Single tryptophan Y160W mutant of homooligomeric E. coli purine nucleoside phosphorylase implies that dimers forming the hexamer are functionally not equivalent
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DOI: 10.1038/s41598-021-90472-4
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… read more here.
Keywords: purine nucleoside; dimers forming; y160w mutant; coli purine ... See more keywords