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Cover Picture: Nanomolar Competitive Inhibitors of Mycobacterium tuberculosis and Streptomyces coelicolor Type II Dehydroquinase (ChemMedChem 2/2007)
Author(s) -
Prazeres Verónica F. V.,
SánchezSixto Cristina,
Castedo Luis,
Lamb Heather,
Hawkins Alastair R.,
RiboldiTunnicliffe Alan,
Coggins John R.,
Lapthorn Adrian J.,
GonzálezBello Concepción
Publication year - 2007
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.200790000
Subject(s) - streptomyces coelicolor , mycobacterium tuberculosis , stereochemistry , shikimate pathway , chemistry , shikimic acid , streptomyces , derivative (finance) , non competitive inhibition , nuclear magnetic resonance spectroscopy , mycobacterium , antibiotics , biochemistry , microbiology and biotechnology , enzyme , tuberculosis , biology , biosynthesis , bacteria , genetics , medicine , pathology , financial economics , economics
The cover picture shows two representations of two potent competitive inhibitors of Mycobacterium tuberculosis and Streptomyces coelicolor dehydroquinase with a bacterial culture in the background. These enzymes operate in the shikimic acid pathway, which is an important target for the development of new antibiotics. On the right, the bioactive conformation of the 3‐nitrophenyl derivative as bound to the Mycobacterium tuberculosis active site, obtained from NMR spectroscopy, is highlighted. On the left, the picture depicts the proposed binding mode for the most potent inhibitor reported to date against any dehydroquinase, a 6‐benzothiophenyl derivative (4 n M ). For more details, see the Full Paper by C. González‐Bello et al. on p. 194 ff.