Ground state destabilization from a positioned general base in the ketosteroidisomerase active site

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From: Biochemistry(Vol. 52, Issue 6)
Publisher: American Chemical Society
Document Type: Report
Length: 86 words

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Abstract :

The comparison of binding affinities of ground state analogues for bacterial ketosteroidisomerase (KSI) with a wild-type anionic Asp general base and with uncharged Asn and Ala in the general base position is described in this article. The results, supported by additional structural observations, suggest that ground state destabilization from the negatively charged Asp38 general base provide a modest contribution to KSI catalysis. Furthermore, they also provide a clear illustration of the well-recognized concept that enzymes evolve for catalytic function and not to maximize ground state binding.

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Gale Document Number: GALE|A332263028