Enzymes must be ordered to allow the stabilization of transition states by their active sites,
yet dynamic enough to adopt alternative conformations suited to other steps in their catalytic …

Organophosphate-degrading enzyme from Agrobacterium radiobacter P230 (OPDA) is a
recently discovered enzyme that degrades a broad range of organophosphates. It is very …

The α/βhydrolase superfamily has rapidly expanded in recent years and continues to do so
at an expeditious pace. According to the ESTHER database (http://bioweb.ensam.inra.fr/…

The ϵ subunit of the Escherichia coli replicative DNA polymerase III is the proofreading 3′–5′
exonuclease. Structures of its catalytic N-terminal domain (ϵ186) were determined at …

Insect carboxylesterases from the αEsterase gene cluster, such as αE7 (also known as E3)
from the Australian sheep blowfly Lucilia cuprina (LcαE7), play an important physiological …

To efficiently catalyze a chemical reaction, enzymes are required to maintain fast rates for
formation of the Michaelis complex, the chemical reaction and product release. These distinct …

Azole drugs selectively target fungal sterol biosynthesis and are critical to our antifungal
therapeutic arsenal. However, resistance to this class of drugs, particularly in the major human …

The emergence of enzymes through the neofunctionalization of noncatalytic proteins is
ultimately responsible for the extraordinary range of biological catalysts observed in nature. …

Developments in computational chemistry, bioinformatics, and laboratory evolution have
facilitated the de novo design and catalytic optimization of enzymes. Besides creating useful …

Characterizing the adaptive landscapes that encompass the emergence of novel enzyme
functions can provide molecular insights into both enzymatic and evolutionary mechanisms. …