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Results 1 - 10 of 12 > >>
EC Number
Reaction
Commentary
Reference
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
PFTA is a bifunctional enzyme showing alpha-amylase as well as cyclodextrin-hydrolyzing activity
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
residues Asp204, Glu240, and Asp305 are involved in catalysis, residues His118, Ala206, Lys207, and His304 are important for starch binding
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
the active site structure involves the catalytic residues D197, E233, and D300, reaction mechanism
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
reaction mechanism and kinetic mechanism
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
mode of action
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
TVAII is a bifunctional enzyme showing alpha-amylase as well as cyclodextrin-hydrolyzing activity, the enzyme hydrolyzes alpha-1,4-glucosidic linkages and alpha-1,6-glucosidic linkages, active site structure and substrate binding structure, Trp356 is involved in substrate binding, and Tyr374 is involved in substrate orientation for catalysis
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
isozyme Amyl III acts on the alpha-1,4-glycosidic linkage of the inner granule and releases oligosaccharides, decomposition of granules into G2 and G3
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
Tyr105 and Thr212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of alpha-amylase 1
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
active site mobility and structure of the psychrophilic alpha-amylase, ligand binding mechanism and conformational changes, side chains involved in substrate binding are strictly conserved, overview
Results 1 - 10 of 12 > >>