Single tryptophan Y160W mutant of homooligomeric E. coli purine nucleoside phosphorylase implies that dimers forming the hexamer are functionally not equivalent
Abstract E. coli purine nucleoside phosphorylase is a homohexamer, which structure, in the apo form, can be described as a trimer of dimers. Earlier studies suggested that ligand binding and kinetic properties are well described by two binding constants and two sets of kinetic constants. However, mo...
Saved in:
| Main Authors: | , , , , , , , |
|---|---|
| Format: | article |
| Language: | EN |
| Published: |
Nature Portfolio
2021
|
| Subjects: | |
| Online Access: | https://doaj.org/article/496f274ca99b4a1f857d7a1fc80b317d |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|