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Information on EC 3.2.1.1 - alpha-amylase and Organism(s) Homo sapiens and UniProt Accession P04745

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IUBMB 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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Homo sapiens
UNIPROT: P04745
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-amylase 1
P04745
-
AMY1
P04745
-
HSA
P04745
-
HSAmy
P04745
-
HSAmy-ar
P04745
multiple mutant enzyme
1,4-alpha-D-glucan glucanohydrolase
-
-
-
-
alpha-amylase
-
type IX-A
Alpha-amylase carcinoid
-
-
-
-
alpha-amylase HA
-
-
Amy c6
-
-
-
-
AMY1
-
-
-
-
Amylase THC 250
-
-
-
-
amylase, alpha-
-
-
-
-
Amylopsin
-
-
-
-
Bactosol TK
-
-
-
-
Buclamase
-
-
-
-
Clarase
-
-
-
-
Clone 103
-
-
-
-
Clone 168
-
-
-
-
Clone PHV19
-
-
-
-
Clones GRAMY56 and 963
-
-
-
-
diastase
-
-
-
-
endoamylase
-
-
-
-
Fortizyme
-
-
-
-
G 995
-
-
-
-
glycogenase
-
-
-
-
HAS
-
human salivary alpha-amylase
High pI alpha-amylase
-
-
-
-
human salivary alpha-amylase
-
commercial preparation
Isozyme 1B
-
-
-
-
Kleistase L 1
-
-
-
-
Low pI alpha-amylase
-
-
-
-
Maxamyl
-
-
-
-
Maxilase
-
-
-
-
Meiotic expression upregulated protein 30
-
-
-
-
Pancreatic alpha-amylase
-
-
-
-
Pivozin
-
-
-
-
Ptyalin
-
-
-
-
Spitase CP 1
-
-
-
-
TAA
-
-
-
-
Taka-amylase A
-
-
-
-
Takatherm
-
-
-
-
Thermamyl
-
-
-
-
Thermolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
show the reaction diagram
the active site structure involves the catalytic residues D197, E233, and D300, reaction mechanism
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-90-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
maltoheptaoside + H2O
?
show the reaction diagram
P04745
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
-
-
?
maltopentaoside + H2O
?
show the reaction diagram
P04745
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
-
-
?
starch + H2O
?
show the reaction diagram
P04745
25°C, pH 6.9
-
-
?
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
show the reaction diagram
-
-
the increase of absorbance of 2-chloro-4-nitrophenol liberated by HSA is measured continuously at 400 nm
-
?
2-chloro-4-nitrophenyl alpha-D-maltotrioside + H2O
?
show the reaction diagram
-
-
-
?
2-chloro-4-nitrophenyl alpha-maltotrioside + H2O
?
show the reaction diagram
-
-
-
?
2-chloro-4-nitrophenyl-4-O-beta-D-galactopyranosyl-maltoside + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
commercial substrate for a flourescence-based assay, pH 7.0
-
-
?
4-nitrophenyl maltoheptaoside + H2O
maltotriose + maltotetraose + 4-nitrophenyl maltotetraoside + 4-nitrophenyl maltotrioside
show the reaction diagram
-
-
-
?
alpha-maltosyl fluoride + H2O
maltose + fluoride
show the reaction diagram
-
-
-
-
?
alpha-maltotriosyl fluoride + H2O
maltotriose + fluoride
show the reaction diagram
amylose + H2O
malto-oligosaccharides
show the reaction diagram
malto-oligosaccharides + H2O
maltose
show the reaction diagram
-
hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
maltopentaose + H2O
maltotriose + maltose
show the reaction diagram
-
-
major products
-
?
maltosyl fluoride + H2O
maltose + fluoride
show the reaction diagram
-
-
-
?
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside + H2O
?
show the reaction diagram
-
-
-
-
?
starch + H2O
?
show the reaction diagram
starch + H2O
fragments of starch
show the reaction diagram
-
-
-
-
?
starch + H2O
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
amylose + H2O
malto-oligosaccharides
show the reaction diagram
starch + H2O
?
show the reaction diagram
-
salivary alpha-amylase digests a portion of ingested starch in the stomach before it enters the intestine and is exposed to pancreatic amylase. A role of salivary alpha-amylase is bacterial clearance from the mouth and prevention of bacterial attachment to oral surfaces
-
-
?
starch + H2O
fragments of starch
show the reaction diagram
-
-
-
-
?
starch + H2O
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sorghum procyanidin tetramer
P04745
thermodynamics, and binding and inhibition kinetics, overview
-
1,2,3,4,6-pentagalloyl-beta-D-glucose
-
mixed non-competitive inhibition, KEI: 0.0026 mM, KEIS: 0.0039 mM, tested in a concentration range of 0.04 to 0.5 mM, reduced inhibitory efficiency of the mutants W58L and Y151M with 92 and 97% remaining enzyme activity at 0.00235 mM inhibitor concentration, respectively, pH 6.0, 37°C
acacetin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 14.1% maximum inhibition
acarbose
acarviosine-glucose
binding mechanism, resistance to rearrangement, enzyme-inhibitor complex crystal structure analysis
acarviostatin 103
-
component isolated from Streptomyces sp. strain PW638, also inhibitory to alpha-glucosidase, EC 3.2.1.3
alpha-acarviosinyl-1,4-alpha-D-glucopyranosyl-1,6-D-glucopyranosylidene-spiro-thiohydantoin
-
i.e. PTS-G-TH, mixed-competitive type inhibition
catechin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 13.1% maximum inhibition
Cl-
-
above 100 mM
daidzein
-
a isoflavone, 0.888 mM, pH 6.0, room temperature, 23.3% maximum inhibition
diosmetin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 19.2% maximum inhibition
epicatechin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 10.3% maximum inhibition
ethyl caffeate
-
pH 7.0
eupafolin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 99.4% maximum inhibition
fisetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 85.6% maximum inhibition
genistein
-
a isoflavone, 0.888 mM, pH 6.0, room temperature, 25.1% maximum inhibition
genkwanin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 17.5% maximum inhibition
glucopyranosylidene-spiro-thiohydantoin
-
i.e. G-TH, mixed-competitive type inhibition
hesperetin
-
a flavanone, 0.888 mM, pH 6.0, room temperature, 39.8% maximum inhibition
isoacarbose
binding mechanism, resistance to rearrangement, enzyme-inhibitor complex crystal structure analysis, binding highly perturbs catalytic residue D300
isorhamnetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 35.4% maximum inhibition
kaempferol
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 34.5% maximum inhibition
luteolin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 88.8% maximum inhibition
montbretin A
-
glycosylated acyl-flavonols, originally isolated from an extract of Crocosmia crocosmiiflora, measured in the presence and in the absence of 5 mM dithiothreitol, competitive inhibitor, more effective than montbretin B and C due to its free meta-hydroxyl group of the cinnamic acid moiety
montbretin B
-
glycosylated acyl-flavonols, originally isolated from an extract of Crocosmia crocosmiiflora, less effective than montbretin A due to the hydroxy group of montbretin A in the cinnamic acid moiety, respnsible for the tight binding
montbretin C
-
glycosylated acyl-flavonols, a methyl ether of the cinnamic acid moiety, originally isolated from an extract of Crocosmia crocosmiiflora, less effective than montbretin A due to the hydroxy group of montbretin A in the cinnamic acid moiety, respnsible for the tight binding
myricetin
naringenin
-
a flavanone, 0.888 mM, pH 6.0, room temperature, 26.9% maximum inhibition
polyethylene glycol 400
-
1500 Da PEG, inhibits the enzyme activity by 14% at 0.02% w/v
-
protein EDI-1
-
the alpha-amylase inhibitory fraction from Triticum dicoccon Schrank composed of emmer dimeric inhibitor 1 (EDI-1) and emmer dimeric inhibitor 2 (EDI-2) sharing very high identity levels with related proteins from Triticum aestivum
-
protein EDI-2
-
the alpha-amylase inhibitory fraction from Triticum dicoccon Schrank composed of emmer dimeric inhibitor 1 (EDI-1) and emmer dimeric inhibitor 2 (EDI-2) sharing very high identity levels with related proteins from Triticum aestivum
-
quercetagetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 97.6% maximum inhibition
quercetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 82.1% maximum inhibition
Rhamnetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 8.1% maximum inhibition
scutellarein
-
a flavone, 0.888 mM, pH 6.0, room temperature, 98.4% maximum inhibition
Vigna unguiculata defensin
-
i.e. VuD1, plant defensins are small protein consisting of 45-54 amino acids, ca. 38% inhibition with 0.1 mg/ml inhibitor, pH 6.5, 37°C
-
wheat amylase inhibitor
-
alpha-amylase inhibitor from wheat kernel, purification
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Br-
greater affinity for the enzyme than chloride and a comparable relative activity
Cl-
allosteric activation. The enzyme is essentially inactive in the absence of chloride ion
ClO3-
activates, optimal concentration is 0.2 mM
HCOO-
activates, optimal concentration is 1 mM
I-
lower affinity for the enzyme than chloride and higher relative activity
N3-
activates, optimal concentration is 1 mM
NO2-
activates, optimal concentration is 1 mM
NO3-
activates, optimal concentration is 0.1 mM
polyethylene glycol 1000
-
1500 Da PEG, increases the enzyme activity by 43% at 0.02% w/v
polyethylene glycol 1500
