Intersubunit communication in glycogen phosphorylase influences substrate recognition at the catalytic sites
Abstract Glycogen phosphorylase (GP) is biologically active as a dimer of identical subunits, each activated by phosphorylation of the serine-14 residue. GP exists in three interconvertible forms, namely GPa (di-phosphorylated form), GPab (mono-phosphorylated form), and GPb (non-phosphorylated form)...
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| Main Authors: | Nahori Kamada, Ayato Ikeda, Yasushi Makino, Hiroshi Matsubara |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Springer
2024-02-01
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| Series: | Amino Acids |
| Subjects: | |
| Online Access: | https://doi.org/10.1007/s00726-023-03362-6 |
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