N-acetylneuraminate lyase
From Proteopedia
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| - | <StructureSection load='5zka' size='340' side='right' caption='N-acetylneuraminate lyase | + | <StructureSection load='5zka' size='340' side='right' caption='N-acetylneuraminate lyase dimer with modified Lys-pyruvate complex with ethylene glycol and triethylene glycol (PDB ID [[5zka]])' scene='91/919012/Cv/1'> |
== Function == | == 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<ref>PMID:6389524</ref>. | + | '''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<ref>PMID:6389524</ref>. |
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | NANL, an aldolase class I enzyme tetramer, is | + | 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 <scene name='91/919012/Cv/3'>Schiff base forms H-bond interactions with Ser, Thr, and conserved Tyr residue also via a water molecule</scene><ref>PMID:30387778</ref> (shown as red sphere). |
==3D structures of N-acetylneuraminate lyase== | ==3D structures of N-acetylneuraminate lyase== | ||
[[N-acetylneuraminate lyase 3D structures]] | [[N-acetylneuraminate lyase 3D structures]] | ||
Current revision
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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
