Publication Abstract from PubMed
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 beta6 and beta7, which may be a reason for the high K(m) values of PDH from Streptococcus mutans.
Crystal structure of prephenate dehydrogenase from Streptococcus mutans.,Ku HK, Do NH, Song JS, Choi S, Yeon SH, Shin MH, Kim KJ, Park SR, Park IY, Kim SK, Lee SJ Int J Biol Macromol. 2011 Nov 1;49(4):761-6. Epub 2011 Jul 20. PMID:21798280[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
