ArticleJournal of bacteriology2004
The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 35 citations in OpenAlex.
- Functions of the prp operon in carbon source metabolism and acetic acid resistance in acetic acid bacteria: a case study in Acetobacter pasteurianus CGMCC 1.41.BMC microbiology · 2026Article
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- Crystal structures of aconitase X enzymes from bacteria and archaea provide insights into the molecular evolution of the aconitase superfamily.Communications biology · 2021Article
- Article
- Characterization of a NovelJournal of bacteriology · 2017Article
- Genetic and Biochemical Characterization of a Gene Operon forThe Journal of biological chemistry · 2017Article
- Article
- Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase.Scientific reports · 2016Article
- Ustilago maydis produces itaconic acid via the unusual intermediate trans-aconitate.Microbial biotechnology · 2016Article
- A large genomic island allows Neisseria meningitidis to utilize propionic acid, with implications for colonization of the human nasopharynx.Molecular microbiology · 2014Article
- Exogenous or L-rhamnose-derived 1,2-propanediol is metabolized via a pduD-dependent pathway in Listeria innocua.Applied and environmental microbiology · 2008Article
- Methanogen homoaconitase catalyzes both hydrolyase reactions in coenzyme B biosynthesis.The Journal of biological chemistry · 2008Article
- The complete genome sequence and analysis of the epsilonproteobacterium Arcobacter butzleri.PloS one · 2007Article
- The three-dimensional crystal structure of the PrpF protein of Shewanella oneidensis complexed with trans-aconitate: insights into its biological function.Protein science : a publication of the Protein Society · 2007Article
- Genomic analysis of carbon source metabolism of Shewanella oneidensis MR-1: Predictions versus experiments.Journal of bacteriology · 2006Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The propionate utilization operons of several bacteria differ from each other in the occurrence of two genes, acnD and prpF, in place of or in addition to the prpD gene encoding an Fe/S-independent 2-methylcitrate dehydratase enzyme. We cloned the acnD and prpF genes from two organisms, Shewanella oneidensis and Vibrio cholerae, and found that, together, the AcnD and PrpF proteins restored the ability of a prpD mutant strain of Salmonella enterica to grow on propionate as a source of carbon and energy. However, neither acnD nor prpF alone was able to substitute for prpD. The AcnD and PrpF proteins were isolated and biochemically analyzed. The AcnD protein required reconstitution of an Fe/S cluster for activity. All detectable AcnD activity was lost after incubation with iron-chelating agents, and no AcnD activity was observed after attempted reconstitution without iron. Nuclear magnetic resonance spectroscopy and in vitro activity assay data showed that AcnD dehydrated 2-methylcitrate and citrate to 2-methyl-cis-aconitate and cis-aconitate, respectively; AcnD also hydrated cis-aconitate. However, 2-methylisocitrate and isocitrate were not substrates for AcnD, indicating that AcnD only catalyzes the first half of the aconitase-like dehydration reactions. No aconitase-like activity was found for PrpF. It is hypothesized that, in vivo, PrpF is an accessory protein required to prevent oxidative damage of the Fe/S center of active AcnD enzyme or that it may be involved in synthesis or repair of the Fe/S cluster present in AcnD.
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