Next Article in Journal
Next Article in Special Issue
Previous Article in Journal
Previous Article in Special Issue
Molecules 2010, 15(4), 2070-2078; doi:10.3390/molecules15042070
Review

Norcoclaurine Synthase: Mechanism of an Enantioselective Pictet-Spengler Catalyzing Enzyme

1, 2, 2, 1 and 1,*
Received: 2 March 2010; in revised form: 18 March 2010 / Accepted: 22 March 2010 / Published: 24 March 2010
(This article belongs to the Special Issue Bifunctional Catalysis)
Download PDF [135 KB, uploaded 18 June 2014]
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 as chiral building blocks for drugs and agrochemicals. Moreover, enzymatic synthesis may offer the advantage of a clean and green synthetic process in the absence of organic solvents and metal catalysts. In this work the reaction mechanism of norcoclaurine synthase is described. This enzyme catalyzes the Pictet-Spengler condensation of dopamine with 4-hydroxyphenylacetaldehyde (4-HPAA) to yield the benzylisoquinoline alkaloids central precursor, (S)-norcoclaurine. Kinetic and crystallographic data suggest that the reaction mechanism occurs according to a typical bifunctional catalytic process.
Keywords: norcoclaurine synthase; (S)-norcoclaurine; Pictet-Spengler condensation; bifunctional catalysis; green synthetic process norcoclaurine synthase; (S)-norcoclaurine; Pictet-Spengler condensation; bifunctional catalysis; green synthetic process
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Export to BibTeX |
EndNote


MDPI and ACS Style

Bonamore, A.; Barba, M.; Botta, B.; Boffi, A.; Macone, A. Norcoclaurine Synthase: Mechanism of an Enantioselective Pictet-Spengler Catalyzing Enzyme. Molecules 2010, 15, 2070-2078.

AMA Style

Bonamore A, Barba M, Botta B, Boffi A, Macone A. Norcoclaurine Synthase: Mechanism of an Enantioselective Pictet-Spengler Catalyzing Enzyme. Molecules. 2010; 15(4):2070-2078.

Chicago/Turabian Style

Bonamore, Alessandra; Barba, Marco; Botta, Bruno; Boffi, Alberto; Macone, Alberto. 2010. "Norcoclaurine Synthase: Mechanism of an Enantioselective Pictet-Spengler Catalyzing Enzyme." Molecules 15, no. 4: 2070-2078.



Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert