Benzothiazinones: prodrugs that covalently modify the decaprenylphosphoryl-[beta]-D-ribose 2'-epimerase DprE1 of Mycobacterium tuberculosis

Authors :: Trefzer, Claudia
Rengifo-Gonzalez, Monica
Hinner, Marlon J.
Schneider, Patricia
Makarov, Vadim
Cole, Stewart T.
Johnsson, Kai
Source :: Journal of the American Chemical Society. Oct 6, 2010, Vol. 132 Issue 39, 13663-13665
Publication Year :: 2010
Abstract: Benzothiazinones (BTZs) have formed a new class of potent antimycobacterial agents. BTZs are activated in the bacterium by reduction of an essential nitro group to a nitroso derivative, which has reacted with a cysteine residue in the active site of decaprenylphosphoryl-[beta]-D-ribose 2E-epimerase (DprE1) of Mycobacterium tuberculosis.

Subjects :: Benzene -- Structure
Benzene -- Chemical properties
Cysteine -- Chemical properties
Mycobacterium tuberculosis -- Control
Nitrogen compounds -- Chemical properties
Organosulfur compounds -- Chemical properties
Organosulfur compounds -- Health aspects
Phosphorylation -- Analysis
Ribose -- Structure
Ribose -- Chemical properties
Chemistry

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