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Single tryptophan Y160W mutant of homooligomeric E. coli purine nucleoside phosphorylase implies that dimers forming the hexamer are functionally not equivalent
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, most of the...
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| Udgivet i: | Sci Rep |
|---|---|
| Main Authors: | , , , , , , , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
Nature Publishing Group UK
2021
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC8160210/ https://ncbi.nlm.nih.gov/pubmed/34045551 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-021-90472-4 |
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