The enzyme participates in a mevalonate pathway that occurs in halophilic archaea. The activity is also present in eubacteria of the Chloroflexi phylum. cf. EC 4.1.1.33, diphosphomevalonate decarboxylase, and EC 4.1.1.110, bisphosphomevalonate decarboxylase.
The enzyme participates in a mevalonate pathway that occurs in halophilic archaea. The activity is also present in eubacteria of the Chloroflexi phylum. cf. EC 4.1.1.33, diphosphomevalonate decarboxylase, and EC 4.1.1.110, bisphosphomevalonate decarboxylase.
negligible inhibition by 6-fluoromevalonate diphosphate (a potent inhibitor of the classical mevalonate pathway), reinforcing its selectivity for monophosphorylated ligands
isopentenol production in Escherichia coli by utilizing phosphomevalonate decarboxylase and Escherchia coli-endogenous phosphatase AphA. The enzymes bypass the isopentenyl diphosphate mevalonate pathways, have reduced energetic requirements, are further decoupled from intrinsic regulation, and are free from isopentenyl diphosphate-related toxicity. Reduced aeration rate has less impact on the bypass pathway than the original mevalonate pathway. The performance of the bypass pathway is primarily determined by the activity of phosphomevalonate decarboxylase
isopentenol production in Escherichia coli by utilizing phosphomevalonate decarboxylase and Escherchia coli-endogenous phosphatase AphA. The enzymes bypass the isopentenyl diphosphate mevalonate pathways, have reduced energetic requirements, are further decoupled from intrinsic regulation, and are free from isopentenyl diphosphate-related toxicity. Reduced aeration rate has less impact on the bypass pathway than the original mevalonate pathway. The performance of the bypass pathway is primarily determined by the activity of phosphomevalonate decarboxylase
Identification in Haloferax volcanii of phosphomevalonate decarboxylase and isopentenyl phosphate kinase as catalysts of the terminal enzyme reactions in an archaeal alternate mevalonate pathway