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- 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
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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.
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- 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
- Computational investigations of allostery in aromatic amino acid biosynthetic enzymes
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