title: Is a proton relay involved in the mechanism of 3-oxo-delta 5-steroid isomerase?
abstract: Previous reports of a UV spectral shift upon binding of the competitive inhibitor 19-nortestosterone (1) to 3-oxo-delta 5-steroid isomerase (KSI), coupled with UV resonance Raman results, have led to the conclusion that the enone moiety is polarized to a degree similar to that produced by complete protonation and that a proton relay may be involved in the enzymatic mechanism (Austin et al., 1992). These conclusions were partly based upon interpretations of the corresponding UV spectra of 1 in aqueous acid solutions. These interpretations are shown to be inconsistent with results of deuterium exchange studies and with spectra of model systems. Consequently, there is no evidence either for an extraordinary polarization of 1 produced by binding to the active site of KSI or for a proton relay mechanism.
authors.affiliation: Department of Chemistry and Biochemistry, University of Maryland Baltimore County 21228-5398.
authors.forename: D C
authors.initials: DC
authors.lastname: Hawkinson
authors.forename: R M
authors.initials: RM
authors.lastname: Pollack
mesh_terms: D002384:Catalysis; D011522:Protons; D013056:Spectrophotometry, Ultraviolet; D013059:Spectrum Analysis, Raman; D013251:Steroid Isomerases / Q000737:chemistry / Q000378:metabolism*; D005723:gamma-Glutamyltransferase / Q000037:antagonists & inhibitors
chemical_list: D011522:Protons; D005723:gamma-Glutamyltransferase; D013251:Steroid Isomerases; C022660:steroid delta-isomerase