N-acylneuraminate-9-phosphate synthase

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N-acylneuraminate-9-phosphate synthase
Identifiers
EC number 2.5.1.57
CAS number 9031-58-7
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

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 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.

Structural studies[edit]

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

References[edit]

  • Roseman S, Jourdian GW, Watson D, Rood R (1961). "Enzymatic synthesis of sialic acid 9-phosphates". Proc. Natl. Acad. Sci. USA. 47 (7): 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 (23): 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 (2): 642–8. PMID 10873658. doi:10.1006/bbrc.2000.2983.