QM/MM modelling of ketosteroid isomerase reactivity indicates that active site closure is integral to catalysis
Version of Record online: 27 FEB 2013
© 2013 The Authors Journal compilation © 2013 FEBS
The FEBS Journal
Special Issue: Catalytic Mechanisms by Biological Systems
Volume 280, Issue 13, pages 3120–3131, July 2013
How to Cite
van der Kamp, M. W., Chaudret, R. and Mulholland, A. J. (2013), QM/MM modelling of ketosteroid isomerase reactivity indicates that active site closure is integral to catalysis. The FEBS Journal, 280: 3120–3131. doi: 10.1111/febs.12158
- Issue online: 18 JUN 2013
- Version of Record online: 27 FEB 2013
- Accepted manuscript online: 29 JAN 2013 04:18AM EST
- Manuscript Accepted: 25 JAN 2013
- Manuscript Revised: 18 JAN 2013
- Manuscript Received: 30 NOV 2012
- EPSRC. Grant Number: EP/G007705/1
Fig. S1. Stabilization along the reaction by the enzyme environment (MM region) .
Fig. S2. Free energy profiles (potentials of mean force) obtained from AM1/CHARMM27 umbrella-sampling MD simulations.
Fig. S3. Potential energy along RC1 of the QM region and the MM region only for seven AM1/CHARMM27 profiles.
Fig. S4. Structures from AM1/CHARMM27 profiles indicating the conformational changes that allow solvation of Asp38 Oδ1.
Table S1. Geometric measurements in key structures from the B3LYP/6-31+G(d)/CHARMM27 optimized potential energy profile.
Table S2. Geometric measurements from QM and QM/MM optimized conformations of methanol hydrogen bonded to O3 in the reactant, intermediate and product of the 5–androstene-3,17–dione to 4–androstene–3,17–dione reaction.
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