N-acetylneuraminate synthase
| N-acetylneuraminate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 N-acetylneuraminic acid synthase dimer, Neisseria meningitidis | |||||||||
| Identifiers | |||||||||
| EC no. | 2.5.1.56 | ||||||||
| CAS no. | 37290-66-7 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
N-acetylneuraminate synthase (EC 2.5.1.56) 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.[1][2]
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.[3]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 1WVO.
References
- ↑ Blacklow RS, Warren L (1962). "Biosynthesis of sialic acids by Neisseria meningitidis". J. Biol. Chem. 237 (11): 3520–6. doi:10.1016/S0021-9258(19)70850-3. 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.
- ↑ Enzyme 2.5.1.56 at KEGG Pathway Database.