Structure-function relationship of the GH168 fucanase reveals an unusual enzyme recognition mechanism for sulfated polysaccharide.
Ontology highlight
ABSTRACT: Sulfated fucan is one of the most recalcitrant polysaccharides. The molecular mechanism underlying the endo-1,3-fucanase, which plays a critical role in the breakdown of sulfated fucan, remains unexplained. Here, we conduct a comprehensive structure-function relationship investigation on the endo-1,3-fucanases within a family space-GH168. The family can be divided into four subfamilies according to phylogenetic relationship and functional similarities. Subfamily I, Ⅱ and Ⅳ preferentially recognize Fucp2(OSO3-), Fucp2,4(OSO3-) and Fucp units at the +1 subsite, respectively, while consistently recognizing the Fucp2(OSO3-) unit at the -1 subsite. Remarkably, two-thirds of the interacting residues are dedicated to the recognitio
SUBMITTER: Chen G
PROVIDER: S-EPMC12534559 | biostudies-literature | 2025 Oct
REPOSITORIES: biostudies-literature
ACCESS DATA