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.
Original language | English |
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Pages (from-to) | 761-766 |
Number of pages | 6 |
Journal | International Journal of Biological Macromolecules |
Volume | 49 |
Issue number | 4 |
DOIs | |
State | Published - 1 Nov 2011 |
Keywords
- Crystal structure
- Prephenate dehydrogenase
- Streptococcus mutans