xt7brv0cz72g https://exploreuk.uky.edu/dips/xt7brv0cz72g/data/mets.xml University of Kentucky University of Kentucky Chemistry Department 20070413 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 Thirty-Third Annual Symposium on Chemistry and Molecular Biology: "Enzyme Catalysis and Mechanisms" text Thirty-Third Annual Symposium on Chemistry and Molecular Biology: "Enzyme Catalysis and Mechanisms" 2007 2017 true xt7brv0cz72g section xt7brv0cz72g 1.. . ,, . -.. ... .... :- .' .- !. ~ ‘ . +1 .. . . 1.»; b- " “,w .. as .". . 3,: 1- . Ur! .'>‘u ‘ ‘w .: ;,",‘r ,w‘ ' .‘x' wit.“ ." V” 1,: ‘-,- ;.. a mm '.'171',!- 1-..1 'fr'. "1 f uni“: t’,‘:,, ~ ’ ‘{ ,.‘, " 1‘” ‘m’mja- :1“ ‘2',“ "~
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8:30 am. Registration and Continental Breakfast, of enzymatic transition states are not yet possible. Transition 4"; J Naff SympOSlum on fr}:- ﬁ 11;: .
Singletary Center for the Arts state structure can be probed by kinetic isotope effects cou— if.» {’32}; 1 ; :3"?
pled to quantum chemical structures of proposed transition 1,171.911 _ 2 $5.75", '_'j;.f-,,z-“:1;

9:10 am. Welcome by Dr. Charles A. Staben, Associate states. An accurate transition state structure provides a blue- {27; C hem lstry ': L"

VP for Research, University of Kentucky - print for the design of transition state analogues. Chemically 1-‘~T"ﬁfi‘m;.’..j ; 1,3} ,;f;,j:;
Singletary Center for the Arts, Recital Hall stable mimics of enzymatic transition states convert the en- 53:31:14)} - 1 ’1'?ng . fir-'11. 1 ‘

ergy of catalysis into binding energy. Thus, transition state 71’ ﬁg; 2:14;}: 1 & i133, _ ‘.3 ‘3‘

9:20 am. Introductory Remarks - Dr. Steven W. Yates, analogues have the potential to bind to target enzymes mil- View, 7'51 igéligxl‘fﬁ31; _ 3;
Chairman, Department of Chemistry, Univer— lions of times more tightly than the substrates. Our drug de- ﬁfe; 5:51 M lecu la r A? "15%;

sity of Kentucky sign program, bUIlt around tranSItlon state theory, is now pro- '~. L, 1354" 2.21;; O 1?»,“22142; ”41:.

ducing powerful transition state analogues for several targets 1‘51“; _ "5'! i" -'

9:30 am. Dr. John A. Gerlt, University of Illinois at Ur- with promise for treatment of T-cell leukemia, B-cell leukemia, wait; if; BIOIOgy i' ".1 .1 , 5:351...

bana-Champaign autoimmune diseases, prostate cancer, head and neck can— a???” g k“,

"Discovering and Predicting New Enzymes in cer, and malaria. Bacterial antibiotics are also being devel- - “1“, {i3igg;sg;“: ,

the Enolase Superfamily" oped in this program. Two compounds, Immucillin-H and ,,L~<“;-E~;;f 2;", ”as“‘,j

, _ _ DADMe-lmmucillin-H are in clinical trials for leukemia and :L‘,j:}.§wt<“-ei . it ”*1“!

Many members of the mechanlstlcally diverse enolase autoimmune diseases. ;,.;' . 1! . ,1 . .1 j, 3%
superfamily have unknown functions. We are using two 1‘1‘.3~.,‘c;f"-=,~ ' / 5%,; “1:,
strategies to assign them: 1) experimental screening of librar— 2:40 pm. Break (Refreshments Available) , 4:..1117? A: ,. , "’f 1733;,
ies of potential substrates, and 2) in silico prediction using 521.3:129'1': ,_ 1;; ’ 5 >6;
homology models and docking of libraries of potential sub- 3:00 pm. Dr. JoAnne Stubbe, Massachusetts Institute of a‘.~f_§:‘“ ,- " 1 i. _- 1‘ 4: Us
strates. Using the ﬁrst strategy, we recently published the Technology l . g :7;
assignments of L—fuconate dehydratase and D-tartrate dehy- "Unnatural Amino Acids: Tools to Investigate - .,‘ . ' 1'5 . ‘ .1 ' {R1131};

