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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
- trypsin
- glycogen
- granule
- lipase
-
acid-schiff
- alpha-glucosidase
- flour
-
amylolytic
- glucoamylase
- aleurone
- grain
- amylose
- parotid
- cereal
- amyloliquefaciens
-
social
-
sympathetic
- acarbose
- amylopectin
- phaseolus
- endosperm
- beta-amylase
-
psychological
- stearothermophilus
-
anxiety
-
acinar
-
gibberellic
-
psychosocial
-
alcian
- honey
-
bread
- dextrin
- amyloglucosidase
-
hypothalamic-pituitary-adrenal
- cyclodextrins
-
transglycosylation
- isoamylase
- pullulanase
-
dough
-
bake
- awakening
-
debranching
- pullulan
-
pas-positive
- energy production
- synthesis
- nutrition
- food industry
- brewing
- industry
- pharmacology
- biotechnology
- biofuel production
- analysis
- agriculture
- detergent
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
alpha-amylase, diastase, alpha amylase, pancreatic alpha-amylase, crustacean cardioactive peptide, maltogenic amylase, taka-amylase a, human salivary alpha-amylase, bacillus licheniformis alpha-amylase, alpha-amylase 2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-alpha-D-glucan glucanohydrolase
1,4-alpha-D-glucan glucanohydrolase and endoamylase
1,4-alpha-D-glucan-glucanohydrolase
acidic amylase
alkaline alpha-amylase
alpha amylase
alpha-1,4 glucan-glucanohydrolase
alpha-1,4-glucan-4-glucanohydrolase
alpha-amylase
alpha-amylase 1
alpha-amylase I
alpha-amylase II
alpha-amylase PA
Amy
Amy-FC1
AMY1
AMY2
amy5
Amy7C
AmyA
AmyB
AmyC
AmyCR
AmyE
AmyK
AmyK38
AmyL
Amyl III
amylopullulanase
AmyQ
AmyUS100
AmyUS100DELTAIG
ApkA
Apu
BAA
BH072alpha-amylase
BLA
Blamy-I
BMA.2
Bsamy-I
cold-active alpha-amylase
cold-adapted alpha-amylase
endo-1,4-alpha-D-glucan glucanohydrolase
endo-1,4-alpha-D-glucan glucohydrolase
endo-1,4-alpha-D-glucanohydrolase
Gt-amy
HSA
htur2110
hyperthermophilic alpha-amylase
-
classified in family 13 of the glucosyl hydrolase superfamily
LAMY
liquozyme
-
commercial preparation, free and immobilzed enzyme, covalently bound to calcium alginate matrix
Low pI alpha-amylase
maltogenic amylase
N8 alpha-amylase
PPA-I
PPA-II
raw-starch-digesting alpha-amylase
RB5AMG_01539
Rbamy5
Ruminococcus bromii intermediary alpha-amylase 5
Saci_1162
salt-tolerant alpha-amylase
Sfamy
SSO1172
TAA
TdAmyA
TfAmy48
thermostable alpha-amylase
-
free and immobilzed enzyme, covalently bound to calcium alginate matrix
Tp-AmyS
additional information
AmyB
exo-acting intracellular alpha-amylase that possesses distinct characteristics from typical alpha-amylases and cyclodextrin-hydrolyzing enzymes such as maltogenic amylase, cyclodextrinase, and neopullulanase
AmyB
exo-acting intracellular alpha-amylase that possesses distinct characteristics from typical alpha-amylases and cyclodextrin-hydrolyzing enzymes such as maltogenic amylase, cyclodextrinase, and neopullulanase
AmyUS100
-
variant of the most thermoactive and thermostable maltohexaose forming alpha-amylase produced in Geobacillus stearothermophilus sp. US100
AmyUS100
-
variant of the most thermoactive and thermostable maltohexaose forming alpha-amylase produced in Geobacillus stearothermophilus sp. US100
additional information
-
the soybean alpha-amylase belongs to glycosyl hydrolase family 13
additional information
-
cf. EC 3.2.1.54, cyclomaltodextrinase, the enzyme belongs to glycoside hydrolase family 13
additional information
the enzyme belongs to the glycoside hydrolase family 13, subfamily 1
additional information
the enzyme belongs to the glycoside hydrolase family 13, subfamily 1
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REACTION
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
-
-
-
-
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
-
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
-
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
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
endo 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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan glucanohydrolase
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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CAS REGISTRY NUMBER
COMMENTARY
9000-90-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-chloro-4-nitrophenyl alpha-D-galactopyranosyl-(1-4)-alpha-D-galactopyranosyl-(1-4)-alpha-D-galactopyranoside + H2O
2-chloro-4-nitrophenol + alpha-D-galactopyranosyl-(1-4)-alpha-D-galactopyranosyl-(1-4)-alpha-D-galactopyranose
-
-
the increase of absorbance of 2-chloro-4-nitrophenol liberated by HSA is measured continuously at 400 nm
-
?
