| Application of a SCC-DFTB QM/MM approach to the investigation of the catalytic mechanism of fatty acid amide hydrolase. | |
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MedLine Citation:
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PMID: 21365225 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Self-consistent charge density functional tight binding (SCC-DFTB) is a promising method for hybrid quantum mechanics/molecular mechanics (QM/MM) simulations of enzyme-catalyzed reactions. The acylation reaction of fatty acid amide hydrolase (FAAH), a promising drug target, was investigated by applying a SCC-DFTB/CHARMM27 scheme. Calculated potential energy barriers resulted in reasonable agreement with experiments for oleamide (OA) and oleoylmethyl ester (OME) substrates, outperforming previous calculations performed at the PM3/CHARMM22 level. Furthermore, the experimental preference of FAAH in hydrolyzing OA faster than OME was adequately reproduced by calculations. All these findings indicate that the SCC-DFTB/CHARMM27 approach can be successfully applied to mechanistic investigations of FAAH-catalyzed reactions. |
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Authors:
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Luigi Capoferri; Marco Mor; Jitnapa Sirirak; Ewa Chudyk; Adrian J Mulholland; Alessio Lodola |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-3-2 |
Journal Detail:
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Title: Journal of molecular modeling Volume: - ISSN: 0948-5023 ISO Abbreviation: - Publication Date: 2011 Mar |
Date Detail:
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Created Date: 2011-3-2 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9806569 Medline TA: J Mol Model Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Dipartimento Farmaceutico, Università degli Studi di Parma, viale G. P. Usberti 27/A Campus Universitario, 43124, Parma, Italy. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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