Structural insight into the catalytic mechanism of the bifunctional enzyme l-fucokinase/GDP-fucose pyrophosphorylase.

ABSTRACT: The bifunctional l-fucokinase/GDP-β-l-fucose pyrophosphorylase (FKP) from Bacteroides fragilis catalyzes the conversion from l-fucose to GDP-β-l-fucose. The reaction product, representing the activated form of l-fucose, is used by all l-fucosyltransferases to incorporate l-fucose. Herein, we report the first X-ray crystal structures of FKP in complex with substrate-product, leading to the dissection of both activity domains and corresponding catalytic mechanisms. The full-length FKP (FKP-FL, 949 amino acids) exists as a tetramer in solution, but the individually prepared N-terminal domain (FKP-NTD corresponding to the sequence 1-496, also containing a SUMO tag) and C-terminal domain (FKP-CTD, the sequence 519-949) form a monomer and a dimer, respectively. FKP-NTD has a single α/β domain an

SUBMITTER: Lin SW 

PROVIDER: S-EPMC11982464 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature