Article
Ground state destabilization from a positioned general base in the ketosteroid isomerase active site.
Biochemistry - 12 Feb 2013
Ruben Eliza A, Schwans Jason P, Sonnett Matthew, Natarajan Aditya, Gonzalez Ana, Tsai Yingssu, Herschlag Daniel
Abstract excerpt
We compared the binding affinities of ground state analogues for bacterial ketosteroid isomerase (KSI) with a wild-type anionic Asp general base and with uncharged Asn and Ala in the general base position to provide a measure of potential ground state destabilization that could arise from the close juxtaposition of the anionic Asp and hydrophobic steroid in the reaction's Michaelis complex. The analogue binding...
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