Structural Insights into the Molecular Evolution of the Archaeal Exo-?-d-Glucosaminidase.

ABSTRACT: The archaeal exo-?-d-glucosaminidase (GlmA), a thermostable enzyme belonging to the glycosidase hydrolase (GH) 35 family, hydrolyzes chitosan oligosaccharides into monomer glucosamines. GlmA is a novel enzyme in terms of its primary structure, as it is homologous to both GH35 and GH42 ?-galactosidases. The catalytic mechanism of GlmA is not known. Here, we summarize the recent reports on the crystallographic analysis of GlmA. GlmA is a homodimer, with each subunit comprising three distinct domains: a catalytic TIM-barrel domain, an ?/? domain, and a ?1 domain. Surprisingly, the structure of GlmA presents features common to GH35 and GH42 ?-galactosidases, with the domain organization resembling that of GH42 ?-galactosidases and the active-site architecture resembling that of GH35 ?-galactosidases. Additionally, the GlmA structure also provides critical information about its catalytic mechanism, in particular, on how the enzyme can recognize glucosamine. Finally, we postulate an evolutionary pathway based on the structure of an ancestor GlmA to extant GH35 and GH42 ?-galactosidases.

SUBMITTER: Mine S 

PROVIDER: S-EPMC6566704 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature