ArticleMolecular biology reports2012
Enzymatic and biological characteristics of enolase in Brucella abortus A19.
Article in Molecular biology reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Pathogenicity and virulence ofVirulence · 2025Review
- Dramatic Changes in Oligomerization Property Caused by Single Residue Deletion in Staphylococcus aureus Enolase.Molecular biotechnology · 2021Article
- Comparative proteomic and genomic analyses of Brucella abortus biofilm and planktonic cells.Molecular medicine reports · 2020Article
- Effect of ions and inhibitors on the catalytic activity and structural stability ofJournal of biosciences · 2019Article
- Immunolocation and enzyme activity analysis of Cryptosporidium parvum enolase.Parasites & vectors · 2017Article
- Mycoplasma synoviae enolase is a plasminogen/fibronectin binding protein.BMC veterinary research · 2014Article
- Characterization of the immunogenicity and pathogenicity of malate dehydrogenase in Brucella abortus.World journal of microbiology & biotechnology · 2014Article
- Enzymatic activity analysis and catalytic essential residues identification of Brucella abortus malate dehydrogenase.TheScientificWorldJournal · 2014Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Brucella abortus is the etiological agent of brucellosis, a disease causing human public health problems as well as major economic losses in domestic animal industries. In this study, the enolase gene of B. abortus A19 was cloned, sequenced and expressed in Escherichia coli BL21. Bacterial-expressed enolase protein (His-eno) was purified and its ability to catalyze the conversion of 2-phosphoglycerate (2-PGE) to phosphoenolpyruvate (PEP) (hereon referred to as enolase activity) was analyzed. Michaelis constant (K(m)) and maximum reaction velocity (V(max)) of the reaction was determined to be 2.0 × 10(-3) M and 178 μM l(-1)min(-1), respectively. Factors influencing the enolase activity of His-eno, such as pH, the presence of metal ions and temperature were investigated in vitro. The results showed that His-eno exhibited maximal enolase activity in pH 8.5 reaction buffer containing 10 mM MgSO(4) at 37 °C. In addition to studying the enzyme activity, binding assays were performed to provide insights into the function of His-eno on pathogenesis and immunity. His-eno exhibits fibronectin-binding ability in immunoblotting assay, suggesting that enolase may play a role in B. abortus colonization, persistence, and invasion of host tissue. Furthermore, Western blot demonstrated His-eno's binding ability to 34 bovine B. abortus positive sera, suggesting that future studies may find enolase a useful as a diagnostic marker or a vaccine candidate for brucellosis.
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