ArticleJournal of bacteriology2014
Identification in Haloferax volcanii of phosphomevalonate decarboxylase and isopentenyl phosphate kinase as catalysts of the terminal enzyme reactions in an archaeal alternate mevalonate pathway.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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45 citing papers in PubMed, 73 citations in OpenAlex.
- Constructing Haloarchaeal MVA Pathway in Serratia marcescens for Synthesis of Ocimene.Biotechnology and applied biochemistry · 2026Article
- Enhanced isoprenoid production inBiochemistry and biophysics reports · 2025Article
- Thermostable Enzyme Variants in the Lower Mevalonate Pathway Improve Isoprenoid Production by Cell-Free Biocatalysis.ACS sustainable chemistry & engineering · 2025Article
- Review
- Elucidating metabolic pathways through genomic analysis in highly heavy metal-resistantHeliyon · 2024Article
- The utility of Streptococcus mutans undecaprenol kinase for the chemoenzymatic synthesis of diverse non-natural isoprenoids.Bioorganic chemistry · 2024Article
- Archaeal mevalonate pathway in the uncultured bacteriumApplied and environmental microbiology · 2024Article
- Article
- Expanded Archaeal Genomes Shed New Light on the Evolution of Isoprenoid Biosynthesis.Microorganisms · 2024Article
- Advances in the Synthesis and Analysis of Biologically Active Phosphometabolites.International journal of molecular sciences · 2023Review
- A [4Fe-4S] cluster resides at the active center of phosphomevalonate dehydratase, a key enzyme in the archaeal modified mevalonate pathway.Frontiers in microbiology · 2023Article
- The catalytic and structural basis of archaeal glycerophospholipid biosynthesis.Extremophiles : life under extreme conditions · 2022Review
- Alternative metabolic pathways and strategies to high-titre terpenoid production inNatural product reports · 2022Review
- Article
- Review
- Novel Homologs of Isopentenyl Phosphate Kinase Reveal Class-Wide Substrate Flexibility.ChemCatChem · 2021Article
- Open Issues for Protein Function Assignment inGenes · 2021Article
- Diversifying Isoprenoid PlatformsFrontiers in microbiology · 2021Review
- Isotopic Tracers Unveil Distinct Fates for Nitrogen Sources during Wine Fermentation with Two Non-Microorganisms · 2020Article
- Structural studies of geranylgeranylglyceryl phosphate synthase, a prenyltransferase found in thermophilic Euryarchaeota.Acta crystallographica. Section D, Structural biology · 2020Article
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Mevalonate (MVA) metabolism provides the isoprenoids used in archaeal lipid biosynthesis. In synthesis of isopentenyl diphosphate, the classical MVA pathway involves decarboxylation of mevalonate diphosphate, while an alternate pathway has been proposed to involve decarboxylation of mevalonate monophosphate. To identify the enzymes responsible for metabolism of mevalonate 5-phosphate to isopentenyl diphosphate in Haloferax volcanii, two open reading frames (HVO_2762 and HVO_1412) were selected for expression and characterization. Characterization of these proteins indicated that one enzyme is an isopentenyl phosphate kinase that forms isopentenyl diphosphate (in a reaction analogous to that of Methanococcus jannaschii MJ0044). The second enzyme exhibits a decarboxylase activity that has never been directly attributed to this protein or any homologous protein. It catalyzes the synthesis of isopentenyl phosphate from mevalonate monophosphate, a reaction that has been proposed but never demonstrated by direct experimental proof, which is provided in this account. This enzyme, phosphomevalonate decarboxylase (PMD), exhibits strong inhibition by 6-fluoromevalonate monophosphate but negligible inhibition by 6-fluoromevalonate diphosphate (a potent inhibitor of the classical mevalonate pathway), reinforcing its selectivity for monophosphorylated ligands. Inhibition by the fluorinated analog also suggests that the PMD utilizes a reaction mechanism similar to that demonstrated for the classical MVA pathway decarboxylase. These observations represent the first experimental demonstration in H. volcanii of both the phosphomevalonate decarboxylase and isopentenyl phosphate kinase reactions that are required for an alternate mevalonate pathway in an archaeon. These results also represent, to our knowledge, the first identification and characterization of any phosphomevalonate decarboxylase.
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