AtISA1 and AtISA2 are required for the production of a functional isoamylase-type of debranching enzyme named Iso1, the major isoamylase found in leaves. The absence of Iso1 leads to an 80% decrease in the starch content and to accumulation of water-soluble polysaccharides whose structure is similar to glycogen
AtISA1 and AtISA2 are required for the production of a functional isoamylase-type of debranching enzyme named Iso1, the major isoamylase found in leaves. The absence of Iso1 leads to an 80% decrease in the starch content and to accumulation of water-soluble polysaccharides whose structure is similar to glycogen
AtISA1 and AtISA2 are required for the production of a functional isoamylase-type of debranching enzyme named Iso1, the major isoamylase found in leaves. The absence of Iso1 leads to an 80% decrease in the starch content and to accumulation of water-soluble polysaccharides whose structure is similar to glycogen
glucan debranching occurs primarily at the granule surface via ISA3, but in its absence soluble branched glucans are debranched in the stroma via limit dextrinase. Isoamylase acts at the surface of the starch granule. Atisa3 mutants have more leaf starch and a slower rate of starch breakdown than wild-type plants
mutant lines carrying a defect in AtISA3 display a strong starch-excess phenotype at the end of both the light and the dark phases accompanied by a small modification of the amylopectin structure
mutant lines carrying a defect in AtISA3 display a strong starch-excess phenotype at the end of both the light and the dark phases accompanied by a small modification of the amylopectin structure
mutant lines carrying a defect in AtISA3 display a strong starch-excess phenotype at the end of both the light and the dark phases accompanied by a small modification of the amylopectin structure
isoamylase is one of the starch-debranching enzymes which catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans including amylopectin, branched starch, and glycogen
isoamylase is one of the starch-debranching enzymes which catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans including amylopectin, branched starch, and glycogen
3.2.1.68 isoamylase
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