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N-acetylneuraminate synthase
N-acetylneuraminic acid synthase dimer, Neisseria meningitidis
Identifiers
EC no.	2.5.1.56
CAS no.	37290-66-7
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, a N-acetylneuraminate synthase (EC 2.5.1.56) is an enzyme that catalyzes the chemical reaction

phosphoenolpyruvate + N-acetyl-D-mannosamine + H₂O ${\displaystyle \rightleftharpoons }$ phosphate + N-acetylneuraminate

The 3 substrates of this enzyme are phosphoenolpyruvate, N-acetyl-D-mannosamine, and H₂O, whereas its two products are phosphate and N-acetylneuraminate.

This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is phosphoenolpyruvate:N-acetyl-D-mannosamine C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming). Other names in common use include (NANA)condensing enzyme, N-acetylneuraminate pyruvate-lyase (pyruvate-phosphorylating), and NeuAc synthase. This enzyme participates in aminosugars metabolism.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1WVO.

References

• BLACKLOW RS, WARREN L (1962). "Biosynthesis of sialic acids by Neisseria meningitidis". J. Biol. Chem. 237 (11): 3520–6. doi:10.1016/S0021-9258(19)70850-3. PMID 13971393.
• Komaki E, Ohta Y, Tsukada Y (1997). "Purification and characterization of N-acetylneuraminate synthase from Escherichia coli K1-M12". Biosci. Biotechnol. Biochem. 61 (12): 2046–50. doi:10.1271/bbb.61.2046. PMID 9438985.

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