Enzyme Structure and Function

May 22-24 2014 Enzyme Structure and Function Table of Contents Page General Information Support Staff About Harry Steenbock Downtown Area Map Sponsors Symposium Organizers - Remembering Mo 10 - 11 Schedule 12 - 13 Chair & Speaker Index 14 - 19 Chair Bios 20 - 51 Speakers & Abstracts 52 - 55 Poster Presenter Index 56 - 123 Poster Abstracts The 36th Steenbock Symposium Enzyme Structure and Function Is being held in honor of the life of W W Cleland, our colleague and friend The symposium will bring together leading scientists in the field to discuss their most recent research activities, and how they have been influenced by Professor Cleland’s remarkable contributions to enzyme chemistry The symposium promises to be both a great scientific experience as well as a chance for friends to come together to celebrate the life of our “mechanistic hero.” The Keynote speach will be given by Professor Paul F Cook from the University of Oklahoma, who will tell us about another side of Mo – Wallace the Philatelist 124 Attendee Addresses General Information Name Badges Registration Symposium participants are requested to wear the name badge during all conference activities Pick up conference materials on Thursday, May 22nd, 4:00-8:00 pm Promenade Terrace, Overture Center for the Arts, 201 State Street Opening Reception Thursday, May 22nd, 6:00-8:00 pm Promenade Hall, Overture Center for the Arts, 201 State Street Scientific Talks All talks will be in the Promenade Hall, Overture Center for the Arts, 201 State Street Talks begin at 8:45 am on Friday and conclude by 5:30 pm on Saturday Breakfast & Lunches Friday and Saturday Registration fee includes breakfasts, breaks and lunches at the Overture Center Please wear your name badge Poster Session Posters can be set up beginning Thursday at 4:00 pm and should be removed by Saturday at 5:30 pm Boards are numbered and reserved Please see the reservation list in this booklet and by the boards Closing Banquet Saturday, May 24th, 7:00-10:30 pm, in the Overture Hall Main Lobby, 201 State Street Enzyme Structure and Function Enzyme Structure and Function 36th Steenbock Symposium University of Wisconsin – Madison in honor of W W Cleland Symposium Organizers Hazel M Holden Debra Dunaway-Mariano Frank M Raushel Ivan Rayment Nigel G J Richards Symposium Coordinators Kate Ryan Department of Biochemistry University of Wisconsin – Madison Leah Leighty CALS Conference Services University of Wisconsin – Madison Robin Davies & Laura Vanderploeg Symposium Web Site, Abstract Book & Illustrations 36th Steenbock Symposium May 22nd – 24th, 2014 Harry Steenbock 1886–1967 A distinguished Professor of Biochemistry at the University of Wisconsin-Madison, Professor Steenbock's interests and contributions spanned many areas of nutrition and biochemistry Of special note is his discovery of the conversion of carotenes to vitamin A, the production of vitamin D by ultraviolet irradiation, and his central participation in demonstrating that copper and iron cure nutritional anemia The production of vitamin D by ultraviolet irradiation virtually abolished rickets, a widespread and debilitating disease Professor Steenbock patented the irradiation process for producing vitamin D and conceived the idea of the Wisconsin Alumni Research Foundation (WARF), a nonprofit foundation which invests the proceeds from patents for support of research in the natural sciences at the University of Wisconsin-Madison Professor Steenbock assigned his valuable patents to the Foundation, and revenue from them has provided uniquely flexible resources for fostering sustained scientific development on the Madison campus To honor Professor Steenbock, the Steenbock Endowment sponsors a symposium at the University of Wisconsin-Madison NC K E AV N TO HI LM GI H JO NG AN PI M HA R GO AS N ST ST W LAKE MENDOTA O NS NE E Downtown Area Map N ST LAKE ST MARION ST FRANCES ST R ST ON YT DA ON T PARK ST AI M ET W W E AV KING ST S LL IN RO RT R A MA C S SS GT IN H AS ON BL DT BA REGENT ST STATE CAPITOL OO DAYTON ST ST OC UNIVERSITY AVE JOHNSON ST ER TL ST ST ST Y ILD NR HE 201 State St E RO LL STATE AV BR OC Overture Center R CH IR 525 W Johnson St IS FA DT DoubleTree W CA BU LANGDON ST S N S Y ST PI R HE T LU NO R ,J NG KI VD BL EN L HN Y NE K NC DR JO ILS W LAKE MONONA Enzyme Structure and Function Symposium Sponsors The Steenbock Endowment Department of Biochemistry University of Wisconsin – Madison Individual donations in memory of W W Cleland: Eugene Cordes Perry A & Carolyn S Frey Hazel M Holden & Ivan Rayment Frank M Raushel George H & Susan B Reed Richard B Silverman Poster Awards courtesy of : 36th Steenbock Symposium May 22nd – 24th, 2014 Symposium Organizers Bio Page Organizers Affiliation Hazel M Holden University of Wisconsin-Madison Debra Dunaway-Mariano University of New Mexico 30 Frank M Raushel Texas A&M University 38 Ivan Rayment University of Wisconsin-Madison 50 Nigel G J Richards Indiana University – Purdue University Indianapolis 40 Hazel M Holden Hazel M Holden received her A B in chemistry at Duke University and her Ph D in biochemistry at Washington University, St Louis After postdoctoral positions at the University of Oregon and the University of Arizona, Dr Holden joined the faculty at the University of Wisconsin in 1988 She is now a full professor in the Biochemistry Department Her research interests focus on the structures and functions of enzymes involved in the biosynthesis of unusual di-, tri-, and tetradeoxysugars Enzyme Structure and Function 36th Steenbock Symposium May 22nd – 24th, 2014 Remembering Mo Cleland by Hazel M Holden I have struggled for weeks, debating how to begin this tribute to Mo Cleland, our colleague and our friend Sometimes words are simply inadequate, and that is, indeed, the case here I decided to check the Internet for information about Mo, and I came across an article written in the Northside News in 2010 It is reprinted on the following page, and it truly sums up the Mo we knew as our friend I never understood how important Mo had become to the neighborhood association until the memorial celebration that was held on May 11, 2013 at the University of Wisconsin When his friends from the neighborhood stood up to talk about Mo, many tears started to flow There have been numerous tributes to Mo over the past year, describing his enormous scientific accomplishments All of us who use DTT know of him - the so-called Cleland's reagent Yet he was much more than a list of scientific awards He was a mentor to so many of us In fact, one of the speakers at this meeting told me that he felt closer to Mo than to his own father After Hurricane Katrina hit, it was Mo who called him to make sure he was fine Rather than list out his research honors and achievements, I thought I would tell some “Mo” stories Undoubtedly, there will be many more told throughout the next couple of days There are plenty of them, some of which are not politically correct - but then again, neither was Mo For many years, when my daughter and son, Kelsey and Harrison, were growing up, Mo and I had season tickets to the Madison Symphony Orchestra We would go on Sunday afternoons, and, of course, Mo wouldn’t think of sitting anywhere but in the front row I suspect the orchestra members got to know us We heard some spectacular performances over the years including the Verdi Requiem, which Mo loved Afterwards, Mo would come over for dinner, and over time he became “Uncle Mo.” Kelsey and Harrison always wanted to play hide-and-go-seek Mo was pretty good at seeking, but not so great with hiding After dinner, he would read to Kelsey and Harrison, and Uncle Mo became to them the grandfather they never had He loved stamps, as we all know, and once he came to dinner with a stamp book and some stamps for Kelsey to start her own collection We were also fortunate to travel to a meeting in Australia with Mo, and I can still see him petting the kangaroos in the wildlife park with Kelsey and Harrison It was special to see the interplay between this famous scientist and the “crumb crushers” as Mo referred to them Throughout my career in Wisconsin, Mo was never anything but supportive He would drop everything to take a look at a new structure or discuss a possible catalytic mechanism Mo read every grant I submitted to the NIH and nearly every paper that I ever sent to a journal His advice was invaluable In the last paper we co-authored together in 2012, it was Mo who figured out that a covalent adduct had formed between CoA and GDP-perosamine Needless to say, I miss his insight terribly Along these lines, I have another story to tell about Professor Cleland A post-doctoral fellow in Mo’s laboratory was working on determining the structure of an enzyme, and I got involved in the project by helping to build the protein model When it came time to write the paper, the two of us put Mo’s name on the author list As usual, Mo took time to read the paper and he had his list of comments, among them to take his name off the paper We asked why, and Mo said that he really didn’t need another publication If his name was included, it would detract from the post-doctoral fellow’s contribution, and that wouldn’t be good We took Mo’s name off the paper, but I have to say that to this day we still speak of Mo’s generosity This anecdote exemplifies what is perhaps the most significant aspect of Mo’s scientific career Even with the welldeserved awards and accolades Mo accrued during his life, arguably his most enduring legacy will be all the individuals - graduate students, post-doctoral fellows, and colleagues - that he mentored and helped to achieve their scientific career goals As the above story illustrates, he never wanted or sought out credit for his contributions to another person’s success His unselfish behavior was, and still is, so uncommon That is what made Mo our scientific hero In closing, let me say that the next few days will be a very meaningful time for all of us to celebrate the life of William Wallace “Mo” Cleland We are all lucky to have known Mo He may not be here anymore, but surely his spirit lives on Let us enjoy the talks and the posters, and spend time laughing at “Mo” stories And remember Mo’s insistence that when you interview for a faculty position, make sure you negotiate a good parking spot Enzyme Structure and Function Mo Cleland: scientist, philatelist and opera lover by Ellen Barnard Northside News April/May 2010 William Wallace “Mo” Cleland is a serious man with a passion for opera, Jane Austen and the original plates from which stamps are printed Known as Mo to his friends and to fellow scientists at the University of Wisconsin, Wallace by his philately (stamp collecting) friends, and William only to telemarketers and strangers, he is an 80 years-young man who cares deeply about his family and his neighborhood, and even when he’s weighing in on a heavy subject, has a mischievous gleam in his eye Mo comes from a family of Scottish ministers and scientists-teachers, whom he describes as “natural BSers… both ministers and teachers just love to hear themselves talk!” He was always known by his middle name, Wallace, until friends nicknamed him “Wall-Mo,” later shortening it to Mo He was a “badly behaved” child who struggled with social skills and was moved ahead in school to try to challenge him into behaving better He went to college at the age of 16, finding himself among a group of young “smartasses” and returning war veterans He credits his improvement in social skills to the fact that Oberlin required the men and women to sit down to dinner together every evening, providing the perfect opportunity to get to know women well without the challenges of having to date one He attended the UW-Madison “for the sailing,” got a Ph.D., then was drafted, where he learned that he liked shooting guns, but was not a good soldier “I didn’t well with all that spit-and-polish discipline.” To those who know Mo now, this will come as no surprise, as he is quite adamant about going on his own, independentlyreasoned way through life After the Army, he found himself a rewarding post-doctoral spot and eventually came back at the UW-Madison, where he still works He hasn’t retired because he believes “if you stop, you die.” His career-defining scientific achievement happened in 1963 when he published a theoretical development that became the basis for many other studies and has made the “most cited” scientific discoveries list “I love it when you discover a bunch of little things that help explain bigger mysteries,” he said “I love to solve mysteries’ mysteries and to figure out how things work.” Mo lived on the Isthmus and then the Northside, first on the lake so he could sail right off the pier in his back yard, then moving to a small house on the Northside when he needed less of a house He and his wife raised two daughters, of whom he is very proud Though they are no longer married, he and his ex-wife are the best of friends, “maybe better friends now that we don’t have to figure out how to live together!” He became politically involved when the Mendota Sailing Club was seeking a new clubhouse, joining the Northside Planning Council (NPC) in order to advocate for the outcome he supported He has remained active with the NPC since then He hopes to see many more events where all the people who live in our community get to know each other better and feel more connected to others He also hopes that we don’t forget to look out for each other and for the health and safety of our neighborhoods Mo is deeply generous when it comes to the people and causes that he loves and volunteers his time as generously as his money He will tell you a joke that will catch you by surprise, and his head is full of exotic bits and pieces of information that he shares to “delight and amuse” people He’s opinionated, soft-hearted and a person one would be proud to call “friend.” 36th Steenbock Symposium M o C l e l a n d l o ev s t h e o p e r a a n d i s sh m u si c oc l l e ct i o n h e h o l d s os d e a r May 22nd – 24th, 2014 o w n h e re su rro u n d e d b y th e N-Acylsulfonamide Inhibitors of UDP-Galactopyranose Mutase Act as Carboxylate Mimics and Disrupt Mycobacterial Growth Valerie J Winton*1, Nir London2, Brian K Shoichet2, and Laura L Kiessling1,3 Departments of Chemistry1 and Biochemistry3, University of Wisconsin-Madison, Madison, WI, 53706 USA Department of Chemistry2, University of Toronto, Toronto, ON, M5R 0A3 Canada Mycobacterium tuberculosis is the causative agent of tuberculosis, an infectious disease responsible for over one million deaths per year.1 Mycobacteria are intrinsically resistant to antibiotic treatment due to their thick, hydrophobic cell wall, which constitutes a near-impermeable barrier between drugs and their targets This unique structure contains a highly branched arabinogalactan polysaccharide which provides a covalent attachment point for an exterior layer of mycolic acids.2 The cell wall complex is crucial for mycobacterial viability and pathogenesis, and therefore is an attractive target for potential antibacterial agents UDP-galactopyranose mutase (UGM) provides the activated galactofuranose sugar donor essential for construction of the arabinogalactan.3 A class of 2aminothiazoles, developed in the Kiessling laboratory to target UGM, have been found to inhibit mycobacterial growth.4 These compounds include a carboxylate moiety which is crucial for binding However, carboxylates can be metabolized to toxic by-products5 and are believed to impart unfavorable membrane permeation characteristics.6 In this work, we designed a series of N-acylsulfonamide variants as carboxylate mimics We anticipated that this modification would preserve required binding interactions and would afford greater permeation of the cell envelope while minimizing toxicity to mammalian cells The N-acylsulfonamide analogues were shown to be effective carboxylate mimics, and they exhibit in vitro UGM inhibition comparable to their predecessors In addition, several Nacylsulfonamide derivatives induce superior growth inhibition of Mycobacterium smegmatis in both liquid and solid media cultures WHO and Global Tuberculosis Programme Global Tuberculosis Report 2012 Brennan, P J Tuberculosis 2003, 83, 91-97 Pan, F.; Jackson, M.; Ma, Y.F.; McNeil, M J Bacteriol 2001, 183, 3991–3998 Dykhuizen, E C.; May, J F.; Tongpenyai, A.; Kiessling, L.L J Am Chem Soc 2008, 130, 6706-6707 Skonberg, C., et al Expert Opin Drug Metab Toxicol 2008, 4, 425–438 Klemm, A R., et al BBA-Biomembranes 1998, 1373, 17-26 120 36th Steenbock Symposium May 22nd – 24th, 2014 C TD C od e: a C ombinatorial C od e for E uk aryot ic Transcription Y an J essie Z hang*, Mengmeng Z hang, Y onghua Luo, Sollepura D Y ogesha and J oshua E Mayfield D epartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, U niversity of Texas at Austin, Austin, TX 7812 In eukaryotes, the C-terminal domain of RN A polymerase II (CTD ) orchestrates the temporal and spatial control of transcription and is involved in the epigenetic regulation of gene expression E rrors in CTD regulation can result in cell death, cancer and severe developmental defects The CTD executes its function as transcription modulator through various post-translational modifications on its heptad repeat sequences Recently, novel modifications on new regulatory sites of CTD have been identified, setting the stage for the possibility of combinatorial mechanisms for transcription regulation We focused on two well-characterized modification of CTD , namely serine phosphorylation and prolyl isomerization, and discuss the interplay between the enzymes regulating these modification states Our results established that the selectivity of prolyl isomerization state of CTD on phosphatases can lead to differentiated outcome for the CTD phosphorylation state and therefore, transcription To further investigate the prolyl selectivity, we developed chemical compounds that can be used to probe such subtle structural variation in the CTD binding proteins These compounds closely mimic the cis or trans proline state and can be effectively recognized by CTD phosphatases The application of such chemical probes can help us understand the molecular mechanism of the interplay between phosphorylation and prolyl isomerization state and how that affect the conformational status of CTD in transcription temporally and spatially Enzyme Structure and Function 121 E xploration of the M echanism of Oxalate Decarboxyl ase by H K inetic I sotope E ffects eavy A tom Wen Z hu,‡* Laurie A Reinhardt,§ Whitney F Kellett,‡ and N igel G J Richards‡ ‡ D epartment of Chemistry and Chemical Biology, Indiana U niversity-Purdue U niversity Indianapolis, Indianapolis, IN 46202 U S.A § Institute for E nzyme Research and D epartment of Biochemistry, U niversity of Wisconsin-Madison, Madison, WI 53726 U S.A Oxalate decarboxylase (OxD c) is a Mn-dependent protein which catalyzes the decarboxylation of oxalate to yield formate and carbon dioxide in the presence of O2 [ 1] Heavy atom kinetic isotope effects (KIE s) study has been successfully employed in probing the mechanism of wild type (WT) OxD c KIE s measurements represented a detailed information of the catalytic mechanism of WT OxD c, which the decarboxylation of enzyme bound oxalate involves heterolytic cleavage of C-C bond and consistent with the proton-coupled electron transfer mechanism [ 2] Moreover, the results of KIE s for several site-specific mutations of OxD c, including the R92K , W132F, R270K , E 333D , T165V , and SE N S161-4 D ASN variants, were able to provide more detail on the functional role of these conserved residues in OxD c [ 3,4 ] This poster will present a review of the KIE s study on OxD c and show how these results help us to explain the mechanism of OxD c [ 1] Svedruzic, D ; J onsson, S.; Toyota, C G.; Reinhardt, L A.; Ricagno, S.; Lindqvist, Y ; Richards, N G J A rc h B i oc he m B i ophy s 205 43, 176- 192 [ 2] Reinhardt, L A.; Svedruzic, D ; Chang, C H.; Cleland, W W.; Richards, N G J J A m C he m Soc 03 125, 1244- 1252 [ 3] Svedruzic, D ; Liu, Y ; Reinhardt, L A.; Wroclawska, E ; Cleland, W W.; Richards, N G J A rc h B i oc h em B i ophy s 207 46, 36-47 [ 4] Saylor, B T.; Reinhardt, L A.; Lu, Z ; Shukla, M S.; N guyen, L.; Cleland, W W.; 51, 2911- 2920 Angerhofer, A.; Allen, K N ; Richards, N G J B i o c h em i st ry 201 122 36th Steenbock Symposium May 22nd – 24th, 2014 Target Selection for Killing Lethal Opportunistic Bacterial Pathogens in Cystic Fibrosis Patients Lucas Zimney*, Rachel Gomez, Kaila Matthews and Debra Dunaway-Mariano Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, NM 87131, USA Pseudomonas aeruginosa is an opportunistic pathogen that causes chronic bacterial infections in cystic fibrosis patients Through the formation of thick biofilm and the extensive use of quorum sensing, the bacterium quickly gains antibiotic resistance, making infections extremely difficult to treat In fact, Pseudomonas aeruginosa infections are a leading cause of morbidity and mortality in individuals with cystic fibrosis Lipids such as phosphatidylcholine make up a large percentage of lung surfactant and are available as a carbon source to the bacterium These lipids are broken down into free fatty acids that are activated for further degradation by acyl-CoA synthetases To better understand the role of acyl-CoA synthetases in the bacterium’s pathogenicity and adaptation to the host environment, recombinant protein for nine previously uncharacterized acyl-CoA synthetases was purified and their catalytic efficiencies evaluated through a coupled enzymatic assay In addition, a high-throughput screening assay was developed to qualitatively evaluate the acyl-CoA synthetases’ substrate ranges The results of the high-throughput screen and steady-state kinetics indicate that many of the acyl-CoA synthetases display overlapping and promiscuous specificities, while others display distinct, specific activity A better understanding of the specific roles of acyl-CoA synthetases in Pseudomonas aeruginosa could help guide rational inhibitor design and drug targeting in an effort to more effectively treat Pseudomonas aeruginosa infections Enzyme Structure and Function 123 124 36th Steenbock Symposium May 22nd – 24th, 2014 Symposium Participant Addresses Lynn Abell Bristol-Myers Squibb 90 Dispatch Drive Washington Crossing PA 18977 USA lynn.abell@bms.com David Aceti UW-Madison Biochemistry 445 Henry Mall Madison WI 53706 USA djaceti!@wisc.edu Karen Allen Boston University Dept of Chemistry Metcalf Center for Science & Engineering Boston MA 02215-2521 USA drkallen@bu.edu Mark Anderson UW-Madison Biochemistry 440 Henry Mall Madison WI 53706 USA wombats@nmrfam.wisc.edu Mark Anderson UW-Madison 1710 University Ave Madison WI 53726 USA maander2@facstaff.wisc.edu Vernon Anderson NIH/NIGMS 45 Center Drive Bethesda MD 20892 USA andersonve@mail.nih.gov Michael Andreas UW-Madison 1659 Capital Ave Apt Madison WI 53705 USA mandreas@wisc.edu Richard Armstrong Vanderbilt University Dept of Biochemistry & Chemistry 842 RRB Nashville TN 37205 USA r.armstrong@vanderbilt.edu Paul Attwood The University of Western Australia School of Chemistry and Biochemistry 35 Stirling Highway Crawley WA6009 AUSTRALIA paul.attwood@uwa.edu.au Mikio Bakke Kikkoman USA R&D Laboratory, Inc 505 South Rosa Road, Suite 107 Madison WI 53719 USA mbakke@kikkoman.com David Ballou University of Michigan Dept Biological Chemistry 5301D MSRB III Ann Arbor MI 48109-0600 USA dballou@umich.edu Vahe Bandarian University of Arizona Dept of Chemistry & Biochemistry 1041 E Lowell Street Tucson AZ 85721 USA vahe@email.arizona.edu Oleg Barski NIH/NIGMS/PPBC 45 Center Dr Bethesda MD 8292 USA barskioa@nigms.nih.gov Elham Behshad Incyte Corp 141 & Henry Clay Rd Wilmington DE 19707 USA ebehshad@incyte.com Craig Bingman UW-Madison Department of Biochemistry 433 Babcock Drive Madison WI 53706 USA cbingman@biochem.wisc.edu DJ Black Bio-Logic USA 9050 Executive Park Drive Suite 105C Knoxville TN 37923 USA dj.black@bio-logic.us John Blanchard Albert Einstein College of Medicine of Yeshiva University, Dept of Biochemistry 1300 Morris Park Avenue Bronx NY 10461 USA john.blanchard@einstein.yu.edu Squire Booker Pennsylvania State University Dept of Chemistry 302 Chemistry Bldg University Park PA 16802 USA sjb14@psu.edu Haley Brown UW-Madison 746 W Main St Apt 302 Madison WI 53715 USA habrown3@wisc.edu Nathan Bruender University of Arizona 1041 E Lowell St Bioscience West Rm 539 Tucson AZ 85721 USA bruender@email.arizona.edu Paula Bruice University of California-Santa Barbara Department of Chemistry and Biochemistry Santa Barbara CA 93106 USA pybruice@chem.ucsb.edu Thomas Bruice University of California-Santa Barbara Department of Chemistry & Biochemistry Santa Barbara CA 93106 USA tcbruice@chem.ucsb.edu Tyrel Bryan University of New Mexico 300 Terrace St NE Albuquerque NM 87131 USA tbryan@unm.edu David Cane Brown University Dept of Chemistry, Box H Providence RI 02912-9108 USA david_cane@brown.edu Anne-Marie Carpenter University of South Florida 4202 E Fowler Ave CHE 205 Tampa FL 33620 USA acarpenter@mail.usf.edu Charu Chaudhry Bristol-Myers Squibb Pine Ridge Drive Edison NJ 8820 USA Charu.Chaudhry@BMS.com Yu Chen University of South Florida 12901 Bruce B Downs Blvd MDC 07 Tampa FL 33612 USA ychen1@health.usf.edu Enzyme Structure and Function 125 Symposium Participant Addresses Yuwei Chen University of Arizona 5400 E Williams Blvd Apt 7308 Tucson AZ 85711 USA chen27@uwalumni.com Elsa Cleland University of California-San Diego Ecology, Behavior & Evolution 9500 Gilman Drive La Jolla CA 92093-0116 USA Joan Cleland 355 Pearl Street Boulder CO 80302 USA Darrell Cockburn University of Michigan Medical School 1150 W Medical Ctr Drive Ann Arbor MI 48109 USA dcoc@umich.edu Paul F Cook University of Oklahoma Dept of Chemistry & Biochemistry 101 Stephenson Parkway Norman OK 73019 USA Paul D Cook Grand Valley State University Campus Drive Allendale MI 49401 USA cookp@gvsu.edu Eugene Cordes 3603 Saint Davids Road Newtown Square PA 19073 USA cordeseh@aol.com Susan Colette Daubner St Mary’s University One Camino Santa Maria San Antonio TX 78228 USA sdaubner@stmarytx.edu Victor Davidson University of Central Florida Burnett School of Biomedical Sciences 6900 Lake Nona Blvd Orlando FL 32828 USA victor.davidson@ucf.edu Paritosh Dayal Auburn University 354 W Glenn Ave Apt 105, Lauren Place Auburn AL 36830 USA pvd0001@auburn.edu Daniel Dempsey University of South Florida Department of Chemistry 4202 E Fowler Ave CHE 205 Tampa FL 33620 USA dempseyd@mail.usf.edu John Denu UW-Madison 5905 Linden Pkwy McFarland WI 53558 USA jmdenu@wisc.edu Kevin Desai UW-Madison 303 N Hamilton St Apt 223 Madison WI 53703 USA kkdesai@wisc.edu Roger Diehl UW-Madison 1101 University Ave Madison WI 53706 USA rogercdiehl@gmail.com Cathy Drennan MIT/HHMI 77 Massachusetts Ave Cambridge MA 2139 USA cdrennan@mit.edu Kristin Droege Vanderbilt Graduate School 411 Kirkland Hall Nashville TN 37240 USA kristin.d.droege@vanderbilt.edu Debra Dunaway-Mariano University of New Mexico Dept of Chemistry & Chemical Biology MSC03 2060 Albuquerque NM 87131 USA dd39@unm.edu Holly Ellis Auburn University 179 Chemistry Building Auburn AL 36849 USA ellishr@auburn.edu Rebecca Fagan University of Iowa 51 Newton Rd 4-339 Bowen Science Building Iowa City IA 52242 USA rebecca-fagan@uiowa.edu Paul Fitzpatrick University of Texas at San Antonio Dept of Biochemistry 7703 Floyd Curl Drive San Antonio TX 78229-3900 USA fitzpatrick@biochem.uthsca.edu Wayne Frasch Arizona State University Faculty of Biomedicine and Biotechnology School of Life Sciences Tempe AZ 85287-4501 USA frasch@asu.edu Perry Frey UW-Madison Dept of Biochemistry 433 Babcock Drive Madison WI 53706 USA frey@biochem.wisc.edu Barbara Gerratana NIGMS 2448 39th Place NW Washington DC 20007 USA bgerratana@hotmail.com Rachel Gomez University of New Mexico-MARC University of New Mexico Albuquerque NM 87144 USA rgomez03@unm.edu Michael Goodman Vanderbilt University 1123 Clifton Lane Nashville TN 37204 USA michael.goodman23@gmail.com Charles Grimshaw Takeda California 10410 Science Center Drive San Diego CA 92121 USA Ched.Grimshaw@takeda.com Andrew Gulick Hauptman-Woodward Institute University at Buffalo Structural Biology 700 Ellicott St Buffalo NY 14203 USA gulick@hwi.buffalo.edu 126 36th Steenbock Symposium May 22nd – 24th, 2014 Symposium Participant Addresses Qi Guo University of Iowa 245 Hawkeye Court Iowa City IA 52246 USA qi-guo@uiowa.edu Christopher Halkides UNCW 601 South College Road Wilmington NC 28403 USA halkidesc@uncw.edu Michael Harris CWRU School of Medicine Dept of Biochemistry 2109 Adelbert Rd Cleveland OH 44106 USA meh2@case.edu Lizbeth Hedstrom Brandeis University MS 009 415 South St Waltham MA 2453 USA hedstrom@brandeis.edu Adrian Hegeman University of Minnesota 1970 Folwell Ave St Paul MN 55108 USA hegem007@umn.edu Alvan Hengge Utah State University Department of Chemistry & Biochemistry 300 Old Main Hill Logan UT 84322 USA alvan.hengge@usu.edu Timothy Herdendorf Iowa State University 4192 MBB Pammel Dr Ames IA 50011 USA therdend@iastate.edu Hazel Holden UW-Madison 440 Henry Mall 3424A Biochemical Sciences Bldg Madison WI 53706 USA hazel_holden@biochem.wisc.edu Geoff Horsman Wilfrid Laurier University 75 University Ave W Waterloo N2L 3C5 CANADA geoff.horsman@gmail.com Aaron Hoskins UW-Madison Dept of Biochemistry 433 Babcock Drive Madison WI 53706 USA ahoskins@wisc.edu James Janc Theravance, Inc 901 Gateway Blvd South San Francisco CA 94080 USA jjanc@theravance.com Jiaoyang Jiang UW-Madison 777 Highland Ave School of Pharmacy Madison WI 53705 USA jjiang@pharmacy.wisc.edu Kayunta Johnson-Winters University of Texas-Arlington 700 Planetarium Place Box 19065 Arlington TX 76019 USA kayunta@uta.edu Alexander Justen UW-Madison Dept of Biochemistry 433 Babcock Drive Madison WI 53706 USA ajusten@wisc.edu Whitney Kellett Indiana University Purdue University Indianapolis 402 N Blackford LD 326 Indianapolis IN 46202 USA wkellett@iupui.edu Ambalika Khadria UW-Madison Dept of Chemistry 433 Babcock Drive Madison WI 53706 USA khadria@wisc.edu Laura Kiessling UW-Madison 1101 University Avenue Madison WI 53706 USA kiessling@chem.wisc.edu Virginia Kincaid UW-Madison Dept of Biochemistry 728 E Dayton St Madison WI 53703 USA vkincaid@wisc.edu Jack Kirsch UC Berkeley QB3 Institute 572 Stanley Hall Berkeley CA 94720-3220 USA jfkirsch@berkeley.edu Judith Klinman University of California-Berkeley Dept of Chemistry QB3 Institute Berkeley CA 94720 USA klinman@berkeley.edu Andrew Knappenberger Case Western Reserve University 2660 Mayfield Road Apt Cleveland Heights OH 44106 USA ajk126@case.edu Amnon Kohen University of Iowa Dept of Chem Iowa City IA 52242 USA amnon-kohen@uiowa.edu Nicole Koropatkin University of Michigan Medical School 1150 W Medical Center Dr Ann Arbor MI 48109 USA nkoropat@umich.edu Loren LaPointe UW-Madison Dept of Biochemistry 315 N Pickney Madison WI 53703 USA llapointe@wisc.edu Kafryn W Lieder The Well-Tempered Word, LLC 6906 Tottenham Road Madison WI 53711 USA kafrynw@gmail.com Hsuan-Chun Lin Case Western Reserve University Department of Biochemistry 10900 Euclid Avenue Cleveland OH 44106 USA hxl366@case.edu Yi Lin Marquette University 1810 W Wisconsin Ave Apt 406 Milwaukee WI 53233 USA yi.lin@marquette.edu Enzyme Structure and Function 127 Symposium Participant Addresses John Lipscomb University of Minnesota 6-155 Jackson Hall, BMBB 321 Church St SE Minneapolis MN 55455 USA lipsc001@umn.edu Chunliang Liu University of New Mexico 300 Terrace St NE Albuquerque NM 87131 USA pagani99@unm.edu Danielle Lohman UW-Madison Biochemistry Dept 625 E Mifflin St Madison WI 53703 USA dlohman@wisc.edu Steven Mansoorabadi Auburn University 179 Chemistry Building Auburn AL 36849 USA som@auburn.edu John Markley UW-Madison Biochemistry Dept 433 Babcock Drive Madison WI 53706 USA jmarkley@wisc.edu John Marlier Cal Poly Department of Chemistry & Biochemistry Grand Ave San Luis Obispo CA 93407 USA jmarlier@calpoly.edu Kaila Matthews University of New Mexico 300 Terrace St NE Albuquerque NM 87131 USA kmatth44@unm.edu Rowena Matthews University of Michigan 1609 S University Ave Ann Arbor MI 48104 USA rmatthew@umich.edu Thomas Meek Texas A&M University 2128 TAMU College Station TX 77843-2128 USA tdmeek@tamu.edu David Merkler University of South Florida Department of Chemistry 4202 E Fowler Ave CHE 205 Tampa FL 33620 USA merkler@usf.edu Zachary Miles University of Arizona 1041 E Lowell St Rm 539 Tucson AZ 85721 USA zmiles@email.arizona.edu Brian Miller Florida State University 4005 Chemical Sciences Laboratory Tallahassee FL 32306-4390 USA miller@chem.fsu.edu Morgan Miller Iowa State University 4128 Molecular Biology Building Ames IA 50011 USA millerme@iastate.edu Susan Miller University of California San Francisco 600 16th St., GH S-512B UCSFMC 2280 San Francisco CA 94518-2517 USA smiller@cgl.ucsf.edu Tatiana Mishanina University of Iowa E236 Chemistry Building Iowa City IA 52242 USA tatiana-mishanina@uiowa.edu Lisa Mueller University of Wisconsin-Milwaukee 4535 N Newhall St Shorewood WI 53211 USA lisamueller414@gmail.com Jonathan Musila Auburn University 179 Chemistry Building Auburn AL 36849-5312 USA jmm0090@auburn.edu David Nelson UW-Madison 433 Babcock Drive Biochemistry Laboratories Madison WI 53706 USA nelson@biochem.wisc.edu Mark Nelson DuPont Central Research and Development PO Box 80328 Wilmington DE 19880-0328 USA mark.j.nelson@usa.dupont.com Scott Nelson Iowa State University 4112 Molecular Biology Building Ames IA 50011 USA swn@iastate.edu Derek Nichols University of South Florida College of Medicine Dept of Molecular Medicine Tampa FL 33609 USA dnichol1@health.usf.edu Courtney Niland Case Western Reserve University 2109 Adelbert Rd School of Medicine Wood Building 449-E Cleveland OH 44106 USA cnn7@case.edu Dexter Northrop UW-Madison School of Pharmacy 777 Highland Avenue Madison WI 53705 USA dbnorthrop@pharmacy.wisc.edu David Pagliarini UW-Madison Biochemistry Department 433 Babcock Drive Madison WI 53706 USA pagliarini@wisc.edu June Pais New England Biolabs 240 County Road Ipswich MA 1938 USA pais@neb.com Bruce Palfey University of Michigan Department of Biological Chemistry 1150 W Medical Center Dr Ann Arbor MI 48109 USA brupalf@umich.edu Jared Parker DuPont Rt 141 Henry Clay E228/310B Wilmington DE 19803 USA Jared.B.Parker@dupont.com 128 36th Steenbock Symposium May 22nd – 24th, 2014 Symposium Participant Addresses James Peliska Ave Maria University 5050 Ave Maria Blvd Ave Maria FL 34142 USA james.peliska@avemaria.edu Orville Pemberton University of South Florida Morsani College of Medicine 12901 Bruce B Downs Blvd., MDC Tampa FL 33612-4799 USA opembert@mail.usf.edu Rebecca Phillips UW-Madison 205 S Henry St Apt D Madison WI 53703 USA taphephobia@gmail.com Rex Pratt Wesleyan University Chemistry Dept Lawn Ave Middletown CT 6459 USA rpratt@wesleyan.edu Ron Raines UW-Madison Department of Biochemistry 433 Babcock Drive Madison WI 53706 USA rtraines@wisc.edu Frank Raushel Texas A&M University Dept of Chemistry 3255 TAMU College Station TX 77843-3255 USA raushel@tamu.edu Ivan Rayment UW-Madison 440 Henry Hall 3424B Biochemical Sciences Bldg Madison WI 53706 USA ivan_rayment@biochem.wisc.edu George Reed UW-Madison Dept of Biochemistry 433 Babcock Drive Madison WI 53706 USA ghreed@wisc.edu Laurie Reinhardt UW-Madison 1710 University Ave Madison WI 53726 USA lareinha@wisc.edu Gregory Reinhart Texas A&M University Dept of Biochemistry and Biophysics 2128 TAMU College Station TX 77843 USA gdr@tamu.edu Alan Rendina GlaxoSmithKline 1250 S Collegeville Road Mail Code UP12-110 Collegeville PA 19426 USA alan.r.rendina@gsk.com John Richard University at Buffalo Dept of Chemistry 633 Natural Science Complex Buffalo NY 14260 USA jrichard@buffalo.edu Nigel Richards Indiana Univ.