Starch is a major energy source for all domains of life. Recent advances in structures of starch-degrading enzymes encompass the substrate complex of starch debranching enzyme, the function of surface binding sites in plant isoamylase, details on individual steps in the mechanism of plant disproportionating enzyme and a self-stabilised conformation of amylose accommodated in the active site of plant α-glucosidase. Important inhibitor complexes include a flavonol glycoside, montbretin A, binding at the active site of human pancreatic α-amylase and barley limit dextrinase inhibitor binding to the debranching enzyme, limit dextrinase using a new binding mode for cereal protein inhibitors
Not AvailableMaize starch is an important industrial commodity. Starch synthase, phosphorylase, bran...
α-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydro...
AbstractBackground: α-Amylases catalyze the hydrolysis of α-D-(1,4)-glucan linkages in starch and re...
α-Amylases occur widely in plants, animals, and microorganisms. They often act in synergy with other...
Germinating barley seeds contain multiple forms of α-amylase, which are subject to both differential...
Higher plant, family GH3 β-d-glucan glucohydrolases exhibit exo-hydrolytic and retaining (e→e) mecha...
AbstractBackground α-Amylases catalyze the hydrolysis of glycosidic linkages in starch and other rel...
Most glucoamylases (α-1,4-d-glucan glucohydrolase, EC 3.2.1.3) have structures consisting of both a ...
Starch debranching enzymes, which specifically hydrolyse a-1,6-glucosidic bonds in glucans containin...
Starch is a major storage product of many economically important crops such as wheat, rice, maize, t...
Amylases are widely distributed and are one of the most studied enzymes. These enzymes have wide sca...
International audienceTo investigate the functions of debranching enzymes in starch biosynthesis, we...
Family 3 β-D-glucan glucohydrolases are distributed widely in higher plants. The enzymes catalyze th...
AbstractA novel polysaccharide binding site is identified in domain C of barley α-amylase 1 from the...
α-Glucan debranching enzymes hydrolyse α-1,6-linkages in starch/glycogen, thereby, playing a central...
Not AvailableMaize starch is an important industrial commodity. Starch synthase, phosphorylase, bran...
α-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydro...
AbstractBackground: α-Amylases catalyze the hydrolysis of α-D-(1,4)-glucan linkages in starch and re...
α-Amylases occur widely in plants, animals, and microorganisms. They often act in synergy with other...
Germinating barley seeds contain multiple forms of α-amylase, which are subject to both differential...
Higher plant, family GH3 β-d-glucan glucohydrolases exhibit exo-hydrolytic and retaining (e→e) mecha...
AbstractBackground α-Amylases catalyze the hydrolysis of glycosidic linkages in starch and other rel...
Most glucoamylases (α-1,4-d-glucan glucohydrolase, EC 3.2.1.3) have structures consisting of both a ...
Starch debranching enzymes, which specifically hydrolyse a-1,6-glucosidic bonds in glucans containin...
Starch is a major storage product of many economically important crops such as wheat, rice, maize, t...
Amylases are widely distributed and are one of the most studied enzymes. These enzymes have wide sca...
International audienceTo investigate the functions of debranching enzymes in starch biosynthesis, we...
Family 3 β-D-glucan glucohydrolases are distributed widely in higher plants. The enzymes catalyze th...
AbstractA novel polysaccharide binding site is identified in domain C of barley α-amylase 1 from the...
α-Glucan debranching enzymes hydrolyse α-1,6-linkages in starch/glycogen, thereby, playing a central...
Not AvailableMaize starch is an important industrial commodity. Starch synthase, phosphorylase, bran...
α-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydro...
AbstractBackground: α-Amylases catalyze the hydrolysis of α-D-(1,4)-glucan linkages in starch and re...