ArticleParasitology research2013
Citrate synthase from the liver fluke Fasciola hepatica.
Article in Parasitology research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 7 citations in OpenAlex.
- Proteomic insights into broiler stress responses to LED lighting: Effects on liver proteome under neutral, cool, and warm spectra.PloS one · 2025Article
- Effect ofJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2022Article
- Citrate Synthase and OGDH as Potential Biomarkers of Atherosclerosis under Chronic Stress.Oxidative medicine and cellular longevity · 2021Article
- Cloning, expression, characterization, and immunological properties of citrate synthase from Echinococcus granulosus.Parasitology research · 2019Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Citrate synthase catalyses the first step of the Krebs' tricarboxylic acid cycle. A sequence encoding citrate synthase from the common liver fluke, Fasciola hepatica, has been cloned. The encoded protein sequence is predicted to fold into a largely α-helical protein with high structural similarity to mammalian citrate synthases. Although a hexahistidine-tagged version of the protein could be expressed in Escherichia coli, it was not possible to purify it by nickel-affinity chromatography. Similar results were obtained with a version of the protein which lacks the putative mitochondrial targeting sequence (residues 1 to 29). However, extracts from bacterial cells expressing this version had additional citrate synthase activity after correcting for the endogenous, bacterial activity. The apparent K m for oxaloacetate was found to be 0.22 mM, which is higher than that observed in mammalian citrate synthases. Overall, the sequence and structure of F. hepatica citrate synthase are similar to ones from other eukaryotes, but there are enzymological differences which merit further investigation.
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