Kinetic mechanism and energetics of binding of phosphoryl group acceptors to Mycobacterium tuberculosis cytidine monophosphate kinase

- 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.