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Enzyme Nomenclature
Information on EC 3.2.1.1 - alpha-amylase
for references in articles please use BRENDA:EC3.2.1.1
Word Map on EC 3.2.1.1
- 3.2.1.1
- wheat
- subtilis
- aspergillus
- gland
- cortisol
- maltose
- pancreas
- oryzae
- glycogen
- granule
-
lipase
-
acid-schiff
- alpha-glucosidase
-
flour
-
amylolytic
- glucoamylase
- aleurone
- grain
- amylose
- cereal
- parotid
- amyloliquefaciens
- amylopectin
- phaseolus
- acarbose
-
sympathetic
- beta-amylase
- endosperm
-
gibberellic
-
acinar
- stearothermophilus
-
psychological
-
alcian
- cyclodextrins
-
bread
-
psychosocial
- amyloglucosidase
-
transglycosylation
- dextrin
-
hypothalamic-pituitary-adrenal
- honey
- isoamylase
-
bake
-
pas-positive
- pullulanase
- pullulan
-
debranching
-
dough
-
liquefaction
-
saccharification
- pharmacology
- nutrition
- synthesis
- food industry
- analysis
- detergent
- brewing
- biotechnology
- agriculture
- industry
- medicine
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
3.2.1.1
-
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RECOMMENDED NAME
GeneOntology No.
alpha-amylase
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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
hydrolysis of O-glycosyl bond
-
-
endohydrolysis
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from geothermal soil located on Mount Rittmann, Antartica
-
-
Anoxybacillus amylolyticus MR3CT / ATCC BAA-872 / DSM 15939
isolated from geothermal soil located on Mount Rittmann, Antartica
-
-
Bacillus sp. (in: Bacteria) KSM-1378
and strains CCM 2267, CCM 2268, CCM 2744, CCM 2794, NA 64, CCM 2722, CCM 2216 and CCM 1718
-
-
active site residues Asp214, Glu250, and Asp315, as well as the residues making up the calcium (Asn118, Arg175, Asp184, and His218) and chloride (Arg212, Asn313, and Arg351) binding sites are fully conserved in HdAmyI; disk abalone
UniProt
entomopathogenic parasitic nematode, strain EGG, three isozymes
-
-
a strain belonging to the amylolytic lactic acid bacteria, plasmid encoded gene amy+
-
-
a strain belonging to the amylolytic lactic acid bacteria, plasmid encoded gene amy+
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desert and oasis flies studied, male and female, Neot Hakikar (oasis), Jordan Valley spring (wet), Kfar Adumim starved (arid), Jordan Valley autumn (arid)
-
-
gene for alpha-amylase from Debaryomyces occidentalis was integrated into genome of Saccharomyces cerevisiae
-
-
maize weevil, insecticide-susceptible, resistant no-cost, and resistant cost strains
-
-
isolated from compost soils collected in Taiwan
UniProt
wild-type enzyme and mutant enzymes D206E, D206N, K209F, K209R, E230D, E230Q, S297E, D297N
-
-
-
393406, 393424, 654220, 654581, 664049, 664793, 665150, 665673, 678567, 680534, 701764, 705097, 730179
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hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylase
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-
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393369, 393378, 393404, 393406, 393413, 393417, 393424, 393463, 654220, 658791, 664440, 664793, 665673, 677633, 678567, 680203, 691454, 701764, 717983, 729660
-
-
hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylase
-
-
-
393406, 393411, 393448, 393451, 655521, 657151, 657239, 678760, 682696, 694839, 704750, 717451, 717670, 717883
-
-
-
393366, 393379, 393391, 393405, 393406, 393415, 393455, 393457, 393461, 665673, 677738, 677791, 678567, 701764
-
-
and strains CCM 2267, CCM 2268, CCM 2744, CCM 2794, NA 64, CCM 2722, CCM 2216 and CCM 1718
-
-
wild-type enzyme and mutant enzymes D176N, H180N, E203Q, E208Q and D269N
-
-
-
-
-
wild-type enzyme and mutant enzymes Y63C, R232K, R232W, D234G, H238D, H238N, H238Y, E264V, Y265F, Y265S, D331A, D331E, N329D, N329K, N329V
-
-
strains HRO1 and HRO10, isolated from soil by enrichment on starch at 60°C
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NP 54, isolated from a water sample collected from the hot water spring of the Waimangu volcanic valley in New Zealand
-
-
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393389, 393395, 393396, 393397, 393398, 393399, 393424, 393427, 393433, 393435, 393442, 393458, 393466, 393473, 393474, 393475, 393476, 654363, 654643, 663543, 663880, 664793, 677569, 680292, 691113, 691795, 693546, 695047, 705589, 730802
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-
wild-type enzyme and mutant enzymes H93B, S180N, E205Q, H290N, D291N, W279A
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-
wild-type enzyme and mutant enzymes Y83F, Y83L, Y83N, Y83W, W84F, W84L, W84Y, K210N, K210R
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coexpressed in a construct in Corynebacterium glutamicum, combined with Escherichia coli K-12 lysine decarboxylase for an one-step production of cadaverine
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gene for alpha-amylase from Debaryomyces occidentalis was integrated into genome of Saccharomyces cerevisiae
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-
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393377, 393389, 393424, 656528, 664793, 665673, 666544, 678567, 682444, 691647, 692652, 694610, 704143
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a Gram-negative bacterium. alpha-Amylase production is highly dependent on starch availability and is supressed in the presence of glucose or other reducing sugars whereas the transformed Xanthomonas expressing the hyperthermophilic alpha-amylase from Pyrococcus woesei produces similar levels of recombinant alpha-amylase activity, regardless of the carbon source present in growth medium
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
malfunction
-
construction of the alpha-amylase deletion strain. Inactivation of the amyA gene results in a complete loss of activity, suggesting that the same protein is responsible for the alpha-amylase activity at both locations, extracellular and intracellular
malfunction
-
construction of the alpha-amylase deletion strain. Inactivation of the amyA gene results in a complete loss of activity, suggesting that the same protein is responsible for the alpha-amylase activity at both locations, extracellular and intracellular
-
physiological function
-
alpha-amylases catalyze the hydrolysis of internal alpha-D-(1,4)-glucosidic linkages in starch, glycogen, and related oligo- and polysaccharides to produce maltodextrins, maltooligosaccharides, and glucose
physiological function
SusG is the alpha-amylase expressed concomitantly with Sus-CDEF on the outer surface of the cell and is absolutely required for growth on starch
physiological function
the alpha-amylase is essential for growth on starch, glycogen, and pullulan
physiological function
comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism
physiological function
comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism
physiological function
-
comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism
physiological function
comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism
physiological function
-
alpha-amylases catalyze the hydrolysis of internal alpha-D-(1,4)-glucosidic linkages in starch, glycogen, and related oligo- and polysaccharides to produce maltodextrins, maltooligosaccharides, and glucose
-
physiological function
-
the alpha-amylase is essential for growth on starch, glycogen, and pullulan
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additional information
-
enzyme modification using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride in the presence of a nucleophile, AME, to activate the carboxyl groups of the enzyme, comparisons in anion and cation exchange chromatographies and by native PAGE, overview. The modifications project into the bulk solvent. The enhanced thermostability leads to increased productivity
additional information
determination of the structure of carbohydrate binding CBM58-binding site, the active site, and the surface starch-binding site, directly adjacent to the reducing end of the active site
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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 + maltotriose
-
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans
-
-
?
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
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
-
?
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
-
-
?
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
-
?
pullulan + H2O
panose + maltoheptaose
-
cyclomaltodextrinase activity
-
-
?
raw starch + H2O
malto-oligosaccharides
-
isozymes RBSA-1 and BSA-2, raw starch from corn and potato, the latter is preferred
-
-
?
raw starch + H2O
maltooligosaccharides
-
raw starch from corn, 20% of activity with soluble starch
-
-
?
Remazol Brilliant Blue dyed starch + H2O
malto-oligosaccharides
-
-
-
?
Remazol Brilliant Blue-dyed starch + H2O
malto-oligosaccharides
-
-
-
?
soluble potato starch + H2O
maltotriose + maltose + maltotetraose
-
major products of the enzymatic reaction with starch as substrate
-
?
soluble starch + H2O
maltose
Morimus funereus
-
maximal activity is achieved with horse-radish starch, undetectable activity towards 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
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 sorghum starch + H2O
?
-
62% activity compared to potato soluble starch
-
-
?
tapioca root starch + H2O
?
-
88% activity compared to potato soluble starch
-
-
?
wheat starch + H2O
?
-
56.5% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
wheat starch + H2O
maltohexaose + maltopentaose + maltotriose
-
78% activity compared to potato starch
major end-products of starch hydrolysis
-
?
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
-
-
?
amylopectin + H2O
?
Q6WUB6;
69% of the activity with soluble starch
-
-
?
amylopectin + H2O
?
-
121% of the activity with 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
?
the enzyme shows a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7)
-
-
?
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
?
Q6WUB6;
61% of the activity with soluble 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
?
-
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
?
-
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
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
-
-
?
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
-
-
?