Structural and functional characterization of chitinase from carnivorous plant Drosera adelae.

ABSTRACT: A class I chitinase from the carnivorous sundew plant Drosera adelae was successfully expressed in the methylotrophic yeast Pichia pastoris and efficiently purified using a chitin affinity column. Enzymatic activity assays revealed that the enzyme showed a specific activity of 235.3 ± 10.2 U·mg^-1. Crystallization of wild-type and E167Q catalytic mutant chitinases yielded needle-like microcrystals. X-ray diffraction experiments were performed, and high-resolution datasets were obtained at 1.73 Å and 1.57 Å, respectively. Structural analysis of diffraction data revealed that only the catalytic domain could be resolved in both crystal forms. Using AutoDock Vina, we performed docking simulations of two (GlcNAc)₄ molecules at eight subsites (+4 to -4) of the catalytic doma

SUBMITTER: Yoneda K 

PROVIDER: S-EPMC12667207 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature