Mechaism of Arthrobacter sialophilus neuraminidase: The binding of substrates and transition-state analogs |
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Authors: | Carl A Miller Philip Wang Michael Flashner |
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Institution: | Department of Chemistry, SUNY College of Environmental Science and Forestry, Syracuse, N.Y. 13210 USA |
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Abstract: | 2-Deoxy-2,3-dehydro-N-acetylneuraminic acid and its methyl ester are competitive inhibitors of Arthrobacter sialophilus neuraminidase with Ki = 1.4 × 10?6 and 4.8 × 10?5, respectively. The Km for the substrate, N-acetylneuraminlactose, is 1.0 × 10?3. These data, taken together with the conformation of these compounds, indicate that these compounds are transition-state analogs of the enzyme. These results also suggest that the substrate upon binding to neuraminidase is distorted to a conformation approaching that of a half-chair. |
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Keywords: | dehydro-NANA 2-deoxy-2 3-dehydro-N-acetylneuraminic acid dehydro-NANA methyl ester 2-deoxy-2 3-dehydro-N-acetylneuraminic acid methyl ester |
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