2-chloro-4-nitrophenyl alpha-D-maltoheptaoside + H2O
2-chloro-4-nitrophenol + alpha-D-maltoheptaose
-
-
-
-
?
2-chloro-4-nitrophenyl alpha-D-maltotrioside + H2O
2-chloro-4-nitrophenol + alpha-D-maltotriose
-
-
-
-
?
2-chloro-4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside + H2O
2-chloro-4-nitrophenol + ?
pH 6.8, 30°C
-
-
?
2-chloro-4-nitrophenyl beta-D-maltoheptaoside + H2O
2-chloro-4-nitrophenol + beta-D-maltoheptaose
-
-
-
?
2-chloro-4-nitrophenyl-alpha-D-maltotrioside + H2O
2-chloro-4-nitrophenol + alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose
-
commercial substrate for a flourescence-based assay, pH 7.0
-
-
?
2-chloro-4-nitrophenyl-alpha-maltotrioside + H2O
2-chloro-4-nitrophenol + alpha-maltotrioside
3 glycogen
maltotriose + maltotetraose + maltopentaose
-
approx. 10% of activity with starch
-
-
?
3 starch + 2 H2O
3 malto-oligosaccharides + D-glucose + maltose
-
-
-
-
?
4,6-ethylidene-4-nitrophenyl-alpha-D-maltoheptaoside + H2O
p-nitrophenol + 4,6-ethyliden-[G7]-alpha-D-maltoheptaoside
-
hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside + H2O
p-nitrophenol + 4,6-ethyliden-[G7]-alpha-D-maltoheptaoside
4,6-O-benzylidene 4-nitrophenyl-alpha-D-maltoheptaoside + H2O
4,6-O-benzylidene 4-nitrophenyl-alpha-D-maltosides
-
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
4-nitrophenyl alpha-D-maltopentaoside + H2O
4-nitrophenol + alpha-D-maltopentaose
-
-
-
-
?
4-nitrophenyl alpha-D-maltoside + H2O
4-nitrophenol + alpha-D-maltose
4-nitrophenol is bound at the ative site
-
-
?
4-nitrophenyl maltoheptaoside + H2O
4-nitrophenol + maltoheptaoside
-
-
-
?
4-nitrophenyl maltoheptaoside + H2O
maltotriose + maltotetraose + 4-nitrophenyl maltotetraoside + 4-nitrophenyl maltotrioside
-
-
-
?
4-nitrophenyl-alpha-D-maltopentaoside + H2O
4-nitrophenol + alpha-D-maltopentaose
-
activity measured in total fly homogenates, substrate concentration of 2.2 mM in HEPES buffer, enzyme activity preferentially required for degrading starch components of plant tissue
-
-
?
4-nitrophenyl-alpha-D-maltopentaoside + H2O
4-nitrophenol + alpha-D-maltopentaoside
-
-
-
-
?
acarbose + H2O
?
-
the substrate is a potent inhibitor of alpha-amylases, cyclomaltodextrinase activity
-
-
?
alpha-1,4-glucan + H2O
fragments of alpha-1,4-glucan
-
-
-
-
?
alpha-cyclodextrin + H2O
maltooligosaccharides
-
92% of activity with soluble starch
-
-
?
ammylopectin + H2O
?
-
the enzyme exhibits higher activity toward soluble starch rather than amylose (55%), amylopectin (41%), dextrin (60%), and glycogen (29%)
-
-
?
amylopectin + H2O
D-glucose + maltose
71.1% activity compared to amylose
-
-
?
amylopectin + H2O
D-glucose + maltose + maltotriose
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans
-
-
?
amylopectin + H2O
maltose + D-glucose
0.5% substrate solution, 12% activity compared to amylose
-
-
?
amylopektin + H2O
?