dratase functions. We now have discovered that members of Radical Propagation in Class I Ribonucleotide x59: :31; ‘f i_ ‘5. , ‘. 'f =3

another orthologous group catalyze the dehydration of both Reductase" Raf-1'23 : ‘71., 1:5; '. :12; '4':
galactarate and L-talarate as well as their interconversion by . . %"tﬁ=“ as '55“ inf; .
epimerization. Using the in silico strategy, we predicted that R'POWC'BOt'de reductases (RNRS) _ catalyze the, thus ,3“ 31 established in the memory of ‘ 5:41“:
members of a divergent orthologous group would catalyze the conversmn 0? nucleotides t0 deoxynucleotldes In all organisms 37.12;}? g _,;,.”3-3 A S N ff 2’} a {Hat
racemization of N—succinyl Arg and N-succinyl Lys. We ex- Plat/"19 an essential role In DNA replication and repair. Class I .1’ 33.1.3972; 1 nna ' a 11:...1121 55‘1“};[5
perimentally veriﬁed these predictions and solved the structure RNRS are composed 0f tW0 homodimeric subunits: R1 (0(2) «1- vr‘s 5» "‘ _'~:’;s;.‘:;

of this N-succinylamino acid racemase. The predicted and and R2(BZ). R2 contains the di—iron tyrosyl radical (Y-) ‘_<-”:s.‘....,';‘;s.-.1 21.:1—___.— .ri;j".1.‘:"j-‘::l’55. 1.}!
experimental structures of liganded complexes are in excellent cofactor essential for activity. R1 contains the active site . 2.. 7:3ng Enzyme Catalysis and £3 .*=' _'
agreement. Thus, computational approaches provide a viable Where nucleotide reduction Occurs. An unresolved EC ‘ _ 1 . .s;
strategy for successfully assigning function to members of the mechanistic issue is how the Y' in R2 generates a transient Ln : :1 s 4;: MGChan'sms £15 . {if
enolase superfamiliy as well as other enzymes discovered in thiyl radical on R1 to initiate the reduction process. This as 8 1%,; jig—w it; 1-,. 1;" -.',
genome projects. Supported by GM-71790. initiation is thought to occur over a 35 A distance and involve 46)- > Q ".j ,,.f 2,1 ‘, E 5;: ‘1 53

_ generation of aromatic amino acid radical intermediates. g x (CI) in; 1;» SPEAKERS 41f I 51-:;;.-;.;;

10140 a.m. Break (Refreshments Available) Experiments using unnatural amino acids ((F)n—tyrosines (n = (D g o ligjﬁiﬁl if 1.7: 7??

. _ 2, 3, 4), 3-hydroxytyrosine, nitrotyrosine, and benzophenone) _c 4.. 8 3117;}?TT'T511 Si.ve‘;151.1j-j=»':'

11:00 am. Poster Session, Room CP-137, Chemistry- in position 356 of R2 have been carried out. These studies 0 g q— “j: 51",“ John A Ger” 1: 711,6?"1"‘i;.3‘::z~.‘=f£
PhYSICS 3“”de provide direct evidence for interrnediacy of a Y356- on the “5 :C >_ ,1: 5 ' .{g

_ propagation pathway. We have recently been able to place ,,_, B x ;:‘.j"v"~j;5;;,.;. .21.; Vern L. Schramm .15., V;;.‘,-,<1,7-1;_;.:§

17-300 P-m- Buffet Lunch, Alumni Rouse [Please return unnatural amino acids in the R1 subunit. These studies have C — it! xi} JoAnne Stubbe fies; 15“”? ‘
registration card by April 6, 2007 for reserva- demonstrated the importance of Y730 and Y731 within R1 for GE) 3? g ﬂame"? 1 154 -., . 33.2: if

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1330 P-m- Dr. VernL. Schramm, Albert Einstein College direct evidence for hole migration through amino acid radical 3 E '>_< "ﬁﬁé‘i'g, Friday, Apr" 13’ 2007 g}: ‘C: 543,7 '31:.

0f Medlcrne intermediates over a long distance. D 3 3 _‘tl€_i:f.‘ti}:l, . ,3’ at; ;.:}j<',f;—;3'7

"Drugs for Cancer and Malaria from Transition 9’3. . Vii-’1 1.1:; f" :31?) >-

State Analysis" 4:10 pm. Closing Remarks - Dr. Anne-Frances Miller, . 71 2.75.1.7. .2, - 17's.” -. 'vﬁfiﬁ’iié

. _ _ _ .. Department of Chemistry, University of Ken- 3 -‘Lv;.lg,ji.'~~.i.- ‘1' Department Of ChemIStry : -3

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Enzyme Catalysrs and Mechanisms 3,,
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é 2.“ ”3” '2 5 John A. Gerlt, Gutgsell Chair, Professor of Biochemistry, Professor of Chemistry and Biophysics, Uni- {,43352' 4,227.35
Z 41,1455" 5‘ ; versity of Illinois at Urbana-Champaign. Dr. Gerlt was born in Sycamore, IL. He received his BS. from Michi- 13,53}, -311,
3 ”5 ‘ ,. gan State University in 1969 and his Ph.D. from Harvard University in 1974. After holding a Jane Coffin Childs ' .1595, ““53;
5 csmﬁe‘é Memorial Fund Fellowship at the NIH, he held faculty positions at Yale University and the University of Maryland ”2;, 23.33%-
34* 25,“ before moving to the University of Illinois, Urbana-Champaign where he is Professor of Chemistry and of Bio- '.,’,;~L,{’._*’ 53.3“?“
I- 55 , “ 4, chemistry, and Gutgsell Chair. Prof. Gerlt has held a Research Career Development Award, an Alfred P. Sloan 2;: .33
W -5: Foundation Fellowship, a Sigma Xi Award for Contribution to Science, and the Repligen Corporation Award in 5g] g
E ‘5‘, Chemistry of Biological Processes. He has served as Co-Chair for the Gordon Research Conference on En-
t w ‘ zymes, Coenzymes, and Metabolic Pathways, a member of NIH’s Physical Biochemistry Study Section, and is “5" 2;,
‘ currently Associate Editor of Biochemistry. Prof. Gerlt’s research interests are in mechanistic enzymology. He 3253*? 2-‘22-342'
- a infers the strategies by which Nature can redesign existing enzymes to catalyze diverse reactions, based on 5 234?:
,: analyses of complete genome DNA sequences, enzyme kinetics, and physical organic chemistry. The Gerlt lab ‘3“ ,5“ .52, '-
3 studies three groups of enzymes that diverged from a common ancestor, but catalyze different reactions. Members of the enolase super- géﬂl‘? ,, _.
family share the ubiquitous ﬁlo-barrel fold and a conserved binding site for an essential divalent metal ion that stabilizes an enolate anion 7‘ {”5“ if
F intermediate. Based on this, the Gerlt group has predicted the functions of unknown proteins discovered in genome projects. Members J‘fﬁﬁ”;
E of the crotonase superfamily share an o. + [5 fold that provides a conserved oxyanion hole used to stabilize enolate anion intermediates. v; :2 *5 l
, The positions of the essential functional groups in this superfamily cannot be predicted within the structure. Therefore, the Gerlt group 533.325.
33 studies diverse members of this superfamily to delineate the structural basis for catalytic diversity. Thus, comparison of the mechanisms ”xx- “$5
.34 of dihydroxynaphthoyl CoA synthase and 2-ketocyclohexanecarboxyl CoA hydrolase, better deﬁnes the mechanisms of both reactions. W 4 “(ff-5'5;
3 Members of the orotidine 5'-phosphate decarboxylase “suprafamily” also share the B/a-barrel fold. However, in contrast to the enolase “j “53%“
a superfamily, these enzymes use consen/ed functional groups to catalyze reactions involving distinct mechanisms. Prof. Gerlt’s compari- £,%‘3,3
,‘ son of enzymes that catalyze aldol and B-ketoacid decarboxylation reactions seeks to better understand this mechanistic plasticity, which 25% 4
may be exploited in the design of new enzymes. j. {53512132.
. .2: _ 3 W353"??? Vern L. Schramm, Professor and Chair, Department of Biochemistry, Albert Einstein College of Medi- 2 $1223., ff
3; '25:;252 .5 cine. A native of South Dakota, Dr. Schramm earned his bachelor’s degree from South Dakota State Col- 3...; 32;,”
.3 . €313: ,. 5355f“. lege, a Master‘s degree from Harvard University and a Ph.D. in the mechanism of enzyme action from the §”-’,,:.2i;§{.2§;§?521f
5 M . 3 Australian National University. Upon returning to the United States, Dr. Schramm served as a NSF-NRC £433.52
3 9.5;“?42‘1‘“ f5; {#3,}, a" - Postdoctoral Fellow at the NASA Ames Research Center. He joined the faculty of the Temple University 212-5": 3%";
3 27:3 J'Hvi‘g‘e. 5,, School of Medicine in 1971 and started his life-long research into the nature of enzymatic transition state .45.},“23;
3:3 I .{i 2.127; structure. In 1987, he moved to New York to become Professor and Chair of Biochemistry at Einstein. He 52‘; News
g ’ ‘t , ,3.- - it; was appointed to the Ruth Merns Chair of Biochemistry in 1995. At Einstein, his research on transition state ‘53,, gym-w-
jg _ $2,235- structure has been extended to become a powerful method for drug design. Dr. Schramm is world-renowned ,3. 1‘" 3...”;
3 3; 4 . . for his research into the “transition-state structure" of enzyme-catalyzed reactions -- the shapes that reacting gﬂiéﬁﬁs‘.’
3 2’3". i, , «235 molecules assume at the instant of enzyme—catalyzed bond changes. The transition-state structures of en- 321 3’, ‘ 5 2i
i 2 ~55: ‘22 2 zyme-catalyzed reactions, provide a blueprint for the design of powerful inhibitors to be used as drugs or Q??? . -3;;
. antibiotics. Two of the inhibitors designed by the Schramm laboratory have entered clinical trials. One shows promise for treating Ieuke- “4-252, ’51,,233',
2 mias that do not respond to other therapy. The second is in clinical trials for development as an agent to treat or prevent autoimmune #3
diseases. These include psoriasis, rheumatoid arthritis. multiple sclerosis, inflammatory bowel disorders, insulin-dependent diabetes and W.}r’f:%a€;“~.
2 tissue transplant rejection. New agents are being explored for malaria, solid tumors and as bacterial antibiotics. Dr. Schramm has pub- 3&3;
Iished over 200 articles and received numerous honors in recognition of his contributions to both research and teaching in biochemistry Naif-5K5,
and enzymology. These include a Merit Research Award from the General Medical Institute of the NIH for work on transition state struc— (4,3,,
ture, the Repligen Award from the American Chemical Society, election as a Fellow of the American Association for the Advancement of 523.3"; \
5 Science, the Rudi Lemberg Award from the Australian Academy of Science, election to the Davidoff Society at Einstein, the George A. “£351;
- Sowell Award for Excellence in Teaching from Temple University School of Medicine, and the Harry Eagle Award for Outstanding Basic .ji'jiS-SFW‘L“,
a Science Teaching from the Albert Einstein College of Medicine. Dr. Schramm has served as the Chair of the Division of Biological Chem- :5‘1’232
istry of the American Chemical Society and is an Associate Editor of the Journal of the American Chemical Society. He serves as a scien- ': {$23.53* 352.,"
5'3 tific advisor to national research resources and several biotechnology companies. ’W;%
; -...-"‘=2;-:': 35 JoAnne Stubbe, Novartis Professor of Chemistry and Biology, Massachusetts Institute of Technology. A ﬁg? ,3; “5-,; ,3
“(3‘ 2 native of Champaign, IL, Prof. Stubbe received her BA. in chemistry from the University of Pennsylvania and her ‘82,, ,,.5,,;‘~._
, , 5 . Ph.D. from the University of California, Berkeley. She pursued postdoctoral research at the University of California, $17.,"
