Biophysical Characterization of a Novel Phosphopentomutase from the Hyperthermophilic Archaeon Thermococcus kodakarensis
Zahra Naz, Jacek Lubkowski, Muhammad Saleem, Mehwish Aslam, Moazur Rahman, Alexander Wlodawer, Naeem Rashid · 2024
Read Biophysical Characterization of a Novel Phosphopentomutase from the Hyperthermophilic Archaeon Thermococcus kodakarensis by Zahra Naz, Jacek Lubkowski, Muhammad Saleem, Mehwish Aslam, Moazur Rahman, Alexander Wlodawer, Naeem Rashid (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-11641776.txt.
Description
Enzymes from heat-loving microbes keep working where ordinary proteins melt, which makes them prized for industry. Zahra Naz and co-authors characterize in 2024 a phosphopentomutase from Thermococcus kodakarensis, an archaeon that thrives near boiling. The enzyme swaps a phosphate between two forms of ribose sugar, though it closely resembles enzymes that act on larger sugars.
The team measured its behavior and solved its three-dimensional structure by X-ray diffraction. The structure revealed a fresh catalytic motif, seen in no relative, that likely explains why it chooses five-carbon sugars over six-carbon ones. It is the first such portrait of a phosphopentomutase from a hyperthermophilic archaeon.
Catalog record
| CREATOR | Zahra Naz, Jacek Lubkowski, Muhammad Saleem, Mehwish Aslam, Moazur Rahman, Alexander Wlodawer, Naeem Rashid |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 37 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |