Structural and functional insights into extreme thermal stability and activity of two GH12 domains of a multidomain glycosidase from a hyperthermophilic euryarchaeon.

ABSTRACT: Bacteria and fungi are well known for efficient degradation of plant polysaccharides thanks to various enzymes involved in plant cell wall decomposition. However, little is known about the role of archaea in this process or the repertoire and features of their polysaccharide-degrading enzymes. In our previous work, we discovered an archaeal multidomain glycosidase (MDG) composed of three catalytic domains (GH5 and two GH12) and two cellulose-binding modules (CBM2). The recombinant MDG and individual GH5 catalytic domain were active against cellulose and a number of other polysaccharides at a wide range of temperatures, with optimum temperatures (T_opt) of 60 °C and 80 °C, respectively. The present study was focused on the characterization of two GH12 domains of the MDG. Purified

SUBMITTER: Zayulina KS 

PROVIDER: S-EPMC12265866 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature