New directions in enzymology

Mechanistic enzymology and protein-structure function

It’s been almost 90 years since the isolation of urease, yet a vigorous debate continues about how enzymes impart such large rate enhancements to slow reactions. This ASBMB annual meeting symposium will examine modern issues in mechanistic enzymology and protein-structure function.

Co-opting cofactors

Recent investigations have revealed that even a well-studied cofactor such as NAD has some unexpected tricks up its sleeve. This session will discuss new developments in cofactor biosynthesis, chemistry and dynamics.

Function detectives

In any newly sequenced genome, as many as 70 percent of the genes do not have assigned functions. It is clear, then, that a substantial fraction of biochemical space still remains to be mapped. This session will spotlight recent successes in assigning functions to orphan enzymes, the discovery of new activities and metabolites.

Collective power

Enzymes operate in a crowded milieu that fosters macromolecular complex formation and complicated quaternary behavior. This session will examine new tools for characterizing enzyme complexes and highlight examples of protein oligomerization as a regulatory strategy.

My one and only

Of course, rate acceleration is only part of what is amazing about enzyme catalysis. How enzymes discriminate between substrates is far more complex than the simple lock-and-key model. This session will discuss strategies for substrate recognition and reaction specificity.
Kate Carroll
Liz Hedstrom
Organizers: Kate Carroll, The Scripps Research Institute, and Liz Hedstrom, Brandeis University