ArticleBiochemistry2010
Characterization of thermophilic archaeal isopentenyl phosphate kinases.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 62 citations in OpenAlex.
- High-Throughput Profiling of Prenylelongases Enables the Assembly of Modified Prenoids.ACS chemical biology · 2026Article
- Thermostable Enzyme Variants in the Lower Mevalonate Pathway Improve Isoprenoid Production by Cell-Free Biocatalysis.ACS sustainable chemistry & engineering · 2025Article
- Article
- Functional Characterization and Screening of Promiscuous Kinases and Isopentenyl Phosphate Kinases for the Synthesis of DMAPP via a One-Pot Enzymatic Cascade.International journal of molecular sciences · 2022Article
- Article
- Review
- Novel Homologs of Isopentenyl Phosphate Kinase Reveal Class-Wide Substrate Flexibility.ChemCatChem · 2021Article
- Probing the Substrate Promiscuity of Isopentenyl Phosphate Kinase as a Platform for Hemiterpene Analogue Production.Chembiochem : a European journal of chemical biology · 2019Article
- The isoprenoid alcohol pathway, a synthetic route for isoprenoid biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Conversion of Mevalonate 3-Kinase into 5-Phosphomevalonate 3-Kinase by Single Amino Acid Mutations.Applied and environmental microbiology · 2019Article
- An Artificial Pathway for Isoprenoid Biosynthesis Decoupled from Native Hemiterpene Metabolism.ACS synthetic biology · 2019Article
- Exploring natural biodiversity to expand access to microbial terpene synthesis.Microbial cell factories · 2019Article
- Metabolic engineering of Methylobacterium extorquens AM1 for the production of butadiene precursor.Microbial cell factories · 2018Article
- Modified mevalonate pathway of the archaeonProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Lipid sugar carriers at the extremes: The phosphodolichols Archaea use in N-glycosylation.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- An Adaptation To Life In Acid Through A Novel Mevalonate Pathway.Scientific reports · 2016Article
- Improving the catalytic activity of isopentenyl phosphate kinase through protein coevolution analysis.Scientific reports · 2016Article
- Orthologs of the archaeal isopentenyl phosphate kinase regulate terpenoid production in plants.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The Putative mevalonate diphosphate decarboxylase from Picrophilus torridus is in reality a mevalonate-3-kinase with high potential for bioproduction of isobutene.Applied and environmental microbiology · 2015Article
- Two strategies for the synthesis of the biologically important ATP analogue ApppI, at a multi-milligram scale.Beilstein journal of organic chemistry · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Archaea synthesize isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), the essential building blocks of isoprenoid compounds, from mevalonate (MVA). However, an analysis of the genomes of several members of the Archaea failed to identify genes for the enzymes required to convert phosphomevalonate (PM) to IPP in eukaryotes. The recent discovery of an isopentenyl kinase (IPK) in Methanocaldococcus jannaschii (MJ) suggests a new variation of the MVA pathway where PM is decarboxylated to give isopentenyl phosphate (IP), which is phosphorylated to produce IPP. A blast search using the MJ protein as a probe revealed a subfamily of amino acid kinases that include the fosfomycin resistance protein fomA, which deactivates the antibiotic by phosphorylation of its phosphonate residue in a reaction similar to the conversion of IP to IPP. IPK genes were cloned from two organisms identified in the search, Methanothermobacter thermautotrophicus (MTH) and Thermoplasma acidophilum (THA), and the His-tagged recombinant proteins were purified by Ni-NTA chromatography. The enzymes catalyze the reversible phosphorylation of IP by ATP, K(eq) = 6.3 +/- 1. The catalytic efficiencies (V/K) of the proteins were approximately 2 x 10(6) M(-1) s(-1). In the reverse direction, ADP was a substrate inhibitor for THA IPK, K(i)(ADP) = 58 +/- 6 microM, but not for MTH IPK. Both enzymes were active over a broad range of pH and temperature. Five compounds, dimethylallyl phosphate, isopentenyl thiolophosphate, 1-butyl phosphate, 3-buten-1-yl phosphate, and geranyl phosphate, were evaluated as alternative substrates for the MTH and THA IP kinases. All of the compounds were phosphorylated, although the catalytic efficiency was low for geranyl phosphate.
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