Catalytic Mechanism of SARS-CoV-2 3-Chymotrypsin-Like Protease as Determined by Steady-State and Pre-Steady-State Kinetics
Jiyun Zhu, Alexandria M. Kemp, Bala C. Chenna, Vivek Kumar, Andrew Rademacher, Sangho Yun, Arthur Laganowsky, Thomas D. Meek · 2024
Read Catalytic Mechanism of SARS-CoV-2 3-Chymotrypsin-Like Protease as Determined by Steady-State and Pre-Steady-State Kinetics by Jiyun Zhu, Alexandria M. Kemp, Bala C. Chenna, Vivek Kumar, Andrew Rademacher, Sangho Yun, Arthur Laganowsky, Thomas D. Meek (2024) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-11667672.txt.
Description
Jiyun Zhu and co-authors published a chemistry study in 2024 on how the main protease of the SARS-CoV-2 virus does its cutting work. That enzyme is the target of the COVID-19 drug Paxlovid. Knowing its exact mechanism can guide drug design. The team measured reaction rates across acidity levels, for a substrate and for blockers, in both steady and early phases.
Rate patterns pointed to two key groups that must sit in the right charge states for the enzyme to work. The data best fit a neutral pair at the active site in the free enzyme. Heavy-water tests added support, showing the more active form dominates there. Early-phase rates ran faster in heavy water. The authors propose a full mechanism for the enzyme.
Catalog record
| CREATOR | Jiyun Zhu, Alexandria M. Kemp, Bala C. Chenna, Vivek Kumar, Andrew Rademacher, Sangho Yun, Arthur Laganowsky, Thomas D. Meek |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 77 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |