ArticleNature2015
UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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Who cites it
74 citing papers in PubMed, 202 citations in OpenAlex.
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- Decarboxylation in Natural Products Biosynthesis.JACS Au · 2024Review
- In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis.Nature catalysis · 2024Article
- Lignin conversion to β-ketoadipic acid byScience advances · 2023Article
- Long-Chain Molecules with Agro-Bioactivities and Their Applications.Molecules (Basel, Switzerland) · 2023Review
- Enzymatic Conversion of COChemical reviews · 2023Review
- Naphthalene Carboxylation in the Sulfate-Reducing Enrichment Culture N47 Is Proposed to Proceed via 1,3-Dipolar Cycloaddition to the Cofactor Prenylated Flavin Mononucleotide.Applied and environmental microbiology · 2023Article
- Improved Assessment of Globularity of Protein Structures and the Ellipsoid Profile of the Biological Assemblies from the PDB.Biomolecules · 2023Article
- Isophthalate:coenzyme A ligase initiates anaerobic degradation of xenobiotic isophthalate.BMC microbiology · 2022Article
- Valorization of Polyethylene Terephthalate to Muconic Acid by EngineeringInternational journal of molecular sciences · 2022Article
- How plants synthesize coenzyme Q.Plant communications · 2022Review
- Flavin-enabled reductive and oxidative epoxide ring opening reactions.Nature communications · 2022Article
- Biosynthesis of triacsin featuring an N-hydroxytriazene pharmacophore.Nature chemical biology · 2021Article
14 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
Abstract
Ubiquinone (also known as coenzyme Q) is a ubiquitous lipid-soluble redox cofactor that is an essential component of electron transfer chains. Eleven genes have been implicated in bacterial ubiquinone biosynthesis, including ubiX and ubiD, which are responsible for decarboxylation of the 3-octaprenyl-4-hydroxybenzoate precursor. Despite structural and biochemical characterization of UbiX as a flavin mononucleotide (FMN)-binding protein, no decarboxylase activity has been detected. Here we report that UbiX produces a novel flavin-derived cofactor required for the decarboxylase activity of UbiD. UbiX acts as a flavin prenyltransferase, linking a dimethylallyl moiety to the flavin N5 and C6 atoms. This adds a fourth non-aromatic ring to the flavin isoalloxazine group. In contrast to other prenyltransferases, UbiX is metal-independent and requires dimethylallyl-monophosphate as substrate. Kinetic crystallography reveals that the prenyltransferase mechanism of UbiX resembles that of the terpene synthases. The active site environment is dominated by π systems, which assist phosphate-C1' bond breakage following FMN reduction, leading to formation of the N5-C1' bond. UbiX then acts as a chaperone for adduct reorientation, via transient carbocation species, leading ultimately to formation of the dimethylallyl C3'-C6 bond. Our findings establish the mechanism for formation of a new flavin-derived cofactor, extending both flavin and terpenoid biochemical repertoires.
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Registered trials
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.