N-acetylneuraminate lyase

From Proteopedia

1 Function
2 Relevance
3 Structural highlights
4 3D structures of N-acetylneuraminate lyase

Function

N-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].

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 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 lyase

N-acetylneuraminate lyase 3D structures

N-acetylneuraminate lyase dimer with modified Lys-pyruvate complex with ethylene glycol and triethylene glycol (PDB ID 5zka)

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References

↑ Uchida Y, Tsukada Y, Sugimori T. Purification and properties of N-acetylneuraminate lyase from Escherichia coli. J Biochem. 1984 Aug;96(2):507-22. doi: 10.1093/oxfordjournals.jbchem.a134863. PMID:6389524 doi:http://dx.doi.org/10.1093/oxfordjournals.jbchem.a134863
↑ Ji W, Sun W, Feng J, Song T, Zhang D, Ouyang P, Gu Z, Xie J. Characterization of a novel N-acetylneuraminic acid lyase favoring industrial N-acetylneuraminic acid synthesis. Sci Rep. 2015 Mar 23;5:9341. doi: 10.1038/srep09341. PMID:25799411 doi:http://dx.doi.org/10.1038/srep09341
↑ Kumar JP, Rao H, Nayak V, Ramaswamy S. Crystal structures and kinetics of N-acetylneuraminate lyase from Fusobacterium nucleatum. Acta Crystallogr F Struct Biol Commun. 2018 Nov 1;74(Pt 11):725-732. doi:, 10.1107/S2053230X18012992. Epub 2018 Oct 17. PMID:30387778 doi:http://dx.doi.org/10.1107/S2053230X18012992