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.

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

• 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.