Theoretical studies of Rhizomucor miehei lipase activation

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Abstract
Computational methods have been used to study the extensive conformational change of Rhizomucor miehei lipase upon activation. Hie present study considers the possible activation route, the energies involved and molecular interactions during the conformational change of the lipase in a hydrophobic environment. The conformational change was studied by conventional molecular dynamics methods and with a combined molecular dynamics and mechanics protocol, in which the conformational change was simulated by restraining Cor pseudotorsional angles in small steps between the two crystallographically observed positions of the lid. In the closed conformer of the enzyme the active site is completely buried under a short helical loop, ‘the lid’. The activation of the lipase consists of a movement of the lid, which results in an open conformer with an exposed active she. From the results of the simulations in the present work we suggest that the lipase in a hydrophobic environment is stabilized in the open form by electrostatic interactions.

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