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...
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| Auteurs principaux: | , , , , , , , |
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| Format: | article |
| Langue: | EN |
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Nature Portfolio
2021
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| Accès en ligne: | https://doaj.org/article/496f274ca99b4a1f857d7a1fc80b317d |
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