| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1987866 | International Journal of Biological Macromolecules | 2009 | 6 Pages |
Abstract
Mycobacterium tuberculosis shikimate dehydrogenase (MtbSD) catalyzes the forth reaction in the shikimate pathway. Here we describe production of K69A, K69H, K69I, K69Q, D105A, and D105N mutant proteins. Screening of several conditions was performed to optimize MtbSD production yield, and an improved purification protocol to obtain homogeneous MtbSD is presented. The rational design of new antitubercular drugs hinges on the availability of M. tuberculosis proteins. Our results show that optimization of expression, disruption, and purification protocols resulted in a higher yield of functional MtbSD enzyme.
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Authors
Valnês da Silva Rodrigues-Junior, Luiz Augusto Basso, Diógenes Santiago Santos,