Transaminases are industrially useful enzymes that can be used to make chiral amines (building blocks for many pharmaceuticals) as well as monomers for polyamines (i.e., diamines and w-amino alkanoates). Last year we published our work on ancestral reconstruction in a family of transaminases - the ancestral enymes had dramatically altered substrate preferences and rates, but the part of the enzyme typically associated with specificity (the active site) was identical in all of the enzymes (ancestors and modern day). We were unable to understand the mechanistic basis of the biochemical differences.
In our most recent paper, Matt Wilding and Andrew Wardern developed a novel molecular dynamics based approach and unique analysis method that let us track substrate:enzyme interactions over time. We found that the enzyme surface played a role in channeling specific compounds (i.e, the good substrates) to the active site, and so influenced the enzymes specificity and catalytic properties. Hopefully, this will help provide a new approach to enzyme engineering in future.