N-acetylneuraminate lyase


N-acetylneuraminate lyase
N-acetylneuraminate lyase
Identifiers
EC number 4.1.3.3
CAS number 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 / EGO

In enzymology, a N-acetylneuraminate lyase (EC 4.1.3.3) is an enzyme that catalyzes the chemical reaction

N-acetylneuraminate \rightleftharpoons N-acetyl-D-mannosamine + pyruvate

Hence, this enzyme has one substrate, N-acetylneuraminate, and two products, N-acetyl-D-mannosamine and 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). Chemistry, Metabolism, and Biological Functions of Sialic Acids. "Advances in Carbohydrate Chemistry and Biochemistry Volume 40". Adv. Carbohydr. Chem. Biochem.. Advances in Carbohydrate Chemistry and Biochemistry 40: 131–234. doi:10.1016/S0065-2318(08)60109-2. ISBN 9780120072408. PMID 6762816.