Activity and Dynamics of an Enzyme, Pig Liver Esterase, in Near-Anhydrous Conditions

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Activity and dynamics of an enzyme, pig liver esterase, in near-anhydrous conditions.

Water is widely assumed to be essential for life, although the exact molecular basis of this requirement is unclear. Water facilitates protein motions, and although enzyme activity has been demonstrated at low hydrations in organic solvents, such nonaqueous solvents may allow the necessary motions for catalysis. To examine enzyme function in the absence of solvation and bypass diffusional const...

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Force field and first principles molecular dynamics simulations on complexes of pig liver esterase (pig liver isoenzymes and a mutant) and selected substrates (1-phenyl-1-ethyl acetate, 1phenyl-2-butylacetate, proline-β-naphthylamide and methyl butyrate) are presented. By restrained force field simulations the access of the substrate to the hidden active site was probed. For a few substrates sp...

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In order to gain a more detailed insight into the relationship between substrate structure and the stereoselectivity of the enzyme pig liver esterase (E.C. 3.1.1 .I .) a large series of mainly meso and prochiral diesters with an open chain or a cyclic structure has been studied and evaluated. Results obtained with 3substituted cyclopropane-l,2-dicarboxylates are incompatible with the three-dime...

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ژورنال

عنوان ژورنال: Biophysical Journal

سال: 2010

ISSN: 0006-3495

DOI: 10.1016/j.bpj.2010.07.066