Journal of Microbiology

Jin Sue Song

2 Articles

X-ray Structure of Prephenate Dehydratase from Streptococcus mutans: Min Hyung Shin , Hyung-Keun Ku , Jin Sue Song , Saehae Choi , Se Young Son , Hee-Dai Kim , Sook-Kyung Kim , Il Yeong Park , Soo Jae Lee; J. Microbiol. 2014;52(6):536-536.; DOI: https://doi.org/10.1007/s12275-014-0701-3

481 View
1 Download

Abstract PDF: In the article by Shin et al. published in Journal of Microbiology 2014; 52, 490-495. Hyo-Jin Yang was omitted as the 6th author of this paper. The authors should be Min Hyung Shin1, Hyung-Keun Ku2, Jin Sue Song1, Saehae Choi1, Se Young Son1, Hyo-Jin Yang2, Hee-Dai Kim3, Sook-Kyung Kim2, Il Yeong Park1*, and Soo Jae Lee1*

X-ray Structure of Prephenate Dehydratase from Streptococcus mutans: Min Hyung Shin , Hyung-Keun Ku , Jin Sue Song , Saehae Choi , Se Young Son , Hee-Dai Kim , Sook-Kyung Kim , Il Yeong Park , Soo Jae Lee; J. Microbiol. 2014;52(6):490-495. Published online March 7, 2014; DOI: https://doi.org/10.1007/s12275-014-3645-8

899 View
1 Download
3 Crossref

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.

Citations

Citations to this article as recorded by

Evaluation of safety and efficacy of an auxotrophic aroA mutant live attenuated vaccine against piscine Streptococcus agalactiae infection
Meng Nie, Changming Guo, Yuhao Dong, Ting Xu, Yaru Sun, Yongjie Liu
npj Vaccines.2026;[Epub] CrossRef
Computational investigations of allostery in aromatic amino acid biosynthetic enzymes
Wanting Jiao
Biochemical Society Transactions.2021; 49(1): 415. CrossRef
Feedback inhibition of the prephenate dehydratase from Saccharomyces cerevisiae and its mutation in huangjiu (Chinese rice wine) yeast
Shuangping Liu, Qilin Yang, Jieqi Mao, Mei Bai, Jiandi Zhou, Xiao Han, Jian Mao
LWT.2020; 133: 110040. CrossRef

Author index