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. 1992 Mar 1;282(Pt 2):511–516. doi: 10.1042/bj2820511

Elucidation of the topological parameters of N-acetylneuraminic acid and some analogues involved in their interaction with the N-acetylneuraminate lyase from Clostridium perfringens.

E Zbiral 1, R G Kleineidam 1, E Schreiner 1, M Hartmann 1, R Christian 1, R Schauer 1
PMCID: PMC1130810  PMID: 1546967

Abstract

A series of neuraminic acid derivatives modified in the side chain or at C-3, C-4 or C-5 were tested as substrates of inhibitors of N-acetylneuraminate lyase (EC 4.1.3.3) from Clostridium perfringens. The results, together with Km and Ki values reported previously, indicate that the region most important for the binding of sialic acids is an equatorial zone reaching from C-8 via the ring oxygen atom to C-4 of the sugar molecule, whereas the substituents at C-9 and C-5 may be varied to a higher extent without significantly disturbing enzyme action. It is shown that stereo-electronic factors are responsible for the immediate heterolytic fragmentation of the cyclic sialic acid into pyruvic acid and 2-acetamidomannose or a related C-6 sugar.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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