| Title : The lipolytic activity of LipJ, a stress-induced enzyme, is regulated by its C-terminal adenylate cyclase domain - Kumari_2021_Future.Microbiol__ |
| Author(s) : Kumari B , Kaur J , Maan P , Kumar A |
| Ref : Future Microbiol , : , 2021 |
|
Abstract :
Aim: The confirmation of lipolytic activity and role of Rv1900c in the mycobacterium physiology Methods: rv1900c/N-terminus domain (rv1900NT) were cloned in pET28a/Escherichia coli, purified by affinity chromatography and characterized. Results: A zone of clearance on tributyrin-agar and activity with pNP-decanoate confirmed the lipolytic activity of Rv1900c. The Rv1900NT demonstrated higher enzyme specific activity, V(max) and k(cat), but Rv1900c was more thermostable. The lipolytic activity of Rv1900c decreased in presence of ATP. Mycobacterium smegmatis expressing rv1900c/rv1900NT altered colony morphology, growth, cell surface properties and survival under stress conditions. The effect was more prominent with Rv1900NT as compared with Rv1900c. Conclusion: The study confirmed the lipolytic activity of Rv1900c and suggested its regulation by the adenylate cyclase domain and role in intracellular survival of bacteria. |
| PubMedSearch : Kumari_2021_Future.Microbiol__ |
| PubMedID: 33960821 |
Kumari B, Kaur J, Maan P, Kumar A (2021)
The lipolytic activity of LipJ, a stress-induced enzyme, is regulated by its C-terminal adenylate cyclase domain
Future Microbiol
:
Kumari B, Kaur J, Maan P, Kumar A (2021)
Future Microbiol
: