EC Number |
Natural Substrates |
---|
2.7.7.27 | ATP + alpha-D-glucose 1-phosphate |
- |
2.7.7.27 | ATP + alpha-D-glucose 1-phosphate |
first step of starch biosynthesis |
2.7.7.27 | ATP + alpha-D-glucose 1-phosphate |
first unique reaction in synthesis of alpha-1,4-glucosidic linkage |
2.7.7.27 | ATP + alpha-D-glucose 1-phosphate |
one of the main regulatory steps in starch biosynthesis in plants |
2.7.7.27 | ATP + alpha-D-glucose 1-phosphate |
major regulated step in the bacterial glycogen biosynthesis pathway |
2.7.7.27 | ATP + alpha-D-glucose 1-phosphate |
key regulatory enzyme of starch biosynthesis |
2.7.7.27 | ATP + alpha-D-glucose 1-phosphate |
ADP-glucose pyrophosphorylase catalyzes the first committed and rate-limiting step in starch biosynthesis |
2.7.7.27 | ATP + alpha-D-glucose 1-phosphate |
different large subunit isoforms allow the enzyme to be efficiently regulated according to the metabolic situation and the starch necessities of a tissue. In source tissues, ADP-glucose diphosphorylase would be finely regulated by the 3-phosphoglycerate/phosphate ratio, whereas in sink tissues, the enzyme would be dependent on the availability of substrates for starch synthesis |
2.7.7.27 | ATP + alpha-D-glucose 1-phosphate |
first committed step in synthesis of ADP-glucose |
2.7.7.27 | ATP + alpha-D-glucose 1-phosphate |
rate-limiting step in starch biosynthesis |