N-acetylneuraminate synthase
N-acetylneuraminate synthase | |||||||||
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Identifiers | |||||||||
EC no. | 2.5.1.56 | ||||||||
CAS no. | 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 / QuickGO | ||||||||
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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
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1WVO.
References
[edit]- 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.