Crystal structures and kinetics of N-acetylneuraminate lyase from Fusobacterium nucleatum

In this study, atomic resolution structures of NanA from Fusobacterium nucleatum (FnNanA) in ligand-free and ligand-bound forms are reported at 2.32 and 1.76   Å resolution, respectively. F. nucleatum is a Gram-negative pathogen that causes gingival and periodontal diseases in human hosts. Like other bacterial N-acetylneuraminate lyases, FnNanA also shares the triosephosphate isomerase (TIM)-barrel fold. As observed in other homologous enzymes, FnNanA forms a tetramer. In order to characterize the structure – function relationship, the steady-state kinetic parameters of the enzyme are also reported.

Source: Acta Crystallographica Section F - October 17, 2018 Category: Biochemistry Authors: Kumar, J.P. Rao, H. Nayak, V. Ramaswamy, S. Tags: N-acetylneuraminate lyase sialic acid catabolism enzyme kinetics Fusobacterium nucleatum research communications Source Type: research