Article
Ultraviolet resonance Raman spectroscopy of delta 5-3-ketosteroid isomerase revisited: substrate polarization by active-site residues.
Biochemistry - 4 Apr 1995
Austin J C, Zhao Q, Jordan T, Talalay P, Mildvan A S, Spiro T G
Abstract excerpt
The delta 5-3-ketosteroid isomerase (EC 5.3.3.1) of Pseudomonas testosteroni promotes extremely rapid conversion of delta 5- to delta 4-3-ketosteroids by a conservative intramolecular proton transfer via an enolic intermediate. The competitive inhibitor 19-nortestosterone displays marked spectroscopic changes upon binding to the enzyme, but the mechanisms responsible for these changes have not been unequivocally...
Topics
- Binding Sites
- Hydrogen Bonding
- Hydrogen-Ion Concentration
- Mutation
- Nandrolone
- Protein Conformation
- Protons
- Pseudomonas
- Recombinant Proteins
- Spectroscopy, Fourier Transform Infrared
- Spectrum Analysis, Raman