N-acylneuraminate-9-phosphate synthase

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In enzymology, a N-acylneuraminate-9-phosphate synthase (EC 2.5.1.57) is an enzyme that catalyzes the chemical reaction

phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H₂O $\rightleftharpoons$ N-acylneuraminate 9-phosphate + phosphate

The 3 substrates of this enzyme are phosphoenolpyruvate, N-acyl-D-mannosamine 6-phosphate, and H₂O, whereas its two products are N-acylneuraminate 9-phosphate and phosphate.

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-acyl-D-mannosamine-6-phosphate 1-(2-carboxy-2-oxoethyl)transferase. Other names in common use include N-acetylneuraminate 9-phosphate lyase, N-acetylneuraminate 9-phosphate sialic acid 9-phosphate synthase, N-acetylneuraminate 9-phosphate synthetase, N-acylneuraminate-9-phosphate pyruvate-lyase, (pyruvate-phosphorylating), and sialic acid 9-phosphate synthetase. 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 2.5.1.57
BRENDA references for 2.5.1.57 (Recommended.)
PubMed references for 2.5.1.57
PubMed Central references for 2.5.1.57
Google Scholar references for 2.5.1.57
Roseman S, Jourdian GW, Watson D and Rood R (1961). "Enzymatic synthesis of sialic acid 9-phosphates". Proc. Natl. Acad. Sci. USA 47: 958–961. doi:10.1073/pnas.47.7.958.
Watson DR, Jourdian GW, Roseman S (1966). "The sialic acids. 8. Sialic acid 9-phosphate synthetase". J. Biol. Chem. 241: 5627–36. PMID 5928202.
Nakata D, Close BE, Colley KJ, Matsuda T, Kitajima K (2000). "Molecular cloning and expression of the mouse N-acetylneuraminic acid 9-phosphate synthase which does not have deaminoneuraminic acid (KDN) 9-phosphate synthase activity". Biochem. Biophys. Res. Commun. 273: 642–8. doi:10.1006/bbrc.2000.2983. PMID 10873658.