ArticleJournal of bacteriology2005
Menaquinone-specific prenyl reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 30 citations in OpenAlex.
- Unraveling the multiplicity of geranylgeranyl reductases in Archaea: potential roles in saturation of terpenoids.Extremophiles : life under extreme conditions · 2024Review
- Membrane Adaptations and Cellular Responses ofInternational journal of molecular sciences · 2023Article
- Presence of Phylloquinone in the Intraerythrocytic Stages ofFrontiers in cellular and infection microbiology · 2022Article
- An automated workflow to screen alkene reductases using high-throughput thin layer chromatography.Biotechnology for biofuels · 2020Article
- Construction of an artificial biosynthetic pathway for hyperextended archaeal membrane lipids in the bacteriumSynthetic biology (Oxford, England) · 2020Article
- Discovery of novel geranylgeranyl reductases and characterization of their substrate promiscuity.Biotechnology for biofuels · 2018Article
- Partial Saturation of Menaquinone inACS central science · 2015Article
- A Metagenomics-Based Metabolic Model of Nitrate-Dependent Anaerobic Oxidation of Methane by Methanoperedens-Like Archaea.Frontiers in microbiology · 2015Article
- Geranylgeranyl reductase and ferredoxin from Methanosarcina acetivorans are required for the synthesis of fully reduced archaeal membrane lipid in Escherichia coli cells.Journal of bacteriology · 2014Article
- Biosynthesis of ubiquinone compounds with conjugated prenyl side chains.Applied and environmental microbiology · 2008Article
- Identification of the bchP gene, encoding geranylgeranyl reductase in Chlorobaculum tepidum.Journal of bacteriology · 2008Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Four genes that encode the homologues of plant geranylgeranyl reductase were isolated from a hyperthermophilic archaeon Archaeoglobus fulgidus, which produces menaquinone with a fully saturated heptaprenyl side chain, menaquinone-7(14H). The recombinant expression of one of the homologues in Escherichia coli led to a distinct change in the quinone profile of the host cells, although the homologue is the most distantly related to the geranylgeranyl reductase. The new compounds found in the profile had successively longer elution times than those of ordinary quinones from E. coli, i.e., menaquinone-8 and ubiquinone-8, in high-performance liquid chromatography on a reversed-phase column. Structural analyses of the new compounds by electron impact-mass spectrometry indicated that their molecular masses progressively increase relative to the ordinary quinones at a rate of 2 U but that they still contain quinone head structures, strongly suggesting that the compounds are quinones with partially saturated prenyl side chains. In vitro assays with dithionite as the reducing agent showed that the prenyl reductase is highly specific for menaquinone-7, rather than ubiquinone-8 and prenyl diphosphates. This novel enzyme noncovalently binds flavin adenine dinucleotide, similar to geranylgeranyl reductase, but was not able to utilize NAD(P)H as the electron donor, unlike the plant homologue.
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