Quarter of a Century after: A Glimpse at the Conformation and Mechanism of <i>Candida antarctica</i> Lipase B

Abstract

Lipase B from Candida antarctica (CAL-B) belongs to the family of α/β-hydrolases, and is one from the most extensively used biocatalysts in the kinetic resolution of amines and alcohols in a racemic state, in the desymmetrization of diacetates or diols, and in the stereoselective synthesis of chiral intermediate compounds for obtaining the various pharmaceuticals and agents which protect plants. There are also many cases of promiscuous reactions catalyzed by CAL-B. The number of very important results appeared recently in the literature in the years 2015–2019, regarding the crystal structure and conformation of CAL-B molecule. Before 2015, there was a long period of a complete lack of information concerning this enzyme’s structure. The earlier reports about CAL-B structure were dated between 1994–1995, and did not provide enough conclusions about the mechanism of the enzyme. The recently solved structures give a hint of the enzyme mechanism in three dimensions.

Keywords

• CAL-B
• crystallographic polymorphism
• enzyme promiscuity
• lipase activity
• esterase activity
• macromolecular crystallography