-
activity is 41% compared to the activity with soluble starch
-
-
?
amylose + H2O
maltotriose + maltotetraose + maltopentaose
-
approx. 10% of activity with starch
-
-
?
amylose + H2O
oligosaccharides
amylose DP17, preferred substrate of mutant enzyme T212Y
-
-
?
beta-cyclodextrin + H2O
D-glucose + maltose
39.0% activity compared to amylose
-
-
?
beta-cyclodextrin + H2O
maltooligosaccharides
-
27% of activity with potato starch
-
-
?
beta-cyclodextrin + H2O
panose + maltoheptaose
-
cyclomaltodextrinase activity
-
-
?
corn starch + H2O
maltohexaose + maltopentaose + maltotriose
-
64% activity compared to potato starch
major end-products of starch hydrolysis
-
?
corn starch + H2O
maltose + maltotriose
-
103.2% activity compared to soluble starch
-
-
?
cyclodextrin + H2O
panose + maltoheptaose
-
cyclomaltodextrinase activity, hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
dextrin + H2O
malto-oligosaccharides
-
67% activity compared to corn starch
-
-
?
gelatinized starch + H2O
maltotetraose + maltopentaose + maltohexaose
-
isozyme RBLA prefers gelatinized starch
-
-
?
glycogen + H2O
D-glucose + maltose
40.2% activity compared to amylose
-
-
?
isopanose + H2O
?
-
cyclomaltodextrinase activity, hydrolysis of alpha-1,6-glucosidic linkages
-
-
?
laminarin + H2O
?
-
lower activity with isozyme AI-1, low activity with isozymes AI-2 and AII
-
-
?
malto-oligosaccharides + H2O
maltose
-
hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
maltodextrin + H2O
malto-oligosaccharides
-
85% activity compared to starch
-
-
?
maltoheptaose + 3 H2O
2 maltose + maltotriose
-
additional product: maltotetraose
-
?
maltoheptaose + H2O
maltotriose + maltose + D-glucose
-
-
identified by thin-layer-chromatography
-
?
maltoheptaoside + H2O
?
all mutants possess the ability to hydrolyze heptasaccharide substrates and generate a similar product profile like the wild-type enzyme. The three mutants W203A, W284A, HSAmy-ar generate less products. They require higher enzyme concentration (600 nM vs. 60 nM for HSAmy and the other mutants) and more time (5 min vs. 2 min) 25°C, pH 6.9
-
-
?
maltohexaose + H2O
maltopentaose + maltotetraose + maltotriose + maltose
-
45% of activity with potato starch
-
-
?
maltohexaose + H2O
maltotetraose + maltotriose + maltose + D-glucose
-
-
identified by thin-layer-chromatography
-
?
maltooligosaccharide + H2O
?
the enzyme shows a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7)
-
-
?
maltooligosaccharides + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose
-
11% of activity with potato starch
-
-
?
maltooligosaccharides + H2O
maltotriose + maltotetraose
-
alpha-amylase activity
main products
-
?
maltopentaose + H2O
maltotetraose + maltotriose + maltose
-
26% of activity with potato starch
-
-
?
maltopentaose + H2O
maltotetraose + maltotriose + maltose + D-glucose
-
-
identified by thin-layer-chromatography
-
?
maltopentaoside + H2O
?
all mutants possess the ability to hydrolyze pentasaccharide substrates and generate a similar product profile like the wild-type enzyme. The three mutants W203A, W284A, HSAmy-ar generate less products. They require higher enzyme concentration (600 nM vs. 60 nM for HSAmy and the other mutants) and more time (5 min vs. 2 min) 25°C, pH 6.9
-
-
?
maltotriose
maltose + glucose + maltotetraose + maltopentaose + maltohexaose
-
the final optimum also mirrors the reverse reaction
-
r
p-nitrophenyl maltoheptaoside + H2O
?
-
a maximum of substrate cleavage was identified at 152 MPa and 64°C, yielding approximately 25% higher substrate conversion after 30 min, as compared to the maximum at ambient pressure and 59°C
-
-
?
p-nitrophenyldi[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
p-nitrophenol + p-nitrophenyl-alpha-D-glucopyranoside + p-nitrophenyldi[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + p-nitrophenyltri[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
-
intestine alpha-amylase
-
?
p-nitrophenyldi[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
p-nitrophenyl-alpha-D-glucopyranoside + p-nitrophenyldi[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + p-nitrophenyltri[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
-
muscle alpha-amylase
-
?
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
?
-
-
-
-
?
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
p-nitrophenol + p-nitrophenyl-alpha-D-glucopyranoside + p-nitrophenyldi[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + p-nitrophenyltri[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + p-nitrophenyltetra[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
-
intestine and muscle alpha-amylase
-
?
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
p-nitrophenyl-alpha-D-glucopyranoside + D-glucose
-
-
predominant product, no p-nitrophenol detected
-
?
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
p-nitrophenyl-alpha-D-glucopyranoside + p-nitrophenyldi[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + p-nitrophenyltri[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + p-nitrophenyltetra[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
-
-
muscle alpha-amylase
-
?
p-nitrophenylpenta[alpha-D-glucopyranosyl(1-4)]-alpha-D-galactopyranoside
?
-
-
-
-
?
potato starch + H2O
maltohexaose + maltopentaose + maltotriose
-
100% activity
major end-products of starch hydrolysis
-
?
potato starch + H2O
maltose + maltotriose
-
50.1% activity compared to soluble starch
-
-
?
pullulan + H2O
D-glucose + maltose
54.4% activity compared to amylose
-
-
?
pullulan + H2O
panose + maltoheptaose
-
cyclomaltodextrinase activity
-
-
?
raw rice starch + H2O
D-glucose + maltose + maltotriose
wild-type enzyme AmyP recombinant chimeric enzyme mutant
-
-
?
raw soluble starch + H2O
?
-
22% activity compared to gelatinized soluble starch
-
-
?
raw starch + H2O
malto-oligosaccharides
-
isozymes RBSA-1 and BSA-2, raw starch from corn and potato, the latter is preferred
-
-
?
Remazol Brilliant Blue dyed starch + H2O
malto-oligosaccharides
-
-
-
?
Remazol Brilliant Blue-dyed starch + H2O
malto-oligosaccharides
-
-
-
?
rice flour + H2O
?
48.7% activity compared to soluble starch
-
-
?
rice starch + H2O
maltose + maltotriose
-
88.2% activity compared to soluble starch
-
-
?
soluble potato starch + H2O
maltotriose + maltose + maltotetraose
-
major products of the enzymatic reaction with starch as substrate
-
?
soluble rice starch + H2O
?
55% activity compared to soluble potato starch
-
-
?
soluble starch + H2O
D-glucose + maltose
93.3% activity compared to amylose
-
-
?
soluble starch + H2O
D-glucose + maltose + maltotriose + maltotetraose
-
-
-
?
soluble starch + H2O
maltose
-
maximal activity is achieved with horse-radish starch, undetectable activity towards potato starch
-
-
?
soluble wheat starch + H2O
?
79% activity compared to soluble potato starch
-
-
?
starch + butanol
butylglucoside + alpha-D-glucose
-
butylglucoside: wild-type ca. 4.5 mg/ml, mutant H222Q ca. 6.5 mg/ml, mutant H222E ca. 3.5 mg/ml, mutant H222D ca. 5.5 mg/mk, identified and analyzed by thin-layer-chromatography and HPLC
-
?
starch + H2O
alpha-D-glucose + maltose
pH 7.0, 85°C
wild-type (alpha-D-glucose: ca. 22 mg/ml, maltose: ca. 5.5 mg/ml), mutants: W177V (alpha-D-glucose: ca. 20 mg/ml, maltose: ca. 5 mg/ml), Y178V (alpha-D-glucose: ca. 19 mg/ml, maltose: ca. 4 mg/ml), and F179V (alpha-D-glucose: ca. 17.5 mg/ml, maltose: ca. 7 mg/ml), almost no maltotriose as product for all variants, identified and analyzed by thin-layer-chromatography and HPLC
-
?
