The Rv1712 locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially Phosphorylates dCMP

The Mycobacterium tuberculosis cmk gene, predicted to encode a CMP kinase (CMK), was cloned and expressed, and its product was purified to homogeneity. Steady-state kinetics confirmed that M. tuberculosis CMK is a monomer that preferentially phosphorylates CMP and dCMP by a sequential mechanism. A plausible role for CMK is discussed. Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Keywords

cytidine phosphate kinase, deoxycytidine phosphate, monomer, phosphotransferase, unclassified drug, cytidylate kinase, nucleoside monophosphate kinase, recombinant protein, bacterial gene, bacterial strain, controlled study, enzyme kinetics, enzyme phosphorylation, gene expression, gene locus, genetic code, molecular cloning, Mycobacterium tuberculosis, nonhuman, priority journal, protein function, protein purification, steady state, amino acid sequence, enzymology, genetics, isolation and purification, kinetics, metabolism, molecular genetics, phosphorylation, sequence alignment, Amino Acid Sequence, Cloning, Molecular, Deoxycytidine Monophosphate, Gene Expression, Kinetics, Molecular Sequence Data, Nucleoside-Phosphate Kinase, Phosphorylation, Recombinant Proteins, Sequence Alignment