Shown below is a proposed mechanism for the cleavage of sialic acid by the viral enzyme neuraminidase.
Question:
Shown below is a proposed mechanism for the cleavage of sialic acid by the viral enzyme neuraminidase. The kcat for the wild-type enzyme at pH = 6.15, 37 °C is 26.8 s-1.
(a) Describe the roles of the following amino acids in the catalytic mechanism: Glu117, Tyr409, and Asp149. List all of the following that apply: general acid/base catalysis (GABC), covalent catalysis, electrostatic stabilization of transition state.
(b) Based on the information shown in the scheme, would you expect mutation of Glu 117 to Ala to have a greater effect on KM or kcat?
(c) For the R374N mutant at pH = 6.15, 37 °C, kcat is 0.020 s-1 , and KM is relatively unaffected. Based on this result, it seems that R374 is more critical for catalysis than for substrate binding. Explain how R374 stabilizes the reaction transition state more than the substrate (i.e., what feature of this reaction would explain tighter binding to the transition state vs. substrate?).
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a Glu117 General acidbase catalysis Glu117 is a general base catalyst that deprotonates the hydroxyl group on the sialic acid substratemaking it a bet...View the full answer
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