3.2.1.20 1,4-alpha-D-glucooligosaccharide + H2O short glucose oligomers, substrate derived from starch by alpha-amylase activity, the enzyme is important in mucosal alpha-glucogenesis, MGAM primes and mucosal sucrase-isomaltase activity sustains and constrains prandial alpha-glucogenesis from starch oligomers, regulation mechanism, overview 3.2.1.20 1,4-alpha-D-glucooligosaccharide + H2O the four isozymes digest all linear starch oligosaccharides to glucose 3.2.1.20 4-nitrophenyl D-glucopyranoside + H2O - 3.2.1.20 alpha-1,4-glucan + H2O - 3.2.1.20 amylopectin + H2O in starch, preferred substrate 3.2.1.20 glycogen + H2O - 3.2.1.20 malto-oligosaccharides + H2O - 3.2.1.20 maltodextrin + H2O - 3.2.1.20 maltoheptaose + 6 H2O - 3.2.1.20 maltooligosaccharides + H2O - 3.2.1.20 maltose + H2O - 3.2.1.20 maltose + H2O probable physiological role of the enzyme in the utilization of exogenous glycoproteins and/or in the turnover of the organism’s own glycoproteins, overview 3.2.1.20 maltose + H2O the enzyme is involved in maltose and starch metabolism 3.2.1.20 maltotriose + 2 H2O - 3.2.1.20 additional information alpha-glucosidase C may be involved in glycogen metabolism 3.2.1.20 additional information synthesis of riboflavin alpha-glucoside is catalyzed by the transglucosylation activity 3.2.1.20 additional information pompe disease, glycosidosis type II, is an autosomal recessive lysosomal storage disease that results from a deficiency of acid alpha-glucosidase. Patients with this disorder are unable to break down lysosomal glycogen, which consequently accumulates in the lysosome 3.2.1.20 additional information glycogen storage disease is caused by lysosomal acid alpha-glucosidase deficiency 3.2.1.20 additional information the enzyme might be mainly responsible for the predominant formation of glucose in starch hydrolysis of the germinating beet endosperm 3.2.1.20 additional information maltose is required for induction. The enzyme may play a role in the breakdown of internal storage polysaccharides containing alpha-1,4 and alpha-1,6 bonds 3.2.1.20 additional information expression is subject to both maltose induction and carbon catabolite repression. Induction of enzyme expression also occurs when starch, amylose, or glycogen are present in the growth medium 3.2.1.20 additional information the enzyme has a function in endogenous metabolism of alpha-glucans provided extracellularly as carbon source 3.2.1.20 additional information induced by maltose but repressed by alpha-D-glucose and fructose 3.2.1.20 additional information induced during growth on maltose and starch 3.2.1.20 additional information the formation of maltase and alpha-glucosidase is induced by trehalose, sucrose or lactose in the growth medium 3.2.1.20 additional information optimal enzyme production reaches a maximum after 24 h growth 3.2.1.20 additional information transcription reaches a maximum 48 h after the start of germination 3.2.1.20 additional information phylogenetic analysis 3.2.1.20 additional information the enzyme catalyzes the final step in the metabolism of carbohydrates, such as starch, to glucose for cell utilization, the oligosaccharide transport system shows high affinity for trehalose and maltose 3.2.1.20 additional information the enzyme has a role in the general carbohydrate metabolism, and in glycoprotein processing 3.2.1.20 additional information the organism does not possess alpha-amylase activity 3.2.1.20 additional information the enzyme prefers partially degraded starch substrate from germinating millet seeds 3.2.1.20 additional information a severe form of enzyme deficiency causes the infantile Pompe disease 3.2.1.20 additional information enzymic digestion profile determination for camel small intestine, overview 3.2.1.20 additional information the neutral alpha-glucosidase is involved in epididymal maturation, which is different in well-fed and undernourished mice, overview 3.2.1.20 additional information alpha-glucosidases play important roles in the digestion of carbohydrates and biosynthesis of viral envelope glycoproteins 3.2.1.20 additional information biotransformation of starch using the alpha-transglucosidase-producing Geobacillus stearothermophilus U2 3.2.1.20 nigerose + H2O alpha-1,3-linkage, exists as abnormal linkage in starch 3.2.1.20 RS toxin + H2O specific for the host-specific Rhizoctonia solani toxin, purified from Rhizoctonia solani-inoculated rice sheath, inactivation of the toxin and inhibition of the fungal mycelial growth 3.2.1.20 soluble starch + H2O the enzyme hydrolyzes alpha-1,4-glycosidic bonds, exo-acting enzyme 3.2.1.20 starch + H2O - 3.2.1.20 starch + H2O one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion