Science, discussed.

QM/MM analysis shows correlation between promiscuity and flexibility

To kick off my 2015 resolution, here’s a paper that uses molecular modelling to correlate the observed promiscuity profile of o-Succinylbenzoate Synthase with the involvement of alternative amino acids within the same active site.

Enzyme Promiscuity in Enolase Superfamily. A Theoretical Study 
of o-Succinylbenzoate Synthase Using QM/MM Methods
M. Sánchez-Tarín, K. Świderek, M. Roca, and I. Tuñón
The Journal of Physical Chemistry B Just Accepted Manuscript


The authors find correlation between their findings (energy profiles of the two reactions) and experimental values and map the stabilising/destabilising effects of residues in the enzyme active site/binding pocket. Rearrangements in an active site conformation have been shown already to be favourable for promiscuity, and the current report suggest a similar scenario.
That enzyme and binding promiscuity enhances/allows the evolution of new functions is now an established concept, but the understanding of the molecular and structural features that can bring it about is still largely under-reported. Experimental and computational (as this one) analysis are thus very welcome.

About Pietro Gatti

Interested in discussing (good) Science Lover of coffee & good films. Ideas all & only my own.

Leave a Reply

Fill in your details below or click an icon to log in: Logo

You are commenting using your account. Log Out / Change )

Twitter picture

You are commenting using your Twitter account. Log Out / Change )

Facebook photo

You are commenting using your Facebook account. Log Out / Change )

Google+ photo

You are commenting using your Google+ account. Log Out / Change )

Connecting to %s


Creative Commons License
This blog is licensed under a Creative Commons Attribution 3.0 License.


Enter your email address to follow this blog and receive notifications of new posts by email.

Join 1,560 other followers

All Categories

%d bloggers like this: