xt7wdb7vqj75 https://exploreuk.uky.edu/dips/xt7wdb7vqj75/data/mets.xml University of Kentucky University of Kentucky Chemistry Department 19930405 A brochure for the Naff Symposium, an event hosted by the University of Kentucky Chemistry Department supported by the Anna S. Naff Endowment Fund. This brochure belongs to the University of Kentucky Chemistry Department Records collection, accession number 2014ua075. archival material  English University of Kentucky Chemistry Department Contact the Special Collections Research Center for information regarding rights and use of this collection. University of Kentucky Chemistry Department Naff Symposium brochures Nineteenth Annual Symposium on Chemistry and Molecular Biology: "Enzyme Catalysis - Mechanism, Structure and Design" text Nineteenth Annual Symposium on Chemistry and Molecular Biology: "Enzyme Catalysis - Mechanism, Structure and Design" 1993 2017 true xt7wdb7vqj75 section xt7wdb7vqj75 _—’— '— ~ “— .
1993 PROGRAM Nineteenth Annual
Symposium on
A.M. P.M. C] O t
9:00 Registration and Coffee - Room 137, 12:15 Buffet Lunch. Faculty Club. (Please return 6 mls I S
Chemistry-Physics Building card by April 1. 1993 for reservations. Cost
$8.00 to be paid at registration.) &
9:30 Welcome by Dr. Lee Magid, Vice President
for Research and Graduate Studies, 1:40 Dr. Perry A. Frey, University of Wisconsin-
University of Kentucky - Room 139. Madison
Chemistry-Physics Building Substrate Binding and Catalysis by UDP- o 6 cu ar
Galactose 4-Epimerase
9:40 Introductory Remarks - Tina Amyes, 0
University of Kentucky The most important problem in mechanistic enzy— B10 0
mology is the elucidation of how enzymes use the sub-
9:45 Dr. William P. Jencks, Brandeis University strate binding process to enhance the rates of reactions.
Sources of the Catalytic Activity oszymes The question of how UDP-galactose 4—epimerase uses
binding interactions to nonreacting portions ot'the sub— ,
Enzymes have the ability to increase reaction rates strate to catalyze hydride transfer from the substrate to
by factors of 10” or more for their specific substrates. A the cofactor. NAD, will be presented. The results of
small fraction of this catalysis can usually be accounted kinetic measurements. NMR and Raman spectroscopy. V, , . ,1 .,
for by well—understood chemistry. such as nucleophilic and x—ray ciystallography will be fused into a coherent f“ , ' ‘ .
catalysis and acid or base catalysis by proton donors and hypothesis that explains how the enzyme uses binding . ,‘ .. '15“ J ,
acceptors at the active site.The source ofthegreaterpart interactions to the uridine 5'—diphosphoryl moiety of ,‘ .
of the observed catalysis is obscure. but it is clear that substrates to enhance the intrinsic. chemical reactivity of ' ' g " .
much of this catalysis arises from noncovalent interac- NAD at the active site. The simplest interpretation ofthe _ / _
tions 'of the substratets) with the active site. Strain, resultswillbeshown to indicate that the enzyme reduces ' ' '
distortion and desolvation in the enzyme—substratecom— the energy of activation for hydn‘de transfer in part by
plex can decrease the activation energy for reaction but electronically destabilizing the nicotinamide ring ofNAD. _ .
require the expenditure of a large amount of binding established In the memory Of
energy. Attraction ofourlimited knowledge ofthe mecha-~ 2:40 Discussion Anna S. Naff
nisnis 01 how catalySis of chemical reactions and oi
movement is mediated will be reviewed. 2:50 Dr. Gregory A. Petsko, Brandeis University
The Structural Enzymology of Proton- '
10:45 Discussion Transfer Reactions ENZYME CATALYSIS -
10:55 Dr. Stephen J. Benkovic. The Pennsylvania The simplest chemical transformations in inetabo- MEC SM’ S RUC U
State University . lisni are the proton transfer reactions exemplified by LG AND DESIGN
Catalytic Antibodies certain isomerases and racemases. We have been study- 3‘ in
mg three such enzymes to understand the structural +03) 8
The field of catalytic antibodies continues to envelop features that lead to efficient proton transfer All ofthese a g ('0
different reaction types and with particularemphasis on enzymes face the common problem of abstracting a a) :5 O SPEAKERS
the. stereochemical-controlof the course of thereaction: hydrogen from a carbon acid ofhigh pKJ with an enzymic 5 E 8 Stephen J, BCI’lkOViC
I Will locus on two issues: 1] the mechanism of action ol base of low pK". We have used X-ray crystallography. ‘H QM) sf
several ofthese antibodies and ii) methods for improving site—directed mutagenesis. and moleculardynamics simu- 0 2H E P61 I 5’ A- Frey
their catalytic efficiency. Mechanistic analysis based on lations to arrive at a set ofprinciples for optimal catalysis E5 0 ' William P. Jencks
structure rcactivity correlations, pre— and steady—state of this simple reaction. 0) 3‘ c: .
kinetics. and other reaction probes suggests that the E E 8 Gregory A' PCtSkO
most effective antibodies possess segments of the cata— 3:50 Discussion 3 g ED
lytic processes found in enzymes. Efforts to further Q 'F‘ 52 .
improve upon the active site framework or to integrate 4:00 Mixer - Room 137. Chemistry-Physics a 5 3 Monday Aprll 5’ 1993
additional functions into the antibody binding site through Building
mutagenesis and combinatorial libraries will be de— .
scribed E Department of Chemistry
University of Kentucky
”‘55 D‘5°“55‘°“ Lexington, Kentucky 40506—0055

