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Substituent effects on the binding of phenols to the D38N mutant of 3-oxo-delta5-steroid isomerase. A probe for the nature of hydrogen bonding to the intermediate.

Biochemistry - 13 Jan 1998

Petrounia I P, Pollack R M

Abstract excerpt

The nature of hydrogen bonding to the intermediate of the reaction catalyzed by 3-oxo-Delta5-steroid isomerase (KSI) was investigated. Substituted phenols bind tightly to the active site of the D38N mutant of KSI, and are analogs of the intermediate dienol. These D38N-phenol complexes exhibit fluorescence, NMR, and UV spectral characteristics similar to D38N complexed with phenolic steroids. The binding of...

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PMID: 9425094
DOI: 10.1021/bi972262s

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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