Eli Lilly Award in Biological Chemistry

Professor Howard Hang, The Rockefeller University

For outstanding research in biological chemistry of unusual merit and independence of thought and originality.


Professor Howard Hang is the recipient of 2017 Eli Lilly Award. His laboratory is broadly interested in developing chemical approaches to understand fundamental aspects of host-microbe interactions and discovering new therapeutic approaches to combat infections. To elucidate key mechanisms involved in host-microbe interactions, the Hang laboratory has developed chemical methods to image and profile the biochemical targets of metabolites that are synthesized endogenously or derived from the environment (diet or microbiota). At the heart of this chemical approach is the design and synthesis of specific chemical reporters, metabolites bearing uniquely reactive groups, that can be chemically or enzymatically incorporated into biomolecules in vitro and in vivo and then selectively labeled with imaging or affinity reagents. Using this strategy, a variety of chemical reporters based on key metabolites (nucleosides, amino acids, lipids and other cofactors) have been developed in the Hang laboratory for the sensitive detection and analysis of metabolite-protein modifications such as palmitoylation, myristoylation, acetylation, prenylation, adenylylation and ADP-ribosylation. These metabolite chemical reporters have been used to functionally characterize metabolite-protein modifications in diverse areas of biology, and enabled the Hang laboratory to discover new mechanisms of host-microbe interactions. The Hang laboratory continues to develop new chemistry to explore host-microbe interactions, and is currently exploring anti-infectives from traditional medicines and beneficial microbiota.

Pfizer Award in Enzyme Chemistry

Professor Emily Balskus, Harvard University

For outstanding work in enzyme chemistry where the presence of enzyme action is unequivocally demonstrated.


Professor Emily Balskus is the recipient of the 2017 Pfizer Award in Enzyme Chemistry in recognition of her contributions to the understanding of enzymatic transformations from the human gut microbiome. Her research, which lies at the interface of chemical biology, enzymology, and microbiology, seeks to use chemical approaches to enhance our understanding of microbes and microbial communities (microbiomes). A major area of interest is elucidating how the metabolic capabilities of the human gut microbiome contribute to human health and disease. Using chemical knowledge to inform bioinformatics, her group mines DNA sequencing data to uncover new gut microbial metabolic pathways and enzymes; deciphering the functions and mechanisms of these enzymes facilitates the characterization of their distribution and abundance in human-associated microbes, the study of their impact on host biology, and the development of chemical tools to probe their roles in complex human microbial communities. Her work is providing a better understanding of how the chemical capabilities of the gut microbiome influence human biology and will illuminate new strategies for treating disease. For example, her group has discovered the enzymes involved in anaerobic choline metabolism, a gut microbial metabolic activity linked to heart, liver, and kidney diseases. The key enzyme in this pathway, choline trimethylamine-lyase, is a new member of the glycyl radical enzyme family, is widespread in human gut microbes, and is a potential target for therapeutic development. She has also uncovered key enzymatic transformations in the biosynthesis of colibactin, a gut bacterial genotoxin of unknown structure that may influence the progression of colorectal cancer. By studying colibactin biosynthesis prior to isolation and structure determination, her group has revealed structural features and biosynthetic logic that has informed ongoing efforts to identify the active genotoxin.

The Repligen Award in Chemistry of Biological Processes

Professor Wilfred A. van der Donk, University of Illinois, Urbana-Champaign

For outstanding contributions to the understanding of biological processes with particular emphasis on structure, function and mechanism.


Professor Wilfred A. van der Donk is the recipient of the 2017 Repligen Award in the Chemistry of Biological Processes in recognition of his contributions to the understanding of natural product biosynthesis. He has been a pioneer in the rapidly growing field of ribosomally synthesized and post-translationally modified peptide (RiPP) natural products. He recognized early on that their biosynthesis follows a similar logic in all three domains of life. His laboratory discovered that substrate-tolerant enzymes recognizing a leader peptide in the substrate direct these downstream post-translational modifications. He discovered that these enzymes are forgiving with respect to the sequence of a core peptide, where the post-translational modifications take place. This physical separation of substrate recognition and chemistry allows nature to evolve new RiPPs, and has been used by his laboratory as a fertile playground for synthetic biology and genome mining. To support these efforts, his group has studied the detailed mechanisms by which enzymes carry out a remarkable number of successive chemical transformations that morph a linear precursor peptide into a structurally complex and often macrocyclic product. In particular, his group reconstituted the biosynthesis of lantithionine-containing peptides and glycocins. He discovered unanticipated chemical transformations such as glutamyl-tRNA dependent dehydration of Ser and Thr residues, the first example of S-glycosylation, an intriguing example of substrate control over stereochemistry of an enzymatic reaction, and an enzyme that acts on 30 very different substrates to generate a combinatorial library of cyclic peptides. His laboratory also studied the biosynthesis of phosphonate natural products, providing a platform for large-scale genome mining with his colleague Bill Metcalf, and studying the mechanisms of phosphonate biosynthetic enzymes, including transformations involved in the production of the clinically-used antibiotic fosfomycin and the commercial herbicide phosphinothricin.

