Abstract | BACKGROUND: RESULTS: CONCLUSIONS: The mechanism of neuraminidase action is distinct from that of other known glycosyl hydrolases. Substrate distortion appears to be the driving force in glycosyl bond hydrolysis and the proton required for catalysis can probably be donated by water, rather than by residues in the active site, thus allowing the enzyme to operate at high pH. The side reaction converting sialic acid to DANA appears reasonably favourable, and it is unclear how this is minimized by the enzyme.
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Authors | W P Burmeister, B Henrissat, C Bosso, S Cusack, R W Ruigrok |
Journal | Structure (London, England : 1993)
(Structure)
Vol. 1
Issue 1
Pg. 19-26
(Sep 15 1993)
ISSN: 0969-2126 [Print] United States |
PMID | 8069621
(Publication Type: Journal Article)
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Chemical References |
- Sialic Acids
- 2-deoxy-2,3-dehydro-N-acetylneuraminic acid
- Neuraminidase
- N-Acetylneuraminic Acid
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Topics |
- Crystallography, X-Ray
(methods)
- Gas Chromatography-Mass Spectrometry
- Influenza B virus
(enzymology)
- Models, Molecular
- Molecular Conformation
- N-Acetylneuraminic Acid
- Neuraminidase
(antagonists & inhibitors, chemistry, metabolism)
- Protein Structure, Secondary
- Sialic Acids
(chemistry, metabolism)
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