xt7m0c4sn340 https://exploreuk.uky.edu/dips/xt7m0c4sn340/data/mets.xml University of Kentucky University of Kentucky Chemistry Department 19780331 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 Fourth Annual Symposium on Chemistry and Molecular Biology: "Regulation of Enzyme Activity" text Fourth Annual Symposium on Chemistry and Molecular Biology: "Regulation of Enzyme Activity" 1978 2017 true xt7m0c4sn340 section xt7m0c4sn340 I" C D e 2. e 5' 5 2 Fourth Annual Symposium on 8:30 Coffee-CP Room 137 0'3 3 S 0 5' 9:00 Welcome and Introduction — CP Room 139 .5 ‘3 g 7§ -h 0 9:15 INTRODUCTION-REGULATION OF ENZYME .< 5 3 ACTIVITY 4; a g — Dr. W. N. Lipscomb — 8 g 3 C) 7? —° 9:30 INDUCED FIT AND ALLOSTERIC INTERAC- 0“< 5* c H E M I S T R Y TIONS IN THE STRUCTURE AND FUNCTION OF YEAST HEXOKINASE a n d — Dr.T. A. Steitz — High resolution structures of monomeric and dimeric M O L E C U L A R yeast hexokinase and their substrate complexes pro- vide important clues to the specificity and mechanism of this kinase and suggest models for its activation. B I O L o G Y The binding of glucose results in a dramatic structural change; one domain of the monomer (40% of the atoms) rotates 12° relative to the other domain, there- by closing off the deep cleft into which the sugar established in memory Of binds. The energy for this induced fit mechanism of _ enzyme specificity comes from a change in the molec- ANNA 5‘ NAFF ular surface area. The subunits of the dimer associate in an asymmetric fashion forming a unique activator binding site between the subunits. 10:30 Discussion and Coffee Break 10:45 ASPARTATE TRANSCARBAMYLASE, AN EX- Regulation Of Enzyme AMPLE OF ENZYME REGULATION A t. .t — Dr. w. N. Lipscomb— C ’V’ Y From two three-dimensional structures at 3 A resolu- tion, and from a large body of biochemical data, some remarks can be made about the assembly, the active site and the regulatory processes in the allosteric en- zyme, aspartate transcarbamylase. The enzyme C6R6 S eakers has six catalytic polypeptide chains (C) and six regula- p tory chains (R) in 03 symmetry. A Zn site of the Professor William N. Lipscomb regulatory chain shows four cysteines as ligands, just Professor Thomas A. Steitz at the boundary between C and R chains. Cytidine triphosphate, the allosteric inhibitor, is located on the R chain some 40 A from the catalytic site. Progress toward a three-dimensional structure in which a sub- strate analogue is bound will also be described. Kinet- ics for a fragment C6 R4 indicate that about half of the 2 MARCH 3] I 1978 inhibition by cytidine triphosphate remains, in some 5 % disagreement with a symmetry model but supporting a Fr" >_< +1 . :0 z 2: sequential model for regulatory processes. The ques- 5 a? a 9 tion of the minimum structure required for regulation '4 (2 > ‘T’ 3 will be discussed in terms of the three-dimensional 5 _g 70:, x-ray diffraction results. ; 5 S: Q . . . E 3. U9, Z Department of Chemistry 11.45 DISCUSSIon g E E University of Kentucky '< 9 Lexington, Kentucky 40506 F th A I S ' Ch ' t d M I I B' I established in memory of Anna S. No” March 31,1978, 9:00 a.m.-12:OO noon Room 139 Chemistry—Physics Building Department of Chemistry University of Kentucky Lexington, Kentucky 40506 Regulation of Enzyme Activity SPEAKERS Professor William N. Lipscomb Gibbs Chemical Laboratory, Harvard University, Nobel Laureate in Chemistry in 1976 “Aspartate Transcarbamylase, an Example of Enzyme Regulation” Professor Thomas A. Steitz Department of Molecular Biophysics and Biochemistry, Yale University “Induced Fit and Allosteric interactions in the Structure and Function of Yeast Hexokinase” The Symposium is supported by the Anna S. Naff Endowment Fund with the assistance of the University of Kentucky Graduate School. For additional information, please contact Professor Donald E. Sands at the Department of Chemistry; phone (606) 258—5823 or 258-5904. Parking will be available at Commonwealth Stadium on Cooper Drive. Shuttle buses run to the main campus. Your cooperation is requested in not smoking during the Symposium. .