| EC |
4.1.3.3 |
| Accepted name: |
N-acetylneuraminate lyase |
| Reaction: |
aceneuramate = N-acetyl-D-mannosamine + pyruvate |
| Glossary: |
aceneuramate = (4S,5R,6R,7S,8R)-5-acetamido-4,6,7,8,9-pentahydroxy-2-oxononanoate |
| Other name(s): |
N-acetylneuraminic acid aldolase; acetylneuraminate lyase; sialic aldolase; sialic acid aldolase; sialate lyase; N-acetylneuraminic aldolase; neuraminic aldolase; N-acetylneuraminate aldolase; neuraminic acid aldolase; neuraminate aldolase; N-acetylneuraminic lyase; N-acetylneuraminic acid lyase; NPL; NALase; NANA lyase; acetylneuraminate pyruvate-lyase; N-acetylneuraminate pyruvate-lyase; NanA; N-acetylneuraminate pyruvate-lyase (N-acetyl-D-mannosamine-forming) |
| Systematic name: |
aceneuramate pyruvate-lyase (N-acetyl-D-mannosamine-forming) |
| Comments: |
This enzyme is involved in the degradation of N-acetylneuraminate. It is specific for the open form of the sugar. It also acts on N-glycoloylneuraminate and on O-acetylated sialic acids, other than 4-O-acetylated derivatives. |
| Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-60-5 |
| References: |
| 1. |
Comb, D.G. and Roseman, S. The sialic acids. I. The structure and enzymatic synthesis of N-acetylneuraminic acid. J. Biol. Chem. 235 (1960) 2529–2537. [PMID: 13811398] |
| 2. |
Schauer, R. Sialic acids. Adv. Carbohydr. Chem. Biochem. 40 (1982) 131–234. [DOI] [PMID: 6762816] |
| 3. |
Kentache, T., Thabault, L., Deumer, G., Haufroid, V., Frederick, R., Linster, C.L., Peracchi, A., Veiga-da-Cunha, M., Bommer, G.T. and Van Schaftingen, E. The metalloprotein YhcH is an anomerase providing N-acetylneuraminate aldolase with the open form of its substrate. J. Biol. Chem. :100699 (2021). [DOI] [PMID: 33895133] |
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| [EC 4.1.3.3 created 1961, modified 2021] |
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