The hydrolysis mechanism of a GH45 cellulase and its potential relation to lytic transglycosylase and expansin function.

ABSTRACT: Family 45 glycoside hydrolases (GH45) are endoglucanases that are integral to cellulolytic secretomes, and their ability to break down cellulose has been successfully exploited in textile and detergent industries. In addition to their industrial relevance, understanding the molecular mechanism of GH45-catalyzed hydrolysis is of fundamental importance because of their structural similarity to cell wall-modifying enzymes such as bacterial lytic transglycosylases (LTs) and expansins present in bacteria, plants, and fungi. Our understanding of the catalytic itinerary of GH45s has been incomplete because a crystal structure with substrate spanning the -1 to +1 subsites is currently lacking. Here we constructed and validated a putative Michaelis complex in silico and used it to elucidate

SUBMITTER: Bharadwaj VS 

PROVIDER: S-EPMC7135978 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature