E-mail

E-mail a Wiley Online Library Link

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

Version of Record online: 27 FEB 2013 | DOI: 10.1111/febs.12158

Thumbnail image of graphical abstract

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.

Complete the form below and we will send an e-mail message containing a link to the selected article on your behalf

Required = Required Field

SEARCH