N-acetylneuraminate lyase

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N-acetylneuraminate lyase
N-acetylneuramininate lyase tetramer, Aliivibrio salmonicida
EC no.
CAS no.9027-60-5
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a N-acetylneuraminate lyase (EC is an enzyme that catalyzes the chemical reaction

N-acetylneuraminate N-acetyl-D-mannosamine + pyruvate

Hence, this enzyme has one substrate, N-acetylneuraminate, and two products, N-acetyl-D-mannosamine and pyruvate.

This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is N-acetylneuraminate pyruvate-lyase (N-acetyl-D-mannosamine-forming). Other names in common use include N-acetylneuraminic acid aldolase, acetylneuraminate lyase, sialic aldolase, sialic acid aldolase, sialate lyase, N-acetylneuraminic aldolase, neuraminic aldolase, N-acetylneuraminate aldolase, neuraminic acid aldolase, N-acetylneuraminic acid aldolase, neuraminate aldolase, N-acetylneuraminic lyase, N-acetylneuraminic acid lyase, NPL, NALase, NANA lyase, acetylneuraminate pyruvate-lyase, and N-acetylneuraminate pyruvate-lyase. This enzyme participates in aminosugars metabolism.

Structural studies[edit]

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1F5Z, 1F6K, 1F6P, 1F73, 1F74, 1F7B, 1FDY, 1FDZ, 1HL2, and 1NAL.


  • COMB DG, ROSEMAN S (1960). "The sialic acids. I. The structure and enzymatic synthesis of N-acetylneuraminic acid". J. Biol. Chem. 235: 2529–37. PMID 13811398.
  • Schauer R (1982). "Advances in Carbohydrate Chemistry and Biochemistry Volume 40; Chapter = Chemistry, Metabolism, and Biological Functions of Sialic Acids". Adv. Carbohydr. Chem. Biochem. Advances in Carbohydrate Chemistry and Biochemistry. 40: 131–234. doi:10.1016/S0065-2318(08)60109-2. ISBN 978-0-12-007240-8. PMID 6762816.