Trapping biosynthetic acyl-enzyme intermediates with encoded 2,3-diaminopropionic acid.

ABSTRACT: Many enzymes catalyse reactions that proceed through covalent acyl-enzyme (ester or thioester) intermediates¹. These enzymes include serine hydrolases^2,3 (encoded by one per cent of human genes, and including serine proteases and thioesterases), cysteine proteases (including caspases), and many components of the ubiquitination machinery^4,5. Their important acyl-enzyme intermediates are unstable, commonly having half-lives of minutes to hours⁶. In some cases, acyl-enzyme complexes can be stabilized using substrate analogues or active-site mutations but, although these approaches can provide valuable insight^7-10, they often result in complexes that are substantially non-native. Here we develop a strategy for incorporating 2,3-diaminoprop

SUBMITTER: Huguenin-Dezot N 

PROVIDER: S-EPMC6436733 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature