Journal
JOURNAL OF MOLECULAR RECOGNITION
Volume 35, Issue 10, Pages -Publisher
WILEY
DOI: 10.1002/jmr.2979
Keywords
Enterococcus faecalis; Homoserine Kinase; homology modelling; Multidrug resistant
Categories
Funding
- DST FIST [SR/FST/LS-I/2017/56]
- DST PURSE [SR/PURSE/2021/77]
- New Delhi, India
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Infections caused by drug-resistant Enterococcus faecalis are a significant problem in hospitals. This study focuses on a critical protein in the bacteria and found that pheniramine has good binding affinity for it.
Infections caused by the bacteria Enterococcus faecalis (also known as E. faecalis) are common in hospitals. This bacterium is resistant to a wide range of medicines and causes a variety of nosocomial infections. An increase in the number of infections caused by multidrug-resistant (MDR) bacteria is causing substantial economic and health issues around the world. Consequently, new therapeutic techniques to tackle the growing threat of E. faecalis infections must be developed as soon as possible. In this regard, we have targeted a protein that is regarded to be critical for the survival of bacteria in this experiment. Homoserine kinase (HSK) is a threonine metabolism enzyme that belongs to the GHMP kinase superfamily. It is a crucial enzyme in threonine metabolism. This enzyme is responsible for a critical step in the threonine biosynthesis pathway. Given the important function that E. faecalis Homoserine Kinase (ESK) plays in bacterial metabolism, we report here cloning, expression, purification and structural studies of E. faecalis HSK using homology modelling. In addition, we have reported on the model's molecular docking and Molecular Dynamic Stimulation (MD Stimulation) investigations to validate the results of the docking experiments. The results were promising. In silico investigations came up with the conclusion: pheniramine has good binding affinity for the E. faecalis HSK.
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