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Crystal structure of prephenate dehydrogenase from Streptococcus mutans.

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 K(m) values of PDH from Streptococcus mutans.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Ku HK,Do NH,Song JS,Choi S,Yeon SH,Shin MH,Kim KJ,Park SR,Park IY,Kim SK,Lee SJ

doi

10.1016/j.ijbiomac.2011.07.009

subject

Has Abstract

pub_date

2011-11-01 00:00:00

pages

761-6

issue

4

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(11)00287-X

journal_volume

49

pub_type

杂志文章

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