starch + H2O
alpha-D-glucose + maltose + maltotriose
pH 7.0, 85°C
mutants: H222Q (alpha-D-glucose: ca. 21 mg/ml, maltose: ca. 5 mg/ml, maltotriose: ca. 2.5 mg/ml), H222D (alpha-D-glucose: ca. 21 mg/ml, maltose: ca. 8 mg/ml, maltotriose: ca. 2.5 mg/ml), H222E (alpha-D-glucose: ca. 13 mg/ml, maltose: ca. 8 mg/ml, maltotriose: ca. 2.0 mg/ml), and V259W (alpha-D-glucose: ca. 16 mg/ml, maltose: ca. 8 mg/ml, maltotriose: ca. 2.5 mg/ml), identified and analyzed by thin-layer-chromatography and HPLC
-
?
starch + H2O
alpha-maltose + ?
-
action mode is endolytic, hydrolysis products have an alpha-anomeric configuration. Degradation of 1% (w/v) starch results in the formation of oligosaccharides in the maltose to maltopentaose range at early time points, followed by an accumulation of maltose, maltotetraose, and small amounts of glucose after 1 h, and its final end products consisted of a high level of 58% (w/w) maltose without concomitant production of glucose
-
-
?
starch + H2O
maltose + malto-oligosaccharides + D-glucose
-
soluble starch
trace amounts of D-glucose
-
?
starch + H2O
maltotriose + glucose + maltose + maltotetraose
-
pH 4, 55°C, various starches are tested: soluble potato starch as reference 100% relative activity, gelatinized amylose: 74%, potato native starch: 0.2%, potato gelatinized starch: 106%, maize native starch: 0.8%, maize gelatinized starch: 53%, rice native starch: 0.5%, and rice gelatinized starch: 52%
identified by thin-layer-chromatography, maltotriose represents 70% of the end products, only traces of glucose, small amounts of maltose and maltotetraose
-
?
starch + H2O
maltotriose + maltohexaose + maltoheptaose + maltose
-
soluble starch
first two are major products, maltohexose and maltose are intermediate products, maltotriose and maltohexaose are major products, maltoheptaose and maltose are intermediate products
-
?
starch + H2O
maltotriose + maltotetraose
-
alpha-amylase activity, preferred substrate
main products
-
?
starch + H2O
oligosaccharides
insoluble blue starch, preferred substrate of mutant enzyme Y105A
-
-
?
starch + methanol
methylglucoside + alpha-D-glucose
-
methylglucoside: wild-type ca. 7.5 mg/ml, mutant H222Q ca. 13 mg/ml, mutant H222E ca. 11 mg/ml, mutant H222D ca. 11 mg/mk, identified and analyzed by thin-layer-chromatography and HPLC
-
?
sweet potato starch + H2O
maltose + maltotriose
-
109.1% activity compared to soluble starch
-
-
?
sweet sorghum starch + H2O
?
-
62% activity compared to potato soluble starch
-
-
?
tapioca root starch + H2O
?
-
88% activity compared to potato soluble starch
-
-
?
wheat flour + H2O
?
53.0% activity compared to soluble starch
-
-
?
wheat starch + H2O
maltohexaose + maltopentaose + maltotriose
-
78% activity compared to potato starch
major end-products of starch hydrolysis
-
?
wheat starch + H2O
maltose + maltotriose
-
92.0% activity compared to soluble starch
-
-
?
2 starch + H2O
2 malto-oligosaccharides + maltose
-
hydrolysis of soluble starch, and degradation of raw starch granules of different source, overview
-
-
?
2-chloro-4-nitrophenyl-alpha-D-maltotrioside + H2O
2-chloro-4-nitrophenol + maltotriose
-
-
-
-
?
2-chloro-4-nitrophenyl-alpha-D-maltotrioside + H2O
2-chloro-4-nitrophenol + maltotriose
-
-
-
-
?
2-chloro-4-nitrophenyl-alpha-maltotrioside + H2O
2-chloro-4-nitrophenol + alpha-maltotrioside
-
acid-stable amylase and common neutral amylase can degrade the substrate at pH 5.4 to release 2-chloro-4-nitrophenol. In presence of 500 mM KSCN the reaction rate of common neutral amylase increases markedly whereas the reaction rate of acid-stable amylase decreases
-
-
?
