Title X-ray Structure of Prephenate Dehydratase from Streptococcus mutans
Author Min Hyung Shin1, Hyung-Keun Ku2, Jin Sue Song1, Saehae Choi1, Se Young Son1, Hee-Dai Kim3, Sook-Kyung Kim2, Il Yeong Park1*, and Soo Jae Lee1*
Address 1College of Pharmacy, Chungbuk National University, Chungbuk 361-763, Republic of Korea, 2Division of Metrology for Quality of Life, Center for Bioanalysis, Korea Research Institute of Standards and Science, Department of Bio-Analytical Science, University of Science and Technology, Daejeon 305-340, Republic of Korea, 3Department of Biotechnology and Bioinformatics, Chungbuk Provincial College, Chungbuk 373-806, Republic of Korea
Bibliography Journal of Microbiology, 52(6),490-495, 2014,
DOI 10.1007/s12275-014-3645-8
Key Words prephenate dehydratase, X-ray structure, S. mutans
Abstract Prephenate dehydratase is a key enzyme of the biosynthesis of L-phenylalanine in the organisms that utilize shikimate pathway. Since this enzymatic pathway does not exist in mammals, prephenate dehydratase can provide a new drug targets for antibiotics or herbicide. Prephenate dehydratase is an allosteric enzyme regulated by its end product. The enzyme composed of two domains, catalytic PDT domain located near the N-terminal and regulatory ACT domain located near the C-terminal. The allosteric enzyme is suggested to have two different conformations. When the regulatory molecule, phenylalanine, is not bound to its ACT domain, the catalytic site of PDT domain maintain open (active) state conformation as Sa-PDT structure. And the open state of its catalytic site become closed (allosterically inhibited) state if the regulatory molecule is bound to its ACT domain as Ct-PDT structure. However, the X-ray structure of prephenate dehydratase from Streptococcus mutans (Sm-PDT) shows that the catalytic site of Sm-PDT has closed state conformation without phenylalanine molecule bound to its regulatory site. The structure suggests a possibility that the binding of phenylalanine in its regulatory site may not be the only prerequisite for the closed state conformation of Sm-PDT.