Carl A. Miller, Philip Wang, Michael Flashner
Aug 29, 1978
Citations
0
Influential Citations
60
Citations
Journal
Biochemical and biophysical research communications
Abstract
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 M and 4.8 × 10−5 M , respectively. The Km for the substrate, N-acetylneuraminlactose, is 1.0 × 10−3 M . 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.