Glycogen phosphorylase, liver form
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Activity of phosphorylase is controlled both by allosteric means (through the noncovalent binding of metabolites) and by covalent modification. Thus AMP allosterically activates, whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase B.
AMPがアロステリック活性化因子、ATP、ADP、G6-Pがアロステリック阻害因子
Glycogen phosphorylase, muscle form
Activity of phosphorylase is controlled both by allosteric means (through the noncovalent binding of metabolites) and by covalent modification. Thus AMP allosterically activates, whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase B.
Glycogen [starch] synthase, liver
Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
Allosteric activation by glucose-6-phosphate. Phosphorylation reduces the activity towards UDP-glucose. When in the non-phosphorylated state, glycogen synthase does not require glucose-6-phosphate as an allosteric activator; when phosphorylated it does (By similarity).
G6-Pがアロステリック活性化因子
リン酸化によりUDP-グルコースに対する活性が低下する。非リン酸化状態で、グリコーゲンシンターゼの活性にG6-Pによる活性化は不要である。
Glycogen [starch] synthase, muscle
Allosteric activation by glucose-6-phosphate. Phosphorylation reduces the activity towards UDP-glucose. When in the non-phosphorylated state, glycogen synthase does not require glucose-6-phosphate as an allosteric activator; when phosphorylated it does (By similarity).
