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A Novel Self-Activation Mechanism of Candida antarctica Lipase B


The Candida antarctica lipase B (CalB), resembling many other lipases structure-wise, contains a flexible lid that undergoes a surprisingly large conformational change when catalyzing hydrophobic substrates (e.g. triglycerides). Despite extensive and important applications in industry, it is so far still elusive whether CalB can be activated on a hydrophobic surface, like other lipases. From large-scale all-atom molecular dynamics simulations, we discovered an open state that strikingly shows a much wider and more stable entrance to the catalytic site than the one suggested by previous crystal structures. Simulations demonstrate that in the newly found open state CalB possesses a ``lid-holder'' structure that intimately harbors the lid of CalB, i.e. a remarkable self-activation mechanism. To account for the unusual interfacial activation of CALB revealed in a recent experiment, we further introduce a simple model: the activation happens only when the binding free energy between the lid and a hydrophobic surface is larger than a critical value, 4.0 kcal/mol that is the one between the lid and the ``lid-holder''. Our findings shed light on possible protein engineering of lipases to permit either the self-activation with broadened catalytic targets (including water soluble ones) or the surface activation with elevated activities.

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Publication details

The article was received on 05 Apr 2017, accepted on 18 May 2017 and first published on 19 May 2017

Article type: Paper
DOI: 10.1039/C7CP02198D
Citation: Phys. Chem. Chem. Phys., 2017, Accepted Manuscript
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    A Novel Self-Activation Mechanism of Candida antarctica Lipase B

    B. Luan and R. Zhou, Phys. Chem. Chem. Phys., 2017, Accepted Manuscript , DOI: 10.1039/C7CP02198D

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