N-acetylneuraminate synthase
| N-acetylneuraminate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.5.1.56 | ||||||||
| CAS number | 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 / EGO | ||||||||
| |||||||||
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 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.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1WVO.
References
- 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 (12): 2046–50. doi:10.1271/bbb.61.2046. PMID 9438985.