Experimentally it is not possible to calculate the energy nor the structure of the substrate during an enzymatic reaction. With the aid of in silico analysis, it is possible to follow the energetic and structural change of the conformers (products and substrates) that are involved in an enzymatic reaction. In the present work, an in silico analysis of the Cefamandole’s structural and energetic change was conducted; both, inside and outside the active site of the β-lactamase K73A fromMycobacterium tuberculosis. The energy for each conformer was determined by molcular mechanics. Cefamandole’s non-hydrolyzed energy, before entering the active site of β-lactamase K73A, was of 333.16 kJ/mol; inside the active site the value changed to 342.06 kJ/mol. The energy of the hydrolyzed Cefamandole inside the active site was of 323.86 kJ/mol; while outside of the active site the energy was 321.76 kJ/mol. The energy surge of the non-hydrolyzed Cefamandole inside the active site is due to a conformational change required to occupy the active site. The decrease in energy of the hydrolyzation makes the reaction irreversible. Hydrolyzed Cefamandole outside of the active site has the lowest energy, which explains the escape from the active site.
- Home
- About us
- EDITORIAL BOARD
- INSTRUCTION TO AUTHOR
- Current Issue
- Archive
- September, 2024
- August, 2024
- July 2024
- June 2024
- May 2024
- April 2024
- March 2024
- February 2024
- January 2024
- December 2023
- November, 2023
- October 2023
- September 2023
- August 2023
- July 2023
- June 2023
- May 2023
- April 2023
- March 2023
- February 2023
- January 2023
- December 2022
- November 2022
- October 2022
- September 2022
- August 2022
- July 2022
- June 2022
- May 2022
- April 2022
- March 2022
- February 2022
- January 2022
- December 2021
- November, 2021
- October, 2021
- September, 2021
- August, 2021
- July, 2021
- June, 2021
- May, 2021
- April 2021
- March 2021
- February 2021
- January 2021
- Submit Article
- Certificate
- Reviewers Form
- Contact Us