| Téléchargement | - Voir le manuscrit accepté : Lactone-bound structures of cyclohexanone monooxygenase provide insight into the stereochemistry of catalysis (PDF, 898 Kio)
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| DOI | Trouver le DOI : https://doi.org/10.1021/cb500442e |
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| Auteur | Rechercher : Yachnin, Brahm J.; Rechercher : McEvoy, Michelle B.; Rechercher : Maccuish, Roderick J. D.; Rechercher : Morley, Krista L.1; Rechercher : Lau, Peter C. K.; Rechercher : Berghuis, Albert M. |
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| Affiliation du nom | - Conseil national de recherches du Canada. Développement des cultures et des ressources aquatiques
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| Format | Texte, Article |
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| Sujet | cyclohexanone; enzyme; lactone; microbial enzyme; polycaprolactone; unspecific monooxygenase; binding site; catalysis; conformational transition; crystal structure; enzyme structure; oxidation; protein conformation; protein cross linking; stereochemistry; stereospecificity |
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| Résumé | The Baeyer-Villiger monooxygenases (BVMOs) are microbial enzymes that catalyze the synthetically useful Baeyer-Villiger oxidation reaction. The available BVMO crystal structures all lack a substrate or product bound in a position that would determine the substrate specificity and stereospecificity of the enzyme. Here, we report two crystal structures of cyclohexanone monooxygenase (CHMO) with its product, ε-caprolactone, bound: the CHMOTight and CHMOLoose structures. The CHMOTight structure represents the enzyme state in which substrate acceptance and stereospecificity is determined, providing a foundation for engineering BVMOs with altered substrate spectra and/or stereospecificity. The CHMOLoose structure is the first structure where the product is solvent accessible. This structure represents the enzyme state upon binding and release of the substrate and product. In addition, the role of the invariant Arg329 in chaperoning the substrate/product during the catalytic cycle is highlighted. Overall, these data provide a structural framework for the engineering of BVMOs with altered substrate spectra and/or stereospecificity. |
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| Date de publication | 2014-09-29 |
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| Dans | |
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| Langue | anglais |
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| Publications évaluées par des pairs | Oui |
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| Numéro du CNRC | NRC-ACRD-56113 |
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| Numéro NPARC | 21275605 |
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| Exporter la notice | Exporter en format RIS |
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| Signaler une correction | Signaler une correction (s'ouvre dans un nouvel onglet) |
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| Identificateur de l’enregistrement | 1e2b203d-281c-480e-8f7c-309ea82bfa26 |
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| Enregistrement créé | 2015-07-14 |
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| Enregistrement modifié | 2020-06-04 |
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