Stringency of the 2-His–1-Asp Active-Site Motif in Prolyl 4-Hydroxylase
Kelly L. Gorres, Khian Hong Pua, Ronald T. Raines · 2009
Read Stringency of the 2-His–1-Asp Active-Site Motif in Prolyl 4-Hydroxylase by Kelly L. Gorres, Khian Hong Pua, Ronald T. Raines (2009) 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/plos-pone-0007635.txt.
Description
Kelly Gorres, Khian Hong Pua, and Ronald Raines published a study in PLOS ONE in 2009 on the metal-binding clasp shared by a family of enzymes. These iron-using enzymes hold their iron with a motif of two histidines and one carboxylate. The family performs many oxidative reactions, including modifying the amino acid proline. The team focused on prolyl 4-hydroxylase, an enzyme needed to build collagen. They tested how strict the motif's requirements are.
Changing parts of the clasp showed how much variation the enzyme tolerates. Stringency data tell chemists which features are non-negotiable for activity. That knowledge guides enzyme engineering and drug design alike. An enzyme that builds collagen is also a target in fibrotic disease. The study is basic enzymology with practical edges. It measures how tightly nature's design is locked.
Catalog record
| CREATOR | Kelly L. Gorres, Khian Hong Pua, Ronald T. Raines |
|---|---|
| YEAR | 2009 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 24 KB |
| LICENSE | Creative Commons Attribution License |
| RIGHTS | CC BY |
| SOURCE | PLOS ONE |
Source: https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0007635