N-acetylneuraminate lyase

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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load='5zka' size='340' side='right' caption='Caption for this structure' scene=''>
== 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''' (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>.
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== Disease ==
 
== Relevance ==
== Relevance ==
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NANL catalyses the rate-limiting step of two biocatalytic reactions producing salicylic acid in industry<ref>PMID:25799411</ref>.
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NANL catalyses the rate-limiting step of two biocatalytic reactions producing sialic acid in industry<ref>PMID:25799411</ref>.
== Structural highlights ==
== Structural highlights ==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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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>.
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==3D structures of N-acetylneuraminate lyase==
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[[N-acetylneuraminate lyase 3D structures]]
</StructureSection>
</StructureSection>
== References ==
== References ==
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<references/>
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[[Category:Topic Page]]

Revision as of 07:16, 4 August 2022

Caption for this structure

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References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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