Marc W. van der Kamp, Robin Chaudret and Adrian J. Mulholland QM/MM modelling of ketosteroid isomerase reactivity indicates that active site closure is integral to catalysis The FEBS Journal 280
Ketosteroid isomerase is a highly efficient enzyme involved in the formation of hormones such as testosterone. We show, using high-level QM/MM potential energy profiles and semi-empirical QM/MM dynamics simulations, that the catalytic cycle involves active site closure, desolvation of the catalytic base, isomerization and reopening of the active site. Closure of the active site is essential for efficient catalysis.
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