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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, 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]

[EC 4.1.3.3 created 1961, modified 2021]

5.1.3.24

Accepted name:

N-acetylneuraminate epimerase

Reaction:

N-acetyl-α-neuraminate = N-acetyl-β-neuraminate (oveall reaction)
(1a) N-acetyl-α-neuraminate = aceneuramate
(1b) aceneuramate = N-acetyl-β-neuraminate

Glossary:

aceneuramate = (4S,5R,6R,7S,8R)-5-acetamido-4,6,7,8,9-pentahydroxy-2-oxononanoate

Other name(s):

sialic acid epimerase; N-acetylneuraminate mutarotase; NanM; NanQ

Systematic name:

N-acetyl-α-neuraminate 2-epimerase

Comments:

Sialoglycoconjugates present in vertebrates are linked exclusively by α-linkages and are released in α form during degradation. This enzyme accelerates maturotation to the β form via the open form (which also occurs as a slow spontaneous reaction). The open form is necessary for further metabolism by the bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Severi, E., Müller, A., Potts, J.R., Leech, A., Williamson, D., Wilson, K.S. and Thomas, G.H. Sialic acid mutarotation is catalyzed by the Escherichia coli β-propeller protein YjhT. J. Biol. Chem. 283 (2008) 4841–4849. [DOI] [PMID: 18063573]
2.	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]

[EC 5.1.3.24 created 2011, modified 2021]