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Inhibition Of The Aminopeptidase From Aeromonas Proteolytica By L-Leucinephosphonic Acid. Spectroscopic And Crystallographic Characterization Of The Transition State Of Peptide Hydrolysis, Carin Stamper, Brian Bennett, Tanya Edwards, Richard C. Holz, Dagmar Ringe, Gregory A. Petsko
Inhibition Of The Aminopeptidase From Aeromonas Proteolytica By L-Leucinephosphonic Acid. Spectroscopic And Crystallographic Characterization Of The Transition State Of Peptide Hydrolysis, Carin Stamper, Brian Bennett, Tanya Edwards, Richard C. Holz, Dagmar Ringe, Gregory A. Petsko
Physics Faculty Research and Publications
The nature of the interaction of the transition-state analogue inhibitor l-leucinephosphonic acid (LPA) with the leucine aminopeptidase from Aeromonas proteolytica (AAP) was investigated. LPA was shown to be a competitive inhibitor at pH 8.0 with a Ki of 6.6 μM. Electronic absorption spectra, recorded at pH 7.5 of [CoCo(AAP)], [CoZn(AAP)], and [ZnCo(AAP)] upon addition of LPA suggest that LPA interacts with both metal ions in the dinuclear active site. EPR studies on the Co(II)-substituted forms of AAP revealed that the environments of the Co(II) ions in both [CoZn(AAP)] and [ZnCo(AAP)] become highly asymmetric and constrained upon the addition of …