Final answer:
Glycogen phosphorylase is regulated through allosteric modifiers and covalent modification. Inhibitors like glucose-6-phosphate and ATP create a less-active form of the enzyme, while activators like AMP create a more active form. Phosphorylation and dephosphorylation of phosphoserine residues also play a role in enzyme regulation.
Step-by-step explanation:
Glycogen phosphorylase is regulated by various mechanisms.
- Allosteric modifiers inhibit or activate the enzyme. Inhibitors for phosphorylase b include glucose-6-phosphate (G6P) and ATP, while activators include AMP. These modifiers create less or more active forms of the enzyme, respectively.
- Covalent modification involves phosphorylation of phosphoserine residues. Phosphorylase a has a phosphate attached, while phosphorylase b is the dephosphorylated form. Phosphorylation results in a less-active enzyme, and dephosphorylation reactivates it.