Identification of catalytic residues in human mevalonate kinase.

@article{Potter1997IdentificationOC,
  title={Identification of catalytic residues in human mevalonate kinase.},
  author={David Potter and Henry M. Miziorko},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 41},
  pages={25449-54}
}
cDNA encoding human mevalonate kinase has been overexpressed and the recombinant enzyme isolated. This stable enzyme is a dimer of 42-kDa subunits and exhibits a Vm = 37 units/mg, Km(ATP) = 74 microM, and Km(DL-MVA) = 24 microM. The sensitivity of enzyme to water-soluble carbodiimide modification of carboxyl groups prompted evaluation of four invariant acidic amino acids (Glu-19, Glu-193, Asp-204, and Glu-296) by site-directed mutagenesis. Elimination of Glu-19's carboxyl group (E19A, E19Q… CONTINUE READING