4 ms·
Enzymes aren't stable and static -- usually in their active site they have significant conformational changes that enable catalysis of the relevant chemical rea
by throwawaybio3 5y ago
Enzymes aren't stable and static -- usually in their active site they have significant conformational changes that enable catalysis of the relevant chemical reaction. It's quite a problem that we don't have general robust ways of directly elucidating those transient structures, a lot of our understanding of catalysis is still held back or slow-evolving because we can only use indirect and cumbersome methods (like isotopic mutation + laser IR)
I would consider most enzymes to be intrinsically disordered at their active sites.
- dekhn 5y agoNo enzymes are not intrinsically disordered at their active sites. They are highly ordered. Most enzymes don't undergo large changes- they accept a molecule, do their business, and release it. You're thinking of other proteins like motor proteins which under go large, controlled conformational changes. The active site is structured to stabilize the transition state of the affected molecule and move it from one state to the next in the chemical reaction. That requires very specific shapes and correlated changes. But of course, this being biology, you can remove all 3 active site residues in a serine protease catalytic triad, and still see proteolysis because the protein, when it binds the substrate, forces the subtrate into its transition pathway. People have been working on these things for quite some time- I saw talks about time-resolved crystallography of active sites, and while they say "significant structure changes", they really only mean localized breathing-like motions, not massive rotations of entire domains.