N-acetylneuraminate lyase
From Proteopedia
(Difference between revisions)
(New page: <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> == Function == '''N-acetylneuraminate lyase''' or '''N-acetylneuraminic acid aldoase...) |
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
== Function == | == Function == | ||
| - | '''N-acetylneuraminate lyase''' or '''N-acetylneuraminic acid | + | '''N-acetylneuraminate lyase''' or '''N-acetylneuraminic acid aldolase''' (NANL) is a class I aldolase which reversibly catalyses the cleavage of N-acetylneuraminic acid (salisilic acid) to N-acetylmannosamine and pyruvate<ref>PMID:6389524</ref>. |
== Disease == | == 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>. | ||
== Structural highlights == | == Structural highlights == | ||
Revision as of 07:21, 3 August 2022
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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
