N-acetylneuraminate lyase

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Revision as of 14:04, 5 September 2022

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

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↑ 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

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 == 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<ref>PMID:30387778</ref>.
+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 <scene name='91/919012/Cv/2'>Lys side chain and pyruvate</scene>. The Schiff base forms H-bond interactions with Ser and Thr and also with conserved Tyr residue via a water molecule<ref>PMID:30387778</ref>.
 ==3D structures of N-acetylneuraminate lyase==
 [[N-acetylneuraminate lyase 3D structures]]