The acid-base-nucleophile catalytic triad in ABH-fold enzymes is coordinated by a set of structural elements.

ABSTRACT: The alpha/beta-Hydrolases (ABH) are a structural class of proteins that are found widespread in nature and includes enzymes that can catalyze various reactions in different substrates. The catalytic versatility of the ABH fold enzymes, which has been a valuable property in protein engineering applications, is based on a similar acid-base-nucleophile catalytic mechanism. In our research, we are concerned with the structure that surrounds the key units of the catalytic machinery, and we have previously found conserved structural organizations that coordinate the catalytic acid, the catalytic nucleophile and the residues of the oxyanion hole. Here, we explore the architecture that surrounds the catalytic histidine at the active sites of enzymes from 40 ABH fold families, where we have identif

SUBMITTER: Denesyuk A 

PROVIDER: S-EPMC7034887 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature