| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8290796 | Archives of Biochemistry and Biophysics | 2013 | 11 Pages |
Abstract
- Substrate addition is random for Mycobacterium tuberculosis CMP kinase (MtCMK).
- CMP and CDP binding to MtCMK showed favorable enthalpy and unfavorable entropy.
- ATP binding to MtCMK was characterized by favorable enthalpy and entropy changes.
- MtCMK:phosphoryl group acceptor complex formation involves a net gain of protons.
- Asp187 of MtCMK is suggested as the likely candidate for the protonation event.
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Authors
Léia Jaskulski, Leonardo A. Rosado, Diana C. Rostirolla, Luis F.S.M. Timmers, Osmar N. de Souza, Diogenes S. Santos, Luiz A. Basso,