Crystal structure of prephenate dehydrogenase from streptococcus mutans

Hyung Keun Ku, Nam Hyuk Do, Jin Sue Song, Saehae Choi, Seung Hoon Yeon, Min Hyung Shin, Kyung Jin Kim, Sang Ryoul Park, Il Young Park, Sook Kyung Kim, Soo Jae Lee

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

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 languageEnglish
Pages (from-to)761-766
Number of pages6
JournalInternational Journal of Biological Macromolecules
Volume49
Issue number4
DOIs
StatePublished - 1 Nov 2011

Keywords

  • Crystal structure
  • Prephenate dehydrogenase
  • Streptococcus mutans

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