ArticleScientific reports2016
An Adaptation To Life In Acid Through A Novel Mevalonate Pathway.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- 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
- 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
- Characterization of novel mevalonate kinases from the tardigrade Ramazzottius varieornatus and the psychrophilic archaeon Methanococcoides burtonii.Acta crystallographica. Section D, Structural biology · 2024Article
- 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
- Functional Insights of Salinity Stress-Related Pathways in Metagenome-ResolvedApplied and environmental microbiology · 2022Article
- Alternative metabolic pathways and strategies to high-titre terpenoid production inNatural product reports · 2022Review
- Article
- Genomic Insights into the Ecological Role and Evolution of a NovelApplied and environmental microbiology · 2021Article
- Novel Homologs of Isopentenyl Phosphate Kinase Reveal Class-Wide Substrate Flexibility.ChemCatChem · 2021Article
- Comparative Genomics Provides Insights into the Genetic Diversity and Evolution of the DPANN Superphylum.mSystems · 2021Article
- Article
- Structural studies of geranylgeranylglyceryl phosphate synthase, a prenyltransferase found in thermophilic Euryarchaeota.Acta crystallographica. Section D, Structural biology · 2020Article
- Reconstruction of the "Archaeal" Mevalonate Pathway from the Methanogenic Archaeon Methanosarcina mazei in Escherichia coli Cells.Applied and environmental microbiology · 2020Article
- Conversion of Mevalonate 3-Kinase into 5-Phosphomevalonate 3-Kinase by Single Amino Acid Mutations.Applied and environmental microbiology · 2019Article
- A linear pathway for mevalonate production supports growth of Thermococcus kodakarensis.Extremophiles : life under extreme conditions · 2019Article
- Modified mevalonate pathway of the archaeonProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Extreme acidophiles are capable of growth at pH values near zero. Sustaining life in acidic environments requires extensive adaptations of membranes, proton pumps, and DNA repair mechanisms. Here we describe an adaptation of a core biochemical pathway, the mevalonate pathway, in extreme acidophiles. Two previously known mevalonate pathways involve ATP dependent decarboxylation of either mevalonate 5-phosphate or mevalonate 5-pyrophosphate, in which a single enzyme carries out two essential steps: (1) phosphorylation of the mevalonate moiety at the 3-OH position and (2) subsequent decarboxylation. We now demonstrate that in extreme acidophiles, decarboxylation is carried out by two separate steps: previously identified enzymes generate mevalonate 3,5-bisphosphate and a new decarboxylase we describe here, mevalonate 3,5-bisphosphate decarboxylase, produces isopentenyl phosphate. Why use two enzymes in acidophiles when one enzyme provides both functionalities in all other organisms examined to date? We find that at low pH, the dual function enzyme, mevalonate 5-phosphate decarboxylase is unable to carry out the first phosphorylation step, yet retains its ability to perform decarboxylation. We therefore propose that extreme acidophiles had to replace the dual-purpose enzyme with two specialized enzymes to efficiently produce isoprenoids in extremely acidic environments.
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