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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Detalles Bibliográficos
Autores principales: Narczyk, Marta, Mioduszewski, Łukasz, Oksiejuk, Aleksandra, Winiewska-Szajewska, Maria, Wielgus-Kutrowska, Beata, Gojdź, Adrian, Cieśla, Joanna, Bzowska, Agnieszka
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8160210/
https://www.ncbi.nlm.nih.gov/pubmed/34045551
http://dx.doi.org/10.1038/s41598-021-90472-4

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8160210/
https://www.ncbi.nlm.nih.gov/pubmed/34045551
http://dx.doi.org/10.1038/s41598-021-90472-4

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