ArticlePloS one2013
Biochemical similarities and differences between the catalytic [4Fe-4S] cluster containing fumarases FumA and FumB from Escherichia coli.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- Evolution and metabolite signaling of fumarases (class I and II): origin, function, and subcellular targeting.Molecular biology and evolution · 2026Article
- Enantioselectivity in the enzymatic dehydration of malate and tartrate: Mirror image specificities of structurally similar dehydratases.Protein science : a publication of the Protein Society · 2023Article
- Chemoproteomics Reveals Disruption of Metal Homeostasis and Metalloproteins by the Antibiotic Holomycin.ACS chemical biology · 2023Article
- Interchangeability of class I and II fumarases in an obligate methanotroph Methylotuvimicrobium alcaliphilum 20Z.PloS one · 2023Article
- Identification of Iron-Sulfur (Fe-S) Cluster and Zinc (Zn) Binding Sites Within Proteomes Predicted by DeepMind's AlphaFold2 Program Dramatically Expands the Metalloproteome.Journal of molecular biology · 2022Article
- A combination of Class-I fumarases and metabolites (α-ketoglutarate and fumarate) signal the DNA damage response inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural and Biochemical Investigations of the [4Fe-4S] Cluster-Containing Fumarate Hydratase fromBiochemistry · 2019Article
- A critical comparison of cellular and cell-free bioproduction systems.Current opinion in biotechnology · 2019Review
- Zinc Toxicity and Iron-Sulfur Cluster Biogenesis inApplied and environmental microbiology · 2019Article
- Metabolic engineering of a carbapenem antibiotic synthesis pathway in Escherichia coli.Nature chemical biology · 2018Article
- EPR spectroscopy of complex biological iron-sulfur systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Biochemical characterization and essentiality ofThe Journal of biological chemistry · 2018Article
- Anaerobic Copper Toxicity and Iron-Sulfur Cluster Biogenesis in Escherichia coli.Applied and environmental microbiology · 2017Article
- Article
- Plasma metabolic profile delineates roles for neurodegeneration, pro-inflammatory damage and mitochondrial dysfunction in the FMR1 premutation.The Biochemical journal · 2016Article
- Crystal structure of an Fe-S cluster-containing fumarate hydratase enzyme from Leishmania major reveals a unique protein fold.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Hypothesis that the Genetic Code Originated in Coupled Synthesis of Proteins and the Evolutionary Predecessors of Nucleic Acids in Primitive Cells.Life (Basel, Switzerland) · 2015Article
- Mesaconase/Fumarase FumD in Escherichia coli O157:H7 and Promiscuity of Escherichia coli Class I Fumarases FumA and FumB.PloS one · 2015Article
- The Harvest suite for rapid core-genome alignment and visualization of thousands of intraspecific microbial genomes.Genome biology · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe highly homologous [4Fe-4S] containing fumarases FumA and FumB, sharing 90% amino acid sequence identity, from Escherichia coli are differentially regulated, which suggests a difference in their physiological function. The ratio of FumB over FumA expression levels increases by one to two orders of magnitude upon change from aerobic to anaerobic growth conditions. METHODOLOGY/PRINCIPAL
findingsTo understand this difference in terms of structure-function relations, catalytic and thermodynamic properties were determined for the two enzymes obtained from homologous overexpression systems. FumA and FumB are essentially identical in their Michaelis-Menten kinetics of the reversible fumarate to L-malate conversion; however, FumB has a significantly greater catalytic efficiency for the conversion of D-tartrate to oxaloacetate consistent with the requirement of the fumB gene for growth on D-tartrate. Reduction potentials of the [4Fe-4S](2+) Lewis acid active centre were determined in mediated bulk titrations in the presence of added substrate and were found to be approximately -290 mV for both FumA and FumB. CONCLUSIONS/SIGNIFICANCE: This study contradicts previously published claims that FumA and FumB exhibit different catalytic preferences for the natural substrates L-malate and fumarate. FumA and FumB differ significantly only in the catalytic efficiency for the conversion of D-tartrate, a supposedly non-natural substrate. The reduction potential of the substrate-bound [4Fe-4S] active centre is, contrary to previously reported values, close to the cellular redox potential.
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