ArticleEnvironmental microbiology2019
Syntrophus aciditrophicus uses the same enzymes in a reversible manner to degrade and synthesize aromatic and alicyclic acids.
Article in Environmental microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Structural Determinants of Catalytic Bias in an AMP-Forming Acetyl-CoA Synthetase frombioRxiv : the preprint server for biology · 2026Article
- Elevated COToxics · 2026Article
- Controlled irrigation suppresses methane emissions by reshaping the rhizosphere microbiomes in rice.Microbiology spectrum · 2026Article
- Crystal structure of a putative 3-hydroxypimelyl-CoA dehydrogenase, Hcd1, from Syntrophus aciditrophicus strain SB at 1.78 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2023Article
- The Acyl-Proteome of Syntrophus aciditrophicus Reveals Metabolic Relationships in Benzoate Degradation.Molecular & cellular proteomics : MCP · 2022Article
- Dynamic acylome reveals metabolite driven modifications inFrontiers in microbiology · 2022Article
- The missing enzymatic link in syntrophic methane formation from fatty acids.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- The Beta Subunit of Non-bifurcating NADH-Dependent [FeFe]-Hydrogenases Differs From Those of Multimeric Electron-Bifurcating [FeFe]-Hydrogenases.Frontiers in microbiology · 2020Article
Corrections and comments
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Authors and funding
15 authors at 2 institutions in 1 country.
Funding
Abstract
Syntrophy is essential for the efficient conversion of organic carbon to methane in natural and constructed environments, but little is known about the enzymes involved in syntrophic carbon and electron flow. Syntrophus aciditrophicus strain SB syntrophically degrades benzoate and cyclohexane-1-carboxylate and catalyses the novel synthesis of benzoate and cyclohexane-1-carboxylate from crotonate. We used proteomic, biochemical and metabolomic approaches to determine what enzymes are used for fatty, aromatic and alicyclic acid degradation versus for benzoate and cyclohexane-1-carboxylate synthesis. Enzymes involved in the metabolism of cyclohex-1,5-diene carboxyl-CoA to acetyl-CoA were in high abundance in S. aciditrophicus cells grown in pure culture on crotonate and in coculture with Methanospirillum hungatei on crotonate, benzoate or cyclohexane-1-carboxylate. Incorporation of
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