2-chloro-4-nitrophenyl-alpha-maltotrioside + H2O
2-chloro-4-nitrophenol + alpha-maltotrioside
-
acid-stable amylase and common neutral amylase can degrade the substrate at pH 5.4 to release 2-chloro-4-nitrophenol. In presence of 500 mM KSCN the reaction rate of common neutral amylase increases markedly whereas the reaction rate of acid-stable amylase decreases
-
-
?
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside + H2O
p-nitrophenol + 4,6-ethyliden-[G7]-alpha-D-maltoheptaoside
-
-
-
-
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside + H2O
p-nitrophenol + 4,6-ethyliden-[G7]-alpha-D-maltoheptaoside
-
-
-
-
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside + H2O
p-nitrophenol + 4,6-ethyliden-[G7]-alpha-D-maltoheptaoside
-
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
?
alpha-cyclodextrin + H2O
?
-
9.2% of the activity with soluble starch
-
-
?
alpha-cyclodextrin + H2O
?
-
9.2% of the activity with soluble starch
-
-
?
alpha-cyclodextrin + H2O
?
-
the activity with alpha-cyclodextrin is 46% of the activity with starch in the same conditions at 0.5% (w/v) substrate concentrations
-
-
?
alpha-cyclodextrin + H2O
?
-
1.1% relative activity compared to amylose as substrate, pH 8.0. 65°C
-
-
?
alpha-cyclodextrin + H2O
?
-
catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
-
-
?
alpha-cyclodextrin + H2O
?
-
catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
-
-
?
alpha-cyclodextrin + H2O
?
-
13% activity compared to starch
-
-
?
amylopectin + H2O
?
69% of the activity with soluble starch
-
-
?
amylopectin + H2O
?
-
121% of the activity with soluble starch
-
-
?
amylopectin + H2O
?
62.2% activity compared to soluble starch
-
-
?
amylopectin + H2O
?
-
67.9% activity compared to gelatinized soluble starch
-
-
?
amylopectin + H2O
?
Geobacillus sp. IIPTN / MTCC 5319
-
86% activity compared to potato soluble starch
-
-
?
amylopectin + H2O
?
-
66.1% of the activity with soluble starch
-
-
?
amylopectin + H2O
?
-
66.1% of the activity with soluble starch
-
-
?
amylopectin + H2O
?
-
74.6% relative activity compared to amylose as substrate, pH 8.0. 65°C
-
-
?
amylopectin + H2O
?
liquefying enzyme. The main products of polysaccharide hydrolysis are G2 to G7. A small amount of G1 is formed after long hydrolysis periods. The enzyme A hydrolyzes long-chain oligosaccharides faster than shorter chain oligosaccharides
-
-
?
amylopectin + H2O
?
at 12% of the activity as compared to amylose
-
-
?
amylopectin + H2O
?
at 12% of the activity as compared to amylose
-
-
?
amylopectin + H2O
?
75% activity compared to soluble potato starch
-
-
?
amylopectin + H2O
?
75% activity compared to soluble potato starch
-
-
?
amylopectin + H2O
?
the enzyme shows a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7)
-
-
?
amylopectin + H2O
?
-
45.2% activity compared to soluble starch
-
-
?
amylopectin + H2O
fragments of amylopectin
-
90% of activity with starch
-
-
?
amylopectin + H2O
fragments of amylopectin
-
90% of activity with starch
-
-
?
amylopectin + H2O
malto-oligosaccharides
-
78% activity compared to starch
-
-
?
amylopectin + H2O
malto-oligosaccharides
-
73% activity compared to corn starch
-
-
?
amylopectin + H2O
maltooligosaccharides
-
from potato, 74% of activity with soluble starch
-
-
?
amylopectin + H2O
maltooligosaccharides
-
137% of activity with soluble starch
-
-
?
amylopectin + H2O
maltooligosaccharides
-
55% of activity with potato starch
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays a low degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays an intermediate degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
?
-
120% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays an intermediate degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays an intermediate degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
?
-
45.5% activity compared to gelatinized soluble starch
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays a high degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack decreases when temperature is raised
-
-
?
amylose + H2O
?
-
activity is 55% compared to the activity with soluble starch
-
-
?
amylose + H2O
?
-
the enzyme exhibits higher activity toward soluble starch rather than amylose (55%), amylopectin (41%), dextrin (60%), and glycogen (29%)
-
-
?
amylose + H2O
?
