July 2010

Meeting Theme: Structure, Mechanism and Regulation in Enzyme Catalysis

 

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.)

 

Meetings---Amzel Meetings---Booker
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.

Metalloenzymes

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.

Structure, Mechanism and Regulation in Enzyme Catalysis

Session: Metals and Redox Chemistry
 Characterization of Two Reaction Intermediates in the Nonheme-Fe(II)-dependent Enzyme Isopenicillin N-Synthase, Carsten Krebs, The Pennsylvania State University

Methane Oxidation by an Integral Membrane Metalloenzyme, Amy C. Rosenzweig, Northwestern University

Structural and Mechanistic Studies on Peptidylglycine Alpha-amidating Enzyme, L. Mario Amzel, Johns Hopkins University School of Medicine

Session: Sulfur Chemistry and Biological Redox

 Radical-dependent Mechanisms of Post-translational Modification, Squire J. Booker, The Pennsylvania State University

Painting the Cysteine Chapel: New Tools to Probe Oxidation Biology, Kate S. Carroll, University of Michigan

Sensing Sulfur Status in Plants: Biochemical Integration of Multiple Inputs, Joseph Jez, Washington University, St. Louis

Session: Processive Enzymes
 Molecular Origami in Nature, Shiou-Chuan (Sheryl) Tsai, University of California, Irvine

Polyketide Megasynthases from Filamentous Fungi, Yi Tang, University of California, Los Angeles

Mycobacterial Polyketide Virulence Factors: Biosynthesis and Inhibition, Luis E. N. Quadri, Brooklyn College, The City University of New York

Session: Kinases, Phosphatases, and Phosphorus in Biological Reactions
 Evolution of a Robust Catalytic Scaffold for Hydrolytic Cleavage of Phosphate Ester Metabolites, Debra Dunaway-Mariano, University of New Mexico

Bivalent Inhibitors of Protein Kinases, Dustin J. Maly, University of Washington, Seattle

Computational Studies of Protein Kinases, J. Andrew McCammon, Investigator, Howard Hughes Medical Institute, University of California, San Diego

Sulfur Chemistry

The session on sulfur chemistry and biological redox, chaired by Carsten Krebs, features three diverse lectures highlighting the unique reactivity of the sulfur atom and its importance in biochemistry. Squire J. Booker (The Pennsylvania State University) will deliver a lecture, titled “Radical-dependent Mechanisms of Post-translational Modification,” in which he will describe several novel modifications of proteins that involve the insertion of sulfur atoms into unactivated C–H bonds. These reactions are considered to be the anaerobic counterpart to some of the reactions discussed in the session “Metals and Redox Chemistry,” involving activated forms of sulfur rather than dioxygen.

The lecture by Kate S. Carroll (University of Michigan), titled “Painting the Cysteine Chapel: New Tools to Probe Oxidation Biology,” will detail new proteomic approaches for detecting modifications occurring on sulfur-containing amino acid residues, which has great impact in the ability to sense cellular oxidative stress.

Joseph Jez (Washington University. St. Louis) will give a lecture, titled “Sensing Sulfur Status in Plants: Biochemical Integration of Multiple Inputs,” detailing mechanisms by which plants regulate their sulfur and thiol concentrations.

Processive Enzymes

Debra Dunaway-Mariano will chair a session on processive enzymes. This session does not include the classical nucleic acid polymerases that are discussed in other events of the meeting. Shiou-Chuan (Sheryl) Tsai (University of California, Irvine), under the title “Molecular Origami in Nature,” will present structural and mechanistic data on natural polyketide synthases, as well as systems based on this chemistry that can be used to synthesize novel polyketides. Fungal polyketide synthases will be discussed by Yi Tang (University of California, Los Angeles) in a lecture titled “Polyketide Megasynthases from Filamentous Fungi.” Luis E. N. Quadri (Brooklyn College, The City University of New York) will present his results on the synthesis and inhibition of bacterial virulence factors in a lecture entitled “Mycobacterial Polyketide Virulence Factors: Biosynthesis and Inhibition.”

Phosphoryl Transfer Reactions

In a session titled “Kinases, Phosphatases and Phosphorus in Biological Reactions” and chaired by L. Mario Amzel, speakers will discuss diverse aspects of the chemistry of phosphoryl transfer reactions. Debra Dunaway-Mariano (University of New Mexico) will present results of her comprehensive work on phosphatases in a lecture entitled “Evolution of a Robust Catalytic Scaffold for Hydrolytic Cleavage of Phosphate Ester Metabolites.”

Dustin J. Maly (University of Washington, Seattle), under the title “Bivalent Inhibitors of Protein Kinases,” will present his results on the development of cell permeable small molecules that allow the activation or inactivation of specific signaling enzymes in living cells, in particular, enzymes that mediate intracellular phosphorylation (the protein kinases and phosphatases).

Detailed aspects of the mechanism of phosphoryl transfer reactions will be presented by J. Andrew McCammon (Investigator, Howard Hughes Medical Institute, University of California, San Diego) who has used molecular dynamics simulations as well as QM/MM computational methods to study kinases and other enzymes. His lecture is titled “Computational Studies of Protein Kinases.”

Click here for more 2011 annual meeting thematic overviews.

For information on  annual meeting registration, housing and abstract submission, click here.

The four symposia also will include presentations chosen from submitted abstracts and will be complemented by related poster sessions. These symposia will present a unique opportunity for investigators interested in the chemistry and the detailed chemical mechanisms underlying biological processes to be exposed to an exciting selection of some of the most important recent developments in this area.

Reference

1. Balasubramanian, R., Smith, S., Rawat, S., Yatsunyk, L., Stemmler, T., and Rosenzweig, A. C. (2010) Oxidation of Methane by a Biological Dicopper Centre. Nature 465, 115 – 119.

Squire J. Booker (Squire@psu.edu) is an associate professor of chemistry and of biochemistry and molecular biology at The Pennsylvania State University. L. Mario Amzel (mamzel@jhmi.edu) is a professor and director of the department of biophysics and biophysical chemistry at the Johns Hopkins University School of Medicine.


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