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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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- 2 Crossref
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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
- Antimicrobial Effects of Herbal Extracts on Streptococcus mutans and Normal Oral Streptococci
- Sung-Hoon Lee
- J. Microbiol. 2013;51(4):484-489. Published online August 30, 2013
- DOI: https://doi.org/10.1007/s12275-013-3312-5
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- 18 Scopus
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Abstract
- Streptococcus mutans is associated with dental caries. A cariogenic biofilm, in particular, has been studied extensively for its role in the formation of dental caries. Herbal extracts such as Cudrania tricuspidata, Sophora flavescens, Ginkgo biloba, and Betula Schmidtii have been used as a folk remedy for treating diseases. The purpose of this study was to evaluate and compare the antibacterial activity of herbal extracts against normal oral streptococci, planktonic and biofilm of S. mutans. Streptococcus gordonii, Streptococcus oralis, Streptococcus salivarius, Streptococcus sanguinis, and S. mutans were cultivated with brain heart infusion broth and susceptibility assay for the herbal extracts was performed according to the protocol of Clinical and Laboratory Standard Institute. Also, S. mutans biofilm was formed on a polystyrene 12-well plate and 8-well chamber glass slip using BHI broth containing 2% sucrose and 1% mannose after conditioning the plate and the glass slip with unstimulated saliva. The biofilm was treated with the herbal extracts in various concentrations and inoculated on Mitis-Salivarius bacitracin agar plate for enumeration of viable S. mutans by counting colony forming units. Planktonic S. mutans showed susceptibility to all of the extracts and S. mutans biofilm exhibited the highest level of sensitivity for the extracts of S. flavescens. The normal oral streptococci exhibited a weak susceptibility in comparison to S. mutans. S. oralis, however, was resistant to all of the extracts. In conclusion, the extract of S. flavescens may be a potential candidate for prevention and management of dental caries.
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