N-acetylneuraminate synthase () is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are phosphoenolpyruvic acid, N-acetyl-D-mannosamine, and water. Its products are the sialic acid, N-Acetylneuraminic acid and orthophosphate (Pi). The enzyme has been characterised from Neisseria meningitidis and Escherichia coli.
This enzyme is a transferase, 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.
Structural studies As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
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