| N-acetylneuraminate lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 N-acetylneuramininate lyase tetramer, Aliivibrio salmonicida | |||||||||
| Identifiers | |||||||||
| EC no. | 4.1.3.3 | ||||||||
| CAS no. | 9027-60-5 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme N-acetylneuraminate lyase (EC 4.1.3.3) catalyzes the chemical reaction
- N-acetylneuraminate N-acetyl-D-mannosamine + pyruvate
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is N-acetylneuraminate pyruvate-lyase (N-acetyl-D-mannosamine-forming). Other names in common use include N-acetylneuraminic acid aldolase, acetylneuraminate lyase, sialic aldolase, sialic acid aldolase, sialate lyase, N-acetylneuraminic aldolase, neuraminic aldolase, N-acetylneuraminate aldolase, neuraminic acid aldolase, N-acetylneuraminic acid aldolase, neuraminate aldolase, N-acetylneuraminic lyase, N-acetylneuraminic acid lyase, NPL, NALase, NANA lyase, acetylneuraminate pyruvate-lyase, and N-acetylneuraminate pyruvate-lyase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1F5Z, 1F6K, 1F6P, 1F73, 1F74, 1F7B, 1FDY, 1FDZ, 1HL2, and 1NAL.
References
- COMB DG, ROSEMAN S (1960). "The sialic acids. I. The structure and enzymatic synthesis of N-acetylneuraminic acid". J. Biol. Chem. 235: 2529–37. PMID 13811398.
- Schauer R (1982). "Advances in Carbohydrate Chemistry and Biochemistry Volume 40; Chapter = Chemistry, Metabolism, and Biological Functions of Sialic Acids". Adv. Carbohydr. Chem. Biochem. Advances in Carbohydrate Chemistry and Biochemistry. 40: 131–234. doi:10.1016/S0065-2318(08)60109-2. ISBN 978-0-12-007240-8. PMID 6762816.