Jump to main content
Jump to site search

Issue 14, 2017
Previous Article Next Article

β-Amyrin biosynthesis: catalytic mechanism and substrate recognition

Author affiliations

Abstract

The enzymatic polycyclization reactions catalyzed by oxidosqualene (OXSQ) cyclases (OSCs) proceed with complete regio- and stereospecificity, leading to the formation of new C–C bonds and chiral centers and to the generation of diverse polycyclic sterols and triterpenoids. The diverse structural array is remarkable, and approximately 150 different carbon frameworks have been found. Detailed investigations on squalene-hopene cyclase (SHC) and lanosterol synthase (LaS) have been reported, but progress in the study of β-amyrin synthase, which is ubiquitously found in plants, has lagged in comparison. In the past several years, remarkable advances in β-amyrin biosynthetic studies have been made. In this review, the catalytic mechanism and substrate recognition of β-amyrin synthase, as revealed by site-directed mutagenesis and substrate analog experiments, are outlined and compared with those of LaS and SHC to highlight the features of β-amyrin synthase.

Graphical abstract: β-Amyrin biosynthesis: catalytic mechanism and substrate recognition

Back to tab navigation

Supplementary files

Article information


Submitted
31 Jan 2017
Accepted
07 Mar 2017
First published
07 Mar 2017

Org. Biomol. Chem., 2017,15, 2869-2891
Article type
Review Article

β-Amyrin biosynthesis: catalytic mechanism and substrate recognition

T. Hoshino, Org. Biomol. Chem., 2017, 15, 2869
DOI: 10.1039/C7OB00238F

Social activity

Search articles by author

Spotlight

Advertisements