N-acetylneuraminate synthase

From Wikipedia, the free encyclopedia

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 $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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

[edit] References

IUBMB entry for 2.5.1.56
BRENDA references for 2.5.1.56 (Recommended.)
PubMed references for 2.5.1.56
PubMed Central references for 2.5.1.56
Google Scholar references for 2.5.1.56
BLACKLOW RS, WARREN L (1962). "Biosynthesis of sialic acids by Neisseria meningitidis". J. Biol. Chem. 237: 3520–6. 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: 2046–50. PMID 9438985.