ArticleJournal of bacteriology2016
Pyrroloquinoline Quinone Ethanol Dehydrogenase in Methylobacterium extorquens AM1 Extends Lanthanide-Dependent Metabolism to Multicarbon Substrates.
Article in Journal of bacteriology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers, 1 of them a synthesis that pooled it.
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Who cites it
59 citing papers in PubMed, 1 synthesis or guideline pooled it, 141 citations in OpenAlex.
- Marine microbiomes and their expanding role in biotechnological potential: a systematic review.Archives of microbiology · 2026Pooled it
- A frameshift mutation drives divergent biosynthesis of metallophores inbioRxiv : the preprint server for biology · 2026Article
- Beneath the surface: expanding the known repertoire of methylotrophic metabolism.Applied and environmental microbiology · 2026Article
- Functional organization and regulatory logic of theApplied and environmental microbiology · 2026Review
- A PQQ-dependent oxidoreductase inFrontiers in cellular and infection microbiology · 2026Article
- Pink powerhouses: insights into the multifaceted role of Methylobacterium in climate-resilient farming.Folia microbiologica · 2025Review
- Expanding on the ability of trivalent actinides to support microbial alcohol metabolism in evolved methylotrophic bacterium.Communications chemistry · 2025Article
- XoxF and the Calvin-Benson cycle mediate lanthanide-dependent growth on methanol inApplied and environmental microbiology · 2025Article
- Lanthanide-dependent isolation of phyllosphere methylotrophs selects for a phylogenetically conserved but metabolically diverse community.bioRxiv : the preprint server for biology · 2025Article
- Deciphering the assembly process of PQQ dependent methanol dehydrogenase.Nature communications · 2025Article
- Methylobacterium extorquens PA1 utilizes multiple strategies to maintain formaldehyde homeostasis during methylotrophic growth.PLoS genetics · 2025Article
- Current study on Pyrroloquinoline quinone (PQQ) therapeutic role in neurodegenerative diseases.Molecular biology reports · 2025Review
- Emerging role of rare earth elements in biomolecular functions.The ISME journal · 2025Review
- Extensive and diverse lanthanide-dependent metabolism in the ocean.The ISME journal · 2025Article
- Identification and characterization of a small-molecule metallophore involved in lanthanide metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mononuclear binding and catalytic activity of europium(III) and gadolinium(III) at the active site of the model metalloenzyme phosphotriesterase.Acta crystallographica. Section D, Structural biology · 2024Article
- Engineering Terpene Production Pathways inMicroorganisms · 2024Article
- Weathered granites and soils harbour microbes with lanthanide-dependent methylotrophic enzymes.BMC biology · 2024Article
- Different lanthanide elements induce strong gene expression changes in a lanthanide-accumulating methylotroph.Microbiology spectrum · 2023Article
- An evolved pyrrolysyl-tRNA synthetase with polysubstrate specificity expands the toolbox for engineering enzymes with incorporation of noncanonical amino acids.Bioresources and bioprocessing · 2023Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lanthanides are utilized by microbial methanol dehydrogenases, and it has been proposed that lanthanides may be important for other type I alcohol dehydrogenases. A triple mutant strain (mxaF xoxF1 xoxF2; named MDH-3), deficient in the three known methanol dehydrogenases of the model methylotroph Methylobacterium extorquens AM1, is able to grow poorly with methanol if exogenous lanthanides are added to the growth medium. When the gene encoding a putative quinoprotein ethanol dehydrogenase, exaF, was mutated in the MDH-3 background, the quadruple mutant strain could no longer grow on methanol in minimal medium with added lanthanum (La IMPORTANCE: ExaF is the most efficient PQQ-dependent ethanol dehydrogenase reported to date and, to our knowledge, the first non-XoxF-type alcohol oxidation system reported to use lanthanides as a cofactor, expanding the importance of lanthanides in biochemistry and bacterial metabolism beyond methanol dehydrogenases to multicarbon metabolism. These results support an earlier proposal that an aspartate residue near the catalytic aspartate residue may be an indicator of rare-earth element utilization by type I alcohol dehydrogenases.
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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.