N-acetylneuraminate lyase
From Proteopedia
Jump to navigationJump to search
| ||||||||||||
ContentsFunctionN-acetylneuraminate lyase or N-acetylneuraminic acid aldolase or D-sialic 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]. RelevanceNANL catalyses the rate-limiting step of two biocatalytic reactions producing sialic acid in industry[2]. Structural highlightsNANL, an aldolase class I enzyme tetramer, is characterized 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, Thr, and conserved Tyr residue also via a water molecule[3] (shown as red sphere). 3D structures of N-acetylneuraminate lyaseN-acetylneuraminate lyase 3D structures
| ||||||||||||
This page was last modified 10:06, 10 July 2023.