3 E, I“ 3" Los Angeles and has held faculty appointments at Williams College, Yale University Medical School, the University 3555‘;W4,,,;”2
:‘5 . .2 2’73":- _- - of Wisconsin, Madison (Professor and Romnes Fellow) and the Massachusetts Institute of Technology as the Ellen 33.33" “2‘32
5} ‘2 3W ‘ .3;) 2‘ Swallow Richards Professor of Chemistry, where she is now the Novartis Professor of Chemistry and Biology. Prof. 21.353223373513755
f3 5 _ -... . _ ; Stubbe’s lab uses chemical methods to understand biological processes. Current activity focuses on four major ‘6; $5.212 3.".
2 _ ‘ "' ",2 a'reas’."Th‘e‘ Stubbe grbup'is’elucidatmg the mechanisms of the three classes of rIbonucIeotide reductases. The .. A 'g2‘;2*
2}? ' group also seeks to understand how the purine biosynthetic pathway may have evolved, and is modulated. Prof. ¥g&\;‘£§3 3
.5 ’ Stubbe seeks to understand the mechanisms of DNA cleavage by antitumor agents, including elucidation of the . 392.493.5253“,
g ‘ “‘32,, structures of the deoxyribose lesions that result, and mechanisms by which they are repaired. Finally, the Stubbe 5532}, ”24,431,321";
2 ‘ group is working towards engineering and understanding polyester biosynthesis, by bacteria, with the objective of “,ﬁ’ .12;
being able to produce bio-renewable sources of biodegradable polymers with properties of thermoplastics. Professor Stubbe has been a .2 $51.5 2 ”32,35.
3‘ recipient of numerous awards including an NIH Career Development Award, the H. I. Romnes Fellowship, the Pfizer Award in Enzyme “U .5532,
9 Chemistry, the ICI-Stuart Pharmaceutical Award for Excellence in Chemistry, the MIT Graduate Student Council Teaching Award, the (1 3.553352 5555355
Arthur C. Cope Scholar Award, the Richards Medal from the Northeast Section of the ACS, the Cotton Medal, the Alfred Bader Award in 2;? f} :‘-,2,;é;~;§:2.,,;
Bioorganic and Bioinorganic Chemistry, the Repligen Award, the American Philosophical Society Award and the John Scott Award. She 2“ .,xv-"-4_.,2'.2. 3359115371
was elected to the American Academy of Arts and Sciences in 1991 and the National Academy of Sciences in 1992. She has served on f’ywﬁgek"
the Editorial Advisory Boards of Biochemistry, J. Am. Chem. Soc, Chemical Reviews, and Proceedings of the National Academy of Sci- 3.52:9" @333;
3 ences, among others. She has also served on NIH study sections, ACS divisional committees and on the World Health Organization "2.153.512“ 3555
‘- (CHEMAL) Committee. She has been organizer of the Gordon Conference on Amino Acid Radicals, and organized the 19th Enzymes 3,5555%?! ‘2".
,. Mechanisms Conference. She has served on numerous advisory boards including the Advisory Committee for Chemistry of the National "-12 “$2,323... .i'
3, Science Foundation. She is author or co-author of over 230 articles in professional and scholarly journals and presents lectures to 5332"»; ,. 5-" ’3»,
i packed halls world—wide. wgi’qu
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FREE PARKING is available in Parking Structure #5 at 409 South Limestone Street (entrances on South Limestone £9 _
' and Upper Street). For additional information, e-mail Professor Anne-Frances Miller, Department of Chemistry, #935,?
5 (afm@uky.edu). ‘ﬁﬁé‘ffw'
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t 2007 Committee: Anne-Frances Miller, Chair (Chemistry), Bert C. Lynn, (Chemistry), David W. Rodgers (Biochemistry) §“%€%
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Symposrum supported by the Anna S. Naff Endowment Fund @ﬁ‘ﬁi
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(additional support provided by the Office of the Vice President for Research, University of Kentucky) 2'_ ﬁﬁiékj
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