Function
Laminarase (LAM) or endo-1,3-beta-glucanase family GH16 or glycoside hydrolase family 16 degrades 1,3-beta glycosyl linkages of beta-glucan via the hydrolysis of glycosidic bonds[1].
Relevance
LAM cleaves laminarin which is an abundant polysaccharide found in alga which serves as carbon storage for nutrition of microbes. The depolymerization of laminarin initiates remineralization which is a key process in ocean biogeochemical cycles[2].
Structural highlights
The 3D structure of laminarase complexed with cellotriose shows the enzyme having a β-jellyroll fold typical to the GH16 family. The of the molecule with 2 Glu residues defined as the nucleophile and acid/base residues in the active site. The ligand is coordinated via H-bonds and CH-π interactions[3].
3D structures of laminarase
Laminarase 3D structures