Gordon Hammes ACS Biochemistry Lectureship

Professor John A. Gerlt

For outstanding contributions in scientific research at the interface of chemistry and biology, particularly in the realm of biochemistry, biological chemistry and molecular biology.

Professor John A. Gerlt is the recipient of the 2017 Gordon Hammes ACS Biochemistry Lectureship in recognition of his contributions to understanding the mechanisms of enzyme-catalyzed reactions, the evolution of functions in enzyme superfamilies, and the assignment of functions to uncharacterized enzymes discovered in genome projects. His mechanistic work has focused on a variety of reactions, including phosphoryl transfer, formation of enolate anions, and decarboxylation. His laboratory devised methods for the synthesis and configurational analysis of oxygen chiral phosphodiesters (16O, 17O, and 18O) and applied these to nucleotidyl transfer and phosphodiester hydrolysis reactions. He was among the first to use site-directed mutagenesis to probe the mechanisms of enzyme-catalyzed reactions, initially focusing on Staphylococcal nuclease. His laboratory cloned the gene for mandelate racemase, which lead to the discovery of the enolase superfamily, the first mechanistic diverse enzyme superfamily, in collaborative work with Patricia Babbitt, George Kenyon, Gregory Petsko, and John Kozarich. His studies of mandelate racemase established that the active site stabilizes an enolate anion intermediate, previously thought to be too unstable to exist, by coordination to an essential divalent metal ion; this catalytic strategy applies to all reactions catalyzed by members of the enolase superfamily. His work on the evolution of function in the enolase, crotonase, and OMP decarboxylase superfamilies generated his interest in devising methods to predict and assign functions to uncharacterized enzymes discovered in genome projects. He has lead three large-scale multidisciplinary projects in this area, with these demonstrating that a combination of enzymology, structure determination (with Steven Almo), and both homology modeling and ligand docking (with Matt Jacobson) provided a powerful approach for predicting the functions of uncharacterized enzymes in novel metabolic pathways. As these studies continue, he is developing community-accessible web tools to analyze sequence-function space in enzyme families as well as their genome context. Gerlt has followed his Ph.D. mentor’s (Frank H. Westheimer) advice to choose interesting problems and follow them, irrespective of how they evolve.

The ACS Chemical Biology Lectureship

Professor Benjamin Cravatt, The Scripps Research Institute

For contributions that have had a major impact on scientific research in the area of Chemical Biology.


Professor Ben Cravatt is the distinguished recipient of the 2017 ACS Chemical Biology Lectureship. The award is in recognition of Prof. Cravatt’s ground-breaking development of activity-based protein profiling technology, which enables the functional annotation of enzymes using active site-directed chemical probes. Through post-genomic profiling of the functional state of enzymes in complex proteomes, Prof. Cravatt has identified key mammalian enzymes involved in regulation of lipid signaling pathways in cancer. Utilizing his activity-based profiling technology in conjunction with advanced mass spectrometry methods, Prof. Cravatt has generated global-scale maps of lipid-binding proteins, amino acid reactivities, and novel functional residues within the proteome. Prof. Cravatt’s technologies have been adopted by academic and industrial labs worldwide for broad-scale functional characterization of enzymes within biological systems, thus having far-reaching implications for our understanding of mammalian physiology and disease.

The Biopolymers Murray Goodman Memorial Prize

Professor Jennifer Doudna, University of California, Berkeley

For outstanding accomplishments in one or more of the areas of biochemistry, biophysical chemistry, biophysics, and/or chemical biology.


Professor Jennifer A. Doudna is the recipient of the 2016 Biopolymers Murray Goodman Memorial Prize. Doudna’s research focuses on determining how non-coding RNAs function in living systems. Following her pioneering work on the structures and catalytic mechanisms of ribozymes, Dr. Doudna made exceptional advances in understanding how small RNAs are produced and used to control gene expression in mammals and bacteria. This line of research led to the breakthrough discovery of an RNA-programmed DNA endonuclease, Cas9, which functions as part of a CRISPR-based acquired immunity system in bacteria. By determining the molecular mechanism by which Cas9 uses RNA to recognize and cleave double-stranded DNA at specific sites, Doudna and collaborator Emmanuelle Charpentier showed how the system could be readily adapted for use in human and other cells and organisms. This transformative technology has influenced fundamental and clinical biology by enabling genetic experiments that were previously difficult or impossible to conduct. As Doudna’s research revealed, the CRISPR-Cas9 enzyme functions by using a 20-nucleotide RNA sequence within a dual-guide RNA structure to base pair with a complementary target sequence within doubled-stranded DNA. By showing how the dual-guide RNA could be redesigned as a single-guide RNA with the necessary structure to bind Cas9 and to direct site-specific Cas9-mediated DNA cleavage, Doudna and Charpentier’s findings almost immediately became a transformative tool for molecular biologists. The CRISPR-Cas9 system has been used for site-specific genome editing in human somatic and pluripotent stem cells, mice, rats, plants, fruit flies, nematodes and fungi. This versatile system is useful in organisms and cell lines, and also in various ex vivo experiments where excision of specific segments of chromosomes is desirable. The CRISPR-Cas9 technology is likely to create new therapeutic strategies as well as impacting the fields of plant and synthetic biology.