-
100% relative activity as reference for substrate specificity studies, pH 8.0. 65°C
-
-
?
amylose + H2O
?
liquefying enzyme. The main products of polysaccharide hydrolysis are G2 to G7. A small amount of G1 is formed after long hydrolysis periods. The enzyme A hydrolyzes long-chain oligosaccharides faster than shorter chain oligosaccharides
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays a high degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
?
-
pH 6.5, 37°C, inhibition studies with acarviosin-containing oligosaccharides
-
-
?
amylose + H2O
?
85% activity compared to soluble potato starch
-
-
?
amylose + H2O
?
85% activity compared to soluble potato starch
-
-
?
amylose + H2O
?
-
with potato amylose as substrate, the enzyme displays an intermediate degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
?
-
best substrate, 117.8% activity compared to soluble starch
-
-
?
amylose + H2O
?
-
best substrate, 117.8% activity compared to soluble starch
-
-
?
amylose + H2O
D-glucose + maltose + maltotriose + maltodextrins
-
best substrate for AmyC, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
amylose + H2O
D-glucose + maltose + maltotriose + maltodextrins
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
best substrate for AmyC, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
amylose + H2O
fragments of amylose
-
1.6times higher activity than with starch
-
-
?
amylose + H2O
fragments of amylose
-
1.6times higher activity than with starch
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate, hydrolysis of alpha-1,4-linkages
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate, hydrolysis of alpha-1,4-linkages
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate, hydrolysis of alpha-1,4-linkages
-
-
?
amylose + H2O
malto-oligosaccharides
-
78% activity compared to potato starch
-
-
?
amylose + H2O
malto-oligosaccharides
-
78% activity compared to potato starch
-
-
?
amylose + H2O
malto-oligosaccharides
-
145% activity compared to starch, the enzyme activity on the amylose as substrate is 1.98times greater than amylopectin
-
-
?
amylose + H2O
malto-oligosaccharides
-
preferred substrate
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate, hydrolysis of alpha-1,4-linkages
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate, hydrolysis of alpha-1,4-linkages
-
-
?
amylose + H2O
maltooligosaccharides
-
65% of activity with soluble starch
-
-
?
amylose + H2O
maltooligosaccharides
-
69% of activity with soluble starch
-
-
?
amylose + H2O
maltooligosaccharides
-
73% of activity with potato starch
-
-
?
amylose + H2O
maltose + D-glucose
0.5% substrate solution, best substrate
-
-
?
amylose + H2O
maltose + D-glucose
0.5% substrate solution, best substrate
-
-
?
beta-cyclodextrin + H2O
?
-
the activity with alpha-cyclodextrin is 48% of the activity with starch in the same conditions at 0.5% (w/v) substrate
-
-
?
beta-cyclodextrin + H2O
?
-
3.7% relative activity compared to amylose as substrate, pH 8.0. 65°C
-
-
?
beta-cyclodextrin + H2O
?
insight into the action of alpha-amylase at the molecular level
-
-
?
beta-limit-dextrin + H2O
D-glucose + maltose + maltotriose + maltodextrins
-
28% of the activity with amylose, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
beta-limit-dextrin + H2O
D-glucose + maltose + maltotriose + maltodextrins
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
28% of the activity with amylose, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
cassava starch + H2O
?
-
129% activity compared to potato soluble starch
-
-
?
cassava starch + H2O
?
Geobacillus sp. IIPTN / MTCC 5319
-
129% activity compared to potato soluble starch
-
-
?
corn flour + H2O
?
Geobacillus sp. IIPTN / MTCC 5319
-
58% activity compared to potato soluble starch
-
-
?
corn starch + H2O
?
-
62% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
corn starch + H2O
?
Geobacillus sp. IIPTN / MTCC 5319
-
107% activity compared to potato soluble starch
-
-
?
corn starch + H2O
maltose + maltotriose + maltotetraose
-
1% starch solution
-
-
?
corn starch + H2O
maltose + maltotriose + maltotetraose
1% starch solution
-
-
?
corn starch + H2O
maltose + maltotriose + maltotetraose
Geobacillus thermoleovorans MTCC 4220
1% starch solution
-
-
?
corn starch + H2O
maltose + maltotriose + maltotetraose
1% starch solution
-
-
?
dextrin + H2O
?
