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Information on EC 3.2.1.1 - alpha-amylase
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3.2.1.1 alpha-amylaseIUBMB Comments
Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. The term "alpha" relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed.
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Word Map
- 3.2.1.1
- wheat
- cortisol
- aspergillus
- maltose
- pancreas
- oryzae
- glycogen
- granule
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acid-schiff
- lipase
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amylolytic
- alpha-glucosidase
- flour
- amylose
- glucoamylase
- aleurone
- grain
- cereal
- parotid
-
social
- amyloliquefaciens
- acarbose
-
sympathetic
-
anxiety
- amylopectin
-
psychological
- beta-amylase
- phaseolus
- stearothermophilus
- endosperm
-
gibberellic
-
alcian
-
hypothalamic-pituitary-adrenal
- dextrin
-
transglycosylation
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psychosocial
-
bread
- honey
-
bake
-
baking
- cyclodextrins
- amyloglucosidase
- isoamylase
-
pas-positive
-
eclosion
- awakening
- pullulanase
-
debranching
- pullulan
-
dough
- brewing
- food industry
- medicine
- pharmacology
- biofuel production
- nutrition
- biotechnology
- energy production
- analysis
- agriculture
- synthesis
- industry
- detergent
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
1,4-alpha-D-glucan glucanohydrolase, 1,4-alpha-D-glucan glucanohydrolase and endoamylase, 1,4-alpha-D-glucan-glucanohydrolase, ABA, acid-stable amylase, acidic amylase, AGXA, AHA, alkaline alpha-amylase, alkalophilic Bacillus alpha-amylase, 
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topREACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
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
mode of action
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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
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
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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
endo mode of action
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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
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
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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
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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
reaction mechanism and kinetic mechanism
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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
residues Asp204, Glu240, and Asp305 are involved in catalysis, residues His118, Ala206, Lys207, and His304 are important for starch binding
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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
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
the reaction mechanism involves no typical conformational change of the flexible loop, residues 303-309, that constitutes the surface edge of the substrate binding cleft, but only a small movement of the segment from residues 304/305, conformational change of catalytic residue Asp300 upon substrate binding, flexibility of the active site depends on the substrate aglycon bound, overview
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
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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
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
endo mode of action
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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
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
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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
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
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PATHWAY SOURCE
PATHWAYS