Why do gram positive have disulphide bonds, which aniline inhibits?
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Gram-positive bacteria utilize disulfide bonds to stabilize extracytoplasmic proteins. These bonds are crucial for protein folding and stability, impacting various biological processes like autolysis, biofilm formation, and bacteriocin production. Inhibitors like certain anilines target enzymes involved in disulfide bond formation, such as Escherichia coli DsbB and Mycobacterium tuberculosis VKOR. These inhibitors hinder the activity of DsbB enzymes, affecting the formation of disulfide bonds in bacteria, potentially disrupting the stability and function of important proteins, including virulence factors. Therefore, understanding the role of disulfide bonds in Gram-positive bacteria and the impact of inhibitors like anilines on these bonds is crucial for developing strategies to target bacterial virulence and pathogenicity.
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| Papers (5) | Insight |
|---|---|
86 Citations | Gram-positive bacteria have disulphide bonds to stabilize extracytoplasmic proteins. Aniline inhibits thiol-disulphide oxidoreductases (TDORs) involved in disulphide bond formation in these bacteria. |
| Gram-positive bacteria have disulfide bonds for protein stability. Aniline inhibits the disulfide bond-forming enzyme DsbB in Gram-negative bacteria, affecting virulence factors and potential antibiotic development. | |
65 Citations | Gram-positive bacteria form disulfide bonds for protein stability. Aniline inhibits these bonds by disrupting the oxidation pathways, affecting protein function and potentially pathogenesis. |
39 Citations | Gram-positive bacteria have disulfide bonds for structural stability. Aniline inhibits these bonds due to its interference with the redox potential, affecting the bacteria's structural integrity. |
10 Citations | Gram-positive bacteria form disulfide bonds crucial for various functions like autolysis, biofilm formation, and bacteriocin activity. Aniline inhibits these bonds, impacting bacterial phenotypes. |
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