSTAVO

Córdoba

Congreso; 2do Congreso Argentino de Bioinformática y Biología Computacional; 2011

Asociación Argentina de Bioinformática y Biología Computacional

The methylation of small organic compounds is a broad reaction found in prokaryotes andeukaryotes metabolic pathways. The methylation is catalyzed by S- adenosyl-L-methionine(SAM) dependant methyltransferases that transfer the Methyl group from SAM to differentacceptors like ubiquinone [1], fatty acids [2] and cathecol [3].Clarkia breweri is a small plant where the formation of methyl salicylic acid (SA) is mediated by a methyltransferase (CbMT) [4]. The protein has been crystallized with SAH and SA in  the active site and it has been suggested that the protein´s primary role is to facilitate the encounter of the reactives but not to reduce the activation barrier [4]. To to get an integral view on the enzymatic activity of CbMT we run Molecular Dynamics (MD) simulations [5] of the enzimatic complex and Quantum Mechanics/Molecular Mechanics (QM/MM) simulations.