The inhibition of mevalonate kinase (MVK) by downstream metabolites is an important mechanism in the regulation of isoprenoid production in a broad range of organisms. The first feedback-resistant MVK was previously discovered in the methanogenic archaeon Methanosarcinamazei. Here， we report the cloning， expression， purification， kinetic characterization and inhibition analysis of MVKs from two other methanogens， Methanosaetaconcilii and Methanocellapaludicola. Similar to the M. mazei MVK， these enzymes were not inhibited by diphosphomevalonate (DPM)， dimethylallyl diphosphate (DMAPP)， isopentenyldiphosphate (IPP)， geranylpyrophosphate (GPP) or farnesylpyrophosphate (FPP). However， they exhibited significantly higher affinity to mevalonate and higher catalytic efficiency than the previously characterized enzyme.