Intersubunit communication in glycogen phosphorylase influences substrate recognition at the catalytic sites

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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Bibliographic Details
Main Authors: Nahori Kamada, Ayato Ikeda, Yasushi Makino, Hiroshi Matsubara
Format: Article
Language:English
Published: Springer 2024-02-01
Series:Amino Acids
Subjects:
Chemical probing
Glycogen phosphorylase
Intersubunit communication
Phospho–dephospho hybrid
Phosphorylation regulation
Substrate recognition
Online Access:https://doi.org/10.1007/s00726-023-03362-6
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https://doi.org/10.1007/s00726-023-03362-6

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