Emerging evidence indicates that the factors that control enzyme efficiency include internal protein dynamics or the protein conformational fluctuations. Computational investigations indicate that the reaction-coupled flexibility is a conserved aspect of the enzyme molecular architecture and promotes catalysis. The hypothesis of promoting role of enzyme dynamics in function has been tested by engineering a hyper-catalytic enzyme to selectively modulate enzyme conformation through external stimulus. An engineered enzyme has been prepared that allows modulation of enzyme conformation through photo-activation. Result will be presented that show that modulation of the reaction coupled dynamics show about 30 fold improvement in the activity of Candida antarctica lipase B over the wild type enzyme.

Engineering hyper-catalytic enzyme by photo-activated conformation modulation

244th National Meeting (2012)

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