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Crystal structures and kinetics of N ‐acetylneuraminate lyase from Fusobacterium nucleatum
Author(s) -
Kumar Jay Prakash,
Rao Harshvardhan,
Nayak Vinod,
Ramaswamy S.
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18012992
Subject(s) - fusobacterium nucleatum , sialic acid , lyase , neuraminic acid , n acetylneuraminic acid , ligand (biochemistry) , biochemistry , catabolism , biology , chemistry , microbiology and biotechnology , triosephosphate isomerase , enzyme , bacteria , porphyromonas gingivalis , genetics , receptor
N ‐Acetyl‐ d ‐neuraminic acid lyase (NanA) catalyzes the breakdown of sialic acid (Neu5Ac) to N ‐acetyl‐ d ‐mannosamine (ManNAc) and pyruvate. NanA plays a key role in Neu5Ac catabolism in many pathogenic and bacterial commensals where sialic acid is available as a carbon and nitrogen source. Several pathogens or commensals decorate their surfaces with sialic acids as a strategy to escape host innate immunity. Catabolism of sialic acid is key to a range of host–pathogen interactions. 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.