Evidence map›Paper›PMID 25636853›Full record

ArticleApplied and environmental microbiology2015

The Putative mevalonate diphosphate decarboxylase from Picrophilus torridus is in reality a mevalonate-3-kinase with high potential for bioproduction of isobutene.

Luca Rossoni, Stephen J Hall, Graham Eastham, Peter Licence, Gill Stephens

Open access · hybridAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. International journal of systematic and evolutionary microbiology · 2024
    Article
  5. Article
  6. ACS chemical biology · 2022
    Article
  7. Article
  8. Article
  9. Isobutene production inMetabolic engineering communications · 2021
    Article
  10. Open life sciences · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Modified mevalonate pathway of the archaeonProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. On the Origin of Isoprenoid Biosynthesis.Molecular biology and evolution · 2018
    Article
  16. Review
  17. Article
  18. Lipid sugar carriers at the extremes: The phosphodolichols Archaea use in N-glycosylation.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Luca RossoniDepartment of Chemical and Environmental Engineering, Biorenewables and Bioprocessing Research Group, University of Nottingham, Nottingham, United Kingdom enxlr@nottingham.ac.uk.
Stephen J HallDepartment of Chemical and Environmental Engineering, Biorenewables and Bioprocessing Research Group, University of Nottingham, Nottingham, United Kingdom.
Graham EasthamLucite International, Wilton Centre, Wilton, United Kingdom.
Peter LicenceSchool of Chemistry, University of Nottingham, Nottingham, United Kingdom.
Gill StephensDepartment of Chemical and Environmental Engineering, Biorenewables and Bioprocessing Research Group, University of Nottingham, Nottingham, United Kingdom.
University of Nottingham · GBLucite International (United Kingdom) · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G023581/1Biotechnology and Biological Sciences Research Council BB/G023581/2
6 · The paper itself

Abstract

Mevalonate diphosphate decarboxylase (MVD) is an ATP-dependent enzyme that catalyzes the phosphorylation/decarboxylation of (R)-mevalonate-5-diphosphate to isopentenyl pyrophosphate in the mevalonate (MVA) pathway. MVD is a key enzyme in engineered metabolic pathways for bioproduction of isobutene, since it catalyzes the conversion of 3-hydroxyisovalerate (3-HIV) to isobutene, an important platform chemical. The putative homologue from Picrophilus torridus has been identified as a highly efficient variant in a number of patents, but its detailed characterization has not been reported. In this study, we have successfully purified and characterized the putative MVD from P. torridus. We discovered that it is not a decarboxylase per se but an ATP-dependent enzyme, mevalonate-3-kinase (M3K), which catalyzes the phosphorylation of MVA to mevalonate-3-phosphate. The enzyme's potential in isobutene formation is due to the conversion of 3-HIV to an unstable 3-phosphate intermediate that undergoes consequent spontaneous decarboxylation to form isobutene. Isobutene production rates were as high as 507 pmol min(-1) g cells(-1) using Escherichia coli cells expressing the enzyme and 2,880 pmol min(-1) mg protein(-1) with the purified histidine-tagged enzyme, significantly higher than reported previously. M3K is a key enzyme of the novel MVA pathway discovered very recently in Thermoplasma acidophilum. We suggest that P. torridus metabolizes MVA by the same pathway.

Indexed as

Adenosine TriphosphateAlkenesCarboxy-LyasesCloning, MolecularEscherichia coliGene ExpressionMevalonic AcidPhosphotransferases (Alcohol Group Acceptor)ThermoplasmalesValeratesAdenosine TriphosphateAlkenesbeta-hydroxyisovaleric acidCarboxy-Lyasesisobutylenemevalonate kinaseMevalonic Acidphosphomevalonic acidPhosphotransferases (Alcohol Group Acceptor)pyrophosphomevalonate decarboxylaseValerates

Identifiers

PMID25636853
PMCPMC4357925
OpenAlexW2044737218

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.