EC Number |
Natural Substrates |
---|
2.4.1.1 | (1,4-alpha-D-glucosyl)n + phosphate |
polysaccharide substrate is glycogen |
2.4.1.1 | (1,4-alpha-D-glucosyl)n + phosphate |
polysaccharide substrate is glycogen, first step in glycogen breakdown removing one glucose at a time |
2.4.1.1 | (1,4-alpha-D-glucosyl)n + phosphate |
polysaccharide substrate is glycogen, mobilization of glucose 1-phosphate as readily useable energy source |
2.4.1.1 | (1,4-alpha-D-glucosyl)n + phosphate |
polysaccharide substrate is starch, phosphorolysis is the physiologic reaction of the starch degrading enzyme |
2.4.1.1 | (1,4-alpha-D-glucosyl)n + phosphate |
the cytosolic isozyme is involved in the processing of incoming carbohydrate during rapid tissue growth, plastidic isozyme is associated with transitory leaf starch metabolism and with the initiation of seed endosperm reserve starch accumulation, but it plays no role in the degradation of the reserve starch |
2.4.1.1 | (maltodextrin)n-1 + alpha-D-glucose 1-phosphate |
maltodextrin phosphorylase is involved in the utilization of maltodextrins |
2.4.1.1 | more |
increased enzyme activity increases 5-phosphoribosyl-1-diphosphate availability in hepatocyte cultures and vice versa, glycogenolysis is a major contributor to PRPP generation in liver tissue in the basal state |
2.4.1.1 | more |
mastoparan binds to the enzyme to negatively regulate sarcoplasmic reticular Ca2+ release in skeletal muscle involving the ryanodine receptor, overview |
2.4.1.1 | more |
the cell volume affects the activity in hepatocytes, thus the enzyme activity is a function of medium osmolarity, activity is increased in hyperosmotic media, overview |
2.4.1.1 | more |
the enzyme regulates the association of glycogen synthase with a proteoglycogen substrate in hepatocytes |