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	
2.7.7.27	ATP + alpha-D-glucose 1-phosphate	rate-limiting step in starch synthesis, both subunits are involved in the allosteric regulation of AGPase	
2.7.7.27	ATP + alpha-D-glucose 1-phosphate	the reduction of cytosolic ADP-glucose pyrophosphorylase activity in shrunken endosperm did not inhibit granule initiation but severely restrained the subsequent enlargement of granules	
2.7.7.27	ATP + alpha-D-glucose 1-phosphate	AGPase, a key regulatory enzyme in starch biosynthesis, is highly regulated, effects of substrates, detailed overview	
2.7.7.27	ATP + alpha-D-glucose 1-phosphate	first committed step of starch biosynthesis in higher plants, identification of identify AGP isoforms essential for this biosynthetic process in sink and source tissues of rice plants	
2.7.7.27	ATP + alpha-D-glucose 1-phosphate	key step in glucan synthesis, the ADPGlc PPases are highly regulated by allosteric activators and inhibitors in accord with the carbon metabolism pathways of the organism	
2.7.7.27	ATP + alpha-D-glucose 1-phosphate	the enzyme is required for starch biosynthesis, while Tdy1 is not required, although tdy1-R mutant leaves retain large amounts of starch on prolonged dark treatment, consistent with a defect in starch catabolism, overview	
2.7.7.27	ATP + alpha-D-glucose-1-phosphate	AGP plays a crucial role in the morphogenesis of petal limbs in Xanthi through the synthesis of starch, which is the main carbohydrate source for expansion growth of petal limbs, in sepal tisues, overview	
2.7.7.27	additional information	elevated CO2 and increasing growth temperatures significantly increase activity of adenosine-5'-diphosphoglucose pyrophosphorylase. The upregulation of leaf carbohydrate metabolism enzymes under elevated CO2 plus temperature would be beneficial for growth and productivity of kidney bean in future climates	
2.7.7.27	additional information	a key enzyme in starch biosynthesis, its expression is regulated at both the transcriptional and post-transcriptional levels during fruit ripening, overview	
2.7.7.27	additional information	ADP-Glc PPase catalyzes the first committed step in starch biosynthesis	
2.7.7.27	additional information	ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis	
2.7.7.27	additional information	ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis. The heat lability of maize endosperm AGPase contributes to yield loss caused by heat stress, overview	
2.7.7.27	additional information	ADP-glucose pyrophosphorylase catalyzes the rate-limiting step in seed starch biosynthesis	
2.7.7.27	additional information	AGPase plays a key role in regulating starch biosynthesis in cereal seeds and is likely the most important determinant of seed strength	
2.7.7.27	additional information	the large subunit is required for AGPase activity in leaf blades