The 2011 annual meeting theme "Structure, Mechanism and Regulation in Enzyme Catalysis" will look at metals and redox chemistry, sulfur chemistry and biological redox, processive enzymes and kinases, phosphatases, and phosphorus in biological reactions. The meeting will be held April 9-13, 2011, in Washington, D.C. (Titled "Structural and Mechanistic Enzymology" in print version.)
|L. Mario Amzel
||Squire J. Booker
The study of enzymes and the reactions that they catalyze is as vibrant today as it was forty years ago. Novel cofactors still are being discovered, and new paradigms still are emerging, as we delve even deeper into enzymatic reactions at the detailed molecular level using a variety of physical and structural methods in concert with computational methods. Moreover, enzymatic substrates are becoming more complex as the field moves from small molecules to reactions in which enzymes construct or modify macromolecules like other proteins, DNA, RNA, carbohydrates and fatty acids. At the 2011 American Society for Biochemistry and Molecular Biology annual meeting, four sessions in the “Structure, Mechanisms and Regulation in Enzyme Catalysis” theme will bring together various aspects of current work on structural and mechanistic enzymology. Given the diversity of the field, subjects were chosen to cover as many areas as possible while minimizing the overlap with those covered in other symposia.
The session on “Metals and Redox Chemistry,” chaired by Squire J. Booker, is expected to offer rich new insight into the remarkable abilities of metalloenzymes to catalyze complex and energy-demanding reactions. The theme of the session will highlight new mechanisms in which the combination of molecular oxygen and a metal cofactor is employed to create oxidants suitably potent to cleave unactivated C–H bonds.
Historically, the study of iron-dependent enzymes has predominated; however, exciting new findings are providing evidence for the use of copper in these transformations. The lecture by Carsten Krebs (The Pennsylvania State University), titled “Characterization of Two Reaction Intermediates in the Nonheme-Fe(II)-dependent Enzyme Isopenicillin N-synthase,” will show how the use of rapid-kinetics methods combined with various spectroscopic techniques can unveil key intermediates in these reactions and allow for their structural characterization.
Amy C. Rosenzweig (Northwestern University) will give a lecture titled “Methane Oxidation by an Integral Membrane Metalloenzyme.” This enzyme, featured in a recent Nature publication from Rosenzweig’s lab (1), uses a dicopper center to hydroxylate the most inert carbon substrate, methane, which exhibits a homolytic bond-dissociation energy of approximately 104 kcal mol–1!
L. Mario Amzel (Johns Hopkins University School of Medicine) will continue with the copper theme, delivering a lecture detailing structural, mechanistic and computational characterization of peptidylglycine α-amidating enzyme. This protein is responsible for the maturation of a number of peptide hormones and neuropeptides and catalyzes two distinct reactions on separate domains: the copper-dependent hydroxylation of the peptide substrate and subsequent zinc-dependent fragmentation of the peptide to afford an amidate.