Function
N-acetylneuraminate lyase or N-acetylneuraminic acid aldolase (NANL) is a class I aldolase which reversibly catalyses the cleavage of N-acetylneuraminic acid (sialic acid) to N-acetylmannosamine and pyruvate[1].
Relevance
NANL catalyses the rate-limiting step of two biocatalytic reactions producing sialic acid in industry[2].
Structural highlights
NANL, an aldolase class I enzyme tetramer, is characterised by TIM-barrel fold and reaction mechanism which involves A Schiff base intermediate formed by covalently bond between a conserved Lys side chain and pyruvate. The Schiff base forms H-bond interactions with Ser and Thr and also with conserved Tyr residue via a water molecule[3].
3D structures of N-acetylneuraminate lyase
N-acetylneuraminate lyase 3D structures