-
activity is 60% compared to the activity with soluble starch
-
-
?
dextrin + H2O
?
-
the enzyme exhibits higher activity toward soluble starch rather than amylose (55%), amylopectin (41%), dextrin (60%), and glycogen (29%)
-
-
?
dextrin + H2O
fragments of dextrin
-
7% of activity with starch
-
-
?
dextrin + H2O
fragments of dextrin
-
7% of activity with starch
-
-
?
dextrin + H2O
maltooligosaccharides
-
27% of activity with soluble starch
-
-
?
dextrin + H2O
maltooligosaccharides
-
catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
-
-
?
dextrin + H2O
maltooligosaccharides
-
catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies
-
-
?
gamma-cyclodextrin + H2O
?
-
2.6% relative activity compared to amylose as substrate, pH 8.0. 65°C
-
-
?
gamma-cyclodextrin + H2O
?
-
21% of the activity with soluble starch
-
-
?
gamma-cyclodextrin + H2O
?
-
lower activity with isozyme AI-2, no activity with isozymes AI-1 and AII
-
-
?
gamma-cyclodextrin + H2O
?
at 3.9% of the activity as compared to amylose
-
-
?
gamma-cyclodextrin + H2O
?
at 3.9% of the activity as compared to amylose
-
-
?
gamma-cyclodextrin + H2O
?
-
39.1% activity compared to soluble starch
-
-
?
gamma-cyclodextrin + H2O
?
-
39.1% activity compared to soluble starch
-
-
?
glycogen + H2O
?
32% of the activity with soluble starch
-
-
?
glycogen + H2O
?
-
glycogen from Ascaris suum, intestine and muscle alpha-amylase
-
-
?
glycogen + H2O
?
-
glycogen from rabbit or Ascaris suum, intestine and muscle alpha-amylase
-
-
?
glycogen + H2O
?
-
104% of the activity with soluble starch
-
-
?
glycogen + H2O
?
-
activity is 29% compared to the activity with soluble starch
-
-
?
glycogen + H2O
?
-
the enzyme exhibits higher activity toward soluble starch rather than amylose (55%), amylopectin (41%), dextrin (60%), and glycogen (29%)
-
-
?
glycogen + H2O
?
-
16.7% relative activity compared to amylose as substrate, pH 8.0. 65°C
-
-
?
glycogen + H2O
?
liquefying enzyme. The main products of polysaccharide hydrolysis are G2 to G7. A small amount of G1 is formed after long hydrolysis periods. The enzyme A hydrolyzes long-chain oligosaccharides faster than shorter chain oligosaccharides
-
-
?
glycogen + H2O
?
the enzyme can degrade both alpha-1,4 and alpha-1,6-linkages of alpha-glucan
-
-
?
glycogen + H2O
fragments of glycogen
-
7% of activity with starch
-
-
-
glycogen + H2O
fragments of glycogen
-
7% of activity with starch
-
-
-
glycogen + H2O
malto-oligosaccharides
-
14% activity compared to starch
-
-
?
glycogen + H2O
malto-oligosaccharides
-
81% activity compared to corn starch
-
-
?
glycogen + H2O
malto-oligosaccharides
-
substrate from oyster
-
-
?
glycogen + H2O
maltooligosaccharides
-
from bovine muscle, 58% of activity with soluble starch
-
-
?
glycogen + H2O
maltooligosaccharides
-
69% of activity with soluble starch
-
-
?
glycogen + H2O
maltose
-
49.5% of the activity with starch
main product
-
?
maltodextrin + H2O
?
87.6% activity compared to soluble starch
-
-
?
maltodextrin + H2O
maltooligosaccharides
-
100% of activity with potato starch
-
-
?
maltoheptaose + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose
-
-
-
-
?
maltoheptaose + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose
-
43% of activity with potato starch
-
-
?
maltopentaose + H2O
malto-oligomers + maltose
-
preferred substrate
-
-
?
maltotetraose + H2O
maltotriose + maltose
-
-
identified by thin-layer-chromatography
-
?
maltotetraose + H2O
maltotriose + maltose
-
46% of activity with potato starch
-
-
?
maltotriose + H2O
?
-
lower activity with isozyme AII, no activity with isozymes AI-1 and AI-2
-
-
?