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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Autores principales: Marta Narczyk, Łukasz Mioduszewski, Aleksandra Oksiejuk, Maria Winiewska-Szajewska, Beata Wielgus-Kutrowska, Adrian Gojdź, Joanna Cieśla, Agnieszka Bzowska
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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R
Q
Acceso en línea:https://doaj.org/article/496f274ca99b4a1f857d7a1fc80b317d
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