 O O
Nrneteenth Annual Symposrum on
Chemistr y &
Molecular Biology
established in the memory of Anna S. Naff
Monday Apr11 5, 1993 9:00 am.
Room 1 39, Chem1stry—Phys1cs Buildmg
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William P. Jencks, Gyula and Katica Tauber Chair in perry A, Frey, Professor of Biochemistry and Co-
BiochemistryandMolecularPharmacodynamics.Brandeis director, Institute for Enzyme Research, University of
University. M.D. Harvard Medical School: Postdoctoral Fel- . Wisconsin-Madison. PhD. Brandeis University; Postdoctoral
low, Harvard University. American Chemical Society Award in Fellow. Harvard University. NIH Postdoctoral Fellow: Ashland
Biological Chemistry; National Academy ofSciences; Foreign Oil Foundation Professorship; Merit Award. National Insti—
Fellow of the Royal Society; American Society of Biological tute of Diabetes and Digestive and Kidney Diseases. Chair,
Chemists Award. Current Advisory Boards: Critical Reviews Division of Biological Chemistry, American Chemical Society.
in Biochemistry and MolecularBiology:Bioorganic Chemistry: Associate Editor: Biochemistry. Editorial Board: Bioorganic
Publications Committee. American Chemical Society. Chemistry.

J . , Q ..
. t Z “ .,

Stephen J. Benkovic, Evan Pugh Professor and Eberly Gregory A. Petsko, Lucille P. Markey Professor of
Chair in Chemistry, The Pennsylvania State University. Biochemistry and Chemistry, Brandeis University. D.Phil.
Ph.D. Cornell University; Postdoctoral Fellow, University of Oxford University. England (Rhodes Scholarship). European
California at Santa Barbara. Alfred P. Sloan Fellow; Pfizer Molecular Biology Organization Short—Term Fellowship to the
Enzyme Award; NationalAcademy of Sciences; Arthur C. Cope Institut de Biologie Physico—Chimique (Paris, France]. Alfred
Scholar Award; NIH Merit Award; Repligen Award, Current P. Sloan Foundation Fellowship; Siddhu Award, American
Advisory Boards include: Bioorganic Chemistry; Biochemistry: Crystallographic Association; Pfizer Award in Enzyme Chem—
Science:Accounts of ChemicalResearch: Protein Science: Jour— istry: Alexander von Humboldt Senior Scientist Award: Max
nal of Medicinal Chemistry: Current Biology. Planck Prize [shared with Professor R. Goody].

Parking available free at Commonwealth Stadium on Cooper Drive. Shuttle buses run to the main campus. Additional parking (for a fee} available
in UK Medical Plaza Parking Garage, located approximately one block south of the Chemistry—Physics Building: this garage can be accessed from
both Rose and Limestone Streets — look for Medical Plaza Parking signs, For additional information. call Tina Amyes. Department of Chemistry,
[606) 257-1411.
1993 Committee: Tina L. Amyes (ChaiITnanl. Louis B. Hersh, John P. Richard, Joseph W. Wilson
Symposium supported by the Anna S. Naff Endowment Fund