Model for the functional active site of Baeyer–Villigerases. X-Ray crystal data for (1S,2R,5R,8S,1′R)-8-endo-benzoyloxy-N-(1′-phenylethyl)bicyclo[3.3.0]octane-2-endo-carboxamide

Autor:	Andrew Willetts, Peter W. H. Wan, Christopher J. Knowles, David E. Hibbs, Adel K. Mish'al, Stanley M. Roberts, Gideon Grogan, Michael B. Hursthouse, Jassem G. Mahdi, Michael Wright, David R. Kelly, Ian N. Taylor
Rok vydání:	1995
Předmět:	chemistry.chemical_classification Ketone biology Bicyclic molecule medicine.drug_class Chemistry Stereochemistry Active site Carboxamide biology.organism_classification Peroxide Pseudomonas putida chemistry.chemical_compound medicine biology.protein Lactone Octane
Zdroj:	J. Chem. Soc., Perkin Trans. 1. :2057-2066
ISSN:	1364-5463 0300-922X
DOI:	10.1039/p19950002057
Popis:	An active-site model for enzyme-catalysed Baeyer–Villiger reactions is proposed and tested by transformation of the tricyclic ketone 6 to the lactone 7( > 98% ee) using purified enzymes from Acinetobacter sp. NCIMB 9871 and Pseudomonas putida NCIMB 10 007 (MO1). The absolute stereochemistry of the lactone 7 was determined by a single-crystal X-ray diffraction structure determination of the (1R′)-α-methylbenzylamide benzoate derivative 11b. Baeyer–Villiger reactions (and Baeyer–Villigerases) are classified by the stereochemistry of the active site and the hydroxy peroxide intermediates.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::8352d12d6b6454f4e3708b46c3c9d70c https://doi.org/10.1039/p19950002057 Zobrazit plný text záznamu