Dissection of Catalytic Site in Crucial Gut Microbiome Enzyme: Bile Salt Hydrolase
| Autor: | Yashpal Yadav, Chand D, Archana Pundle, Mrityunjay K Tiwari, Sureshkumar Ramasamy, Boral D |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences biology Cholesterol Mutant Allosteric regulation Wild type Substrate (chemistry) 010402 general chemistry biology.organism_classification 01 natural sciences Enterococcus faecalis 0104 chemical sciences 03 medical and health sciences chemistry.chemical_compound Hydrolysis Enzyme chemistry Biochemistry 030304 developmental biology |
| DOI: | 10.1101/714493 |
| Popis: | Bile Salt Hydrolases (BSHs) are enzymes from enteric bacteria that catalyze the hydrolysis of Bile Acids and consequently promote the reduction of cholesterol level in the mammalian body. Out of several reported BSHs, the Enterococcus faecalis BSH (EfBSH) has been reported to have the highest enzymatic activity. Herein, we have investigated the mechanistic details of the EfBSH activity. The study was carried out employing two mutants of EfBSH: E269A and R207A, which shows differential catalytic activity. The mutant E269A exhibits significant loss in the BSH activity with an increased affinity towards the substrate as compared to R207A mutant. Further, R207A was found to be involved in allostery with an increased EfBSH activity towards tauro-conjugated bile acids. The structural and electrostatic force analyses of the active sites of the E269A mutant and the wild type EfBSH (wt EfBSH) revealed that the interaction between Glu21 and Arg207 is the determining factor in maintaining the dynamic allostery and high activity of EfBSH. |
| Databáze: | OpenAIRE |
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