norcoclaurine synthase mechanism of an enantioselective pictet-spengler catalyzing enzymenorcoclaurine合酶机制的拆分pictet-spengler催化酶.pdfVIP

Molecules 2010, 15, 2070-2078; doi:10.3390/molecule OPEN ACCESS molecules ISSN 1420-3049 /journal/molecules Review Norcoclaurine Synthase: Mechanism of an Enantioselective Pictet-Spengler Catalyzing Enzyme Alessandra Bonamore 1, Marco Barba 2, Bruno Botta 2, Alberto Boffi 1 and Alberto Macone 1,* 1 Dipartimento di Scienze Biochimiche, Università “Sapienza” P. Aldo Moro 5, 00185, Rome, Italy 2 Dipartimento di Studi di Chimica e Tecnologia delle Sostanze Biologicamente Attive, Università “Sapienza” P. Aldo Moro 5, 00185, Rome, Italy * Author to whom correspondence should be addressed; E-Mail: alberto.macone@uniroma1.it; Tel.: +39-(0)6-4991-0813; Fax: +39-(0)6-444-0062. Received: 2 March 2010; in revised form: 18 March 2010 / Accepted: 22 March 2010 / Published: 24 March 2010 Abstract: The use of bifunctional catalysts in organic synthesis finds inspiration in the selectivity of enzymatic catalysis which arises from the specific interactions between basic and acidic amino acid residues and the substrate itself in order to stabilize developing charges in the transition state. Many enzymes act as bifunctional catalysts using amino acid residues at the active site as Lewis acids and Lewis bases to modify the substrate as required for the given transformation. They bear a clear advantage over non-biological methods for their ability to tackle problems related to the synthesis of enantiopure compounds