Crystal structure of prephenate dehydrogenase from Streptococcus mutans |
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Authors: | Ku Hyung-Keun Do Nam Hyuk Song Jin Sue Choi Saehae Yeon Seung Hoon Shin Min Hyung Kim Kyung-Jin Park Sang-Ryoul Park Il-young Kim Sook-Kyung Lee Soo Jae |
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Institution: | a Division of Metrology for Quality of Life, Center for Bioanalysis, Korea Research Institute of Standards and Science, Department of Bio-Analytical Science, University of Science & Technology, Daejeon 305-340, Republic of Korea b College of Pharmacy, Chungbuk National University, Gaeshin-dong, Heungduk-gu, Cheongju City, Chungbuk, Republic of Korea c Pohang Accelerator Laboratory, Pohang University of Science and Technology, San31, Hyoja-Dong, Nam-Gu, Pohang, Kyungbuk 790-784, Republic of Korea |
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Abstract: | Prephenate dehydrogenase (PDH) is a bacterial enzyme that catalyzes conversion of prephenate to 4-hydroxyphenylpyruvate through the oxidative decarboxylation pathway for tyrosine biosynthesis. This enzymatic pathway exists in prokaryotes but is absent in mammals, indicating that it is a potential target for the development of new antibiotics. The crystal structure of PDH from Streptococcus mutans in a complex with NAD+ shows that the enzyme exists as a homo-dimer, each monomer consisting of two domains, a modified nucleotide binding N-terminal domain and a helical prephenate C-terminal binding domain. The latter is the dimerization domain. A structural comparison of PDHs from mesophilic S. mutans and thermophilic Aquifex aeolicus showed differences in the long loop between β6 and β7, which may be a reason for the high Km values of PDH from Streptococcus mutans. |
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Keywords: | Prephenate dehydrogenase Streptococcus mutans Crystal structure |
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