-Purdue Univ Indianapolis Dept of Chemistry & Chemical Biology 402 N Blackford Street Indianapolis IN 46202-3217 USA ngrichar@iupui.edu Mark Rishavy Cleveland Clinic Foundation 9500 Euclid Avenue Cleveland OH 44195 USA rishavm@ccf.org Santiago Rodriguez Ospina University of South Florida 4202 E Fowler Ave CHE 205 Tampa FL 33620 USA santiago3@mail.usf.edu Daniel Roston UW-Madison Dept of Chemistry 1101 University Ave Madison WI 53706 USA droston@chem.wisc.edu Kate Ryan UW-Madison 420 Henry Mall 1142F Biochemistry Madison WI 53706 USA cryan7@wisc.edu Ari Salinger UW-Madison 436 W Wilson St Apt Madison WI 53703 USA asalinger@wisc.edu John Schloss Marshall University School of Pharmacy One John Marshall Drive Huntington WV 25755 USA schloss@marshall.edu Barbara Schowen University of Kansas 962 East 1338 Road Lawrence KS 66046-9630 USA bschowen@ku.com Richard Schowen University of Kansas 962 East 1338 Road Lawrence KS 66046 USA rschowen@ku.edu Vern Schramm Albert Einstein College of Medicine 1300 Morris Park Avenue Department of Biochemistry Bronx NY 10461 USA vern.schramm@einstein.yu.edu Phillip Schwartz Takeda California, Inc 10410 Science Center Drive San Diego CA 92121 USA phillip.schwartz@takeda.com Lauren Seiple Siemens Healthcare Diagnostics Glasgow Business Community P.O Box 6101; Mail Code 707 Newark DE 19714 USA laseiple@gmail.com Alessandro Senes UW-Madison 433 Babcock Dr Room 415C Madison WI 53706 USA senes@wisc.edu Erica Shepard 4202 268th Avenue NE Redmond WA 98053 USA Nicholas Silvaggi University of Wisconsin-Milwaukee 3210 North Cramer St Milwaukee WI 53211 USA silvaggi@uwm.edu Enzyme Structure and Function 129 Symposium Participant Addresses Paul Sims University of Oklahoma 101 Stephenson Parkway Norman OK 73019 USA psims@ou.edu Kevin Skare 8674 Hampton Bay Place Mason OH 45040 USA kskare@cinci.rr.com Brian Smith Medical College of Wisconsin Department of Biochemistry 8701 Watertown Plank Road Milwaukee WI 53226 USA brismith@mcw.edu Mark Snider The College of Wooster 943 College Mall Wooster OH 44691 USA msnider@wooster.edu Pablo Sobrado Virginia Tech Department of Biochemistry Blacksburg VA 24061 USA psobrado@vt.edu Martin St Maurice Marquette University PO Box 1881 Dept of Biological Sciences Milwaukee WI 53201 USA martin.stmaurice@marquette.edu JoAnne Stubbe MIT 77 Massachusetts Avenue Room 18-598 Cambridge MA 2139 USA stubbe@mit.edu Keenan Taylor UW-Madison IPIB 440 Henry Mall Madison WI 53705 USA kctaylor@wisc.edu James Thoden UW-Madison 440 Henry Mall 2406b Biochemical Sciences Madison WI 53706 USA jbthoden@wisc.edu Peter Tipton University of Missouri Dept of Biochemistry 117 Schweitzer Hall Columbia MO 65211 USA tiptonp@missouri.edu Sarah Toews Keating University of New Mexico 300 Terrace St NE Albuquerque NM 87131 USA setoews@unm.edu Liang Tong Columbia University Department of Biological Sciencces New York NY 10027 USA ltong@columbia.edu Austin Travis MIT 10 Forest Street Cambridge MA 2140 USA atravis@mit.edu Eldon Ulrich UW-Madison Dept of Biochemistry 433 Babcock Dr Madison WI 53706 USA elu@bmrb.wisc.edu Wilfred van der Donk University of Illinois at Urbana-Champaign 161 Roger Adams Laboratory, Box 38-5 600 S Matthews Avenue Urbana IL 61801 USA vddonk@illinois.edu Ronald Viola University of Toledo Department of Chemistry & Biochemistry Toledo OH 43606 USA ron.viola@utoledo.edu Grover Waldrop Louisiana State University Dept of Biological Sciences 206 Life Sciences Building Baton Rouge LA 70803 USA gwaldro@lsu.edu John Wallace University of Adelaide Biochemistry Dept School of Molecular & Biomedical Science Adelaide 5005 AUSTRALIA john.wallace@adelaide.edu.au Patricia Wallace Novozymes Dalgleish Street Thebarton 5031 AUSTRALIA pat.wallace.au@gmail.com Christopher Walsh Harvard Medical School Dept of Biological Chemistry & Molelcular Pharmacology HIM 1046 Boston MA 2215 USA christopher_walsh@hms.harvard.edu Susan Wang Washington State University Molecular Biosciences BLS 202 PO Box 647520 Pullman WA 99164-7520 USA susan_wang@wsu.edu Kittikhun Wangkanont UW-Madison 1813 Keyes Ave Madison WI 53711 USA wangkanont@wisc.edu Douglas Weibel UW-Madison Biochemistry Dept 433 Babcock Drive Madison WI 53706 USA weibel@biochem.wisc.edu Darryl Wesener UW-Madison 433 Babcock Dr Room 461 Madison WI 53706 USA wesener@wisc.edu Karl Wetterhorn UW-Madison 433 Babcock Drive Madison WI 53706 USA wetterhorn@wisc.edu Valerie Winton UW-Madison Chemistry Department 410 N Paterson St Madison WI 53703 USA vwinton@chem.wisc.edu Sanford Wright Novartis Institutes for BioMedical Research 250 Massachusetts Ave Cambridge MA 2139 USA kirk.wright@novartis.com 130 36th Steenbock Symposium May 22nd – 24th, 2014 Symposium Participant Addresses Runhan Yu Brandeis University 60 Fiske Street Waltham MA 2451 USA yrh@brandeis.edu Tonya Zeczycki Brody School of Medicine 600 Moye Blvd Greenville NC 27834 USA zeczyckit@ecu.edu Jie Zhang University of New Mexico 300 Terrace St NE Albuquerque NM 87131 USA jzhang05@unm.edu Yan Zhang University of Texas-Austin 105 E 24th Street Welch Hall 4.260B Austin TX 78712 USA jzhang@cm.utexas.edu Wen Zhu Indiana University-Purdue University Indianapolis 402 N Blackford Street LD326 Indianapolis IN 46202 USA zhuwen@iupui.edu Lucas Zimney University of New Mexico 300 Terrace St NE Albuquerque NM 87131 USA lzimney@unm.edu Enzyme Structure and Function 131 132 36th Steenbock Symposium May 22nd – 24th, 2014 ... Main Lobby, 201 State Street Enzyme Structure and Function Enzyme Structure and Function 36th Steenbock Symposium University of Wisconsin – Madison in honor of W W Cleland Symposium Organizers Hazel... research interests focus on the structures and functions of enzymes involved in the biosynthesis of unusual di-, tri-, and tetradeoxysugars Enzyme Structure and Function 36th Steenbock Symposium... and the Medical Advisory Board of the Howard Hughes Medical Institute Rowena and her husband Larry have two grown children, Brian and Keith, and two grandchildren, Jennifer and David Enzyme Structure