Structural and functional analyses of a bacterial homologue of hormone-sensitive lipase from a metagenomic library

The crystal structure of Est25, a bacterial homologue of hormone-sensitive lipase (HSL), was determined at 1.49 Å resolution. The biochemical properties of Est25 were investigated to clarify the functional capacities of HSL and the potential applications of Est25 in biotechnology.

Structure-based elucidation of the regulatory mechanism for aminopeptidase activity

Crystallographic, functional and single-molecule studies of aminopeptidase PepS have been presented. Substrate length selectivity imposed by the substrate binding hole is a key in the regulation of the catalytic activity along with residue specificity and active-site repositioning.