Pyrazinamide triggers degradation of its target aspartate decarboxylase

Pyrazinamide triggers degradation of its target aspartate decarboxylase

It has been shown that the bioactive component of pyrazinamide, pyrazinoic acid (POA), blocks coenzyme A biosynthesis in M. tuberculosis by binding to the aspartate decarboxylase PanD. Here the authors show that pyrazinamide triggers degradation of PanD by stimulating its degradation by the caseinol...

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Autores principales: Pooja Gopal, Jickky Palmae Sarathy, Michelle Yee, Priya Ragunathan, Joon Shin, Shashi Bhushan, Junhao Zhu, Tatos Akopian, Olga Kandror, Teck Kwang Lim, Martin Gengenbacher, Qingsong Lin, Eric J. Rubin, Gerhard Grüber, Thomas Dick
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/840f3d486eeb4f43af457982724b4b9d
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Sumario:It has been shown that the bioactive component of pyrazinamide, pyrazinoic acid (POA), blocks coenzyme A biosynthesis in M. tuberculosis by binding to the aspartate decarboxylase PanD. Here the authors show that pyrazinamide triggers degradation of PanD by stimulating its degradation by the caseinolytic protease Clp.

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