-
1500 Da PEG, increases the enzyme activity by 39% at 0.02% w/v
-
polyethylene glycol 2000
-
1500 Da PEG, increases the enzyme activity by 34% at 0.02% w/v
polyethylene glycol 4600
-
1500 Da PEG, increases the enzyme activity by 29% at 0.02% w/v
polyethylene glycol 600
-
1500 Da PEG, increases the enzyme activity by 33% at 0.02% w/v
polyethylene glycol 8000
-
1500 Da PEG, increases the enzyme activity by 40% at 0.02% w/v
polyvinyl alcohol
-
10 kDa: increases the enzyme activity by 40% at 0.02% w/v, 50 kDa: increases the enzyme activity by 42% at 0.02% w/v
Triton X-100
-
increases the enzyme activity by 45% at 0.02% w/v
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.45 - 1.3
2-chloro-4-nitrophenyl alpha-maltotrioside
3.6
2-chloro-4-nitrophenyl-alpha-D-maltotrioside
-
commercial substrate, pH 7.0
4.5
alpha-maltosyl fluoride
-
30°C, pH 7.0
0.51
alpha-maltotriosyl fluoride
-
30°C, pH 7.0
0.06 - 0.27
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.98
2-chloro-4-nitrophenyl alpha-D-maltotrioside
pH 7.0, 30°C
1.9 - 15.8
2-chloro-4-nitrophenyl alpha-maltotrioside
443
alpha-maltosyl fluoride
-
30°C, pH 7.0
283 - 285
alpha-maltotriosyl fluoride
150
maltosyl fluoride
pH 7.0, 30°C
8.5 - 175
p-nitrophenylhexa[alpha-D-glucopyranosyl(1-4)]-alpha-D-glucopyranoside
additional information
additional information
-
KM-values of wild-type and mutant enzymes
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00235
1,2,3,4,6-pentagalloyl-beta-D-glucose
-
pH 6.0, 37°C, the mutants Y151M and W58L exhibit reduced inhibitory efficiency with 92 and 97% remaining enzyme activity at 0.00235 mM inhibitor concentration, respectively, pH 6.0, 37°C
0.0013
ethyl caffeate
-
pH 7.0, uncompetitive inhibition
0.0000081
montbretin A
-
pH 7.0, in presence of 1 mM CaCl2
0.0036
montbretin B
-
pH 7.0, in presence of 1 mM CaCl2
0.0061
montbretin C
-
pH 7.0, in presence of 1 mM CaCl2
0.11
myricetin
-
pH 7.0, competitive inhibition
additional information
additional information
-
inhibition kinetics, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000996
acarbose
Homo sapiens
-
pH 6.0, room temperature
0.048
eupafolin
Homo sapiens
-
a flavone, pH 6.0, room temperature
0.0196
fisetin
Homo sapiens
-
a flavonol, pH 6.0, room temperature
0.0184
luteolin
Homo sapiens
-
a flavone, pH 6.0, room temperature
0.0302
myricetin
Homo sapiens
-
a flavonol, pH 6.0, room temperature
0.0102
quercetagetin
Homo sapiens
-
a flavonol, pH 6.0, room temperature
0.0214
quercetin
Homo sapiens
-
a flavonol, pH 6.0, room temperature
0.00964
scutellarein
Homo sapiens
-
a flavone, pH 6.0, room temperature
additional information
acarviostatin 103
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110.94
P04745
commercial enzyme preparation, solution, pH 6.9, 37°C
55.77
P04745
commercial enzyme preparation, solution, pH 6.9, 37°C, in presence of 4 mg/ml Sorghum procyanidin tetramer
5500
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
P04745
assay at
5.5
-
assay at
6
-
assay at
6.5
-
assay at
6.9 - 7.1
-
-
7 - 8.5
-
hydrolysis of alpha-maltotriosyl fluoride
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
P04745
assay at
37
P04745
assay at
30
assay at
37
-
assay at
6
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 7.6
P04745
identification of several isozymes in salivary gland by two-dimensional gel electrophoresis and mass spectrometry analysis, detailed overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is secreted
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
P04745
the enzyme belongs to the glycosyl hydrolase family 13, GH13
physiological function
P04745
as one of receptors of the acquired membrane, human salivary alpha-amylase (HSA) plays an important role in the formation of caries. The conformation of the enzyme is altered in the presence of SPC-tetramer. The conformation changes of enzyme HSA might contribute to the reduction of the adhesion of cariogenic bacteria and finally decrease the occurrence of dental caries. Preventive effect of Sorghum procyanidins on dental caries
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
-
x * 54000, pancreatic enzyme, SDS-PAGE
55000
-
x * 55000, non-glycosylated alpha-amylase
56000
56091
-
x * 56091, deduced from nucloeotide sequence
56095
-
x * 56095, mass spectrometry
56133
-
1 * 56133, isoenzymes of family B, SDS-PAGE
61856
-
1 * 61856, isoenzymes of family A, SDS-PAGE
62000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
P04745
glycosylation pattern analysis of isozymes, overview
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HSAmy and HSAmy-ar both show characteristics of a protein with ordered secondary structures, suggesting that the overall conformation of HSamy still retains in the mutant HSAmy-ar. Single or double mutations also do not alter the overall conformation of the enzyme
P04745
crystals of wild-type and F256W mutant alpha-amylase, crystals diffract to 2.1 a resolution
-
enzyme from salivary gland
-
enzyme in complex with carbohydrate and proteinaceous inhibitors
-
purified dimeric enzyme, hanging drop vapour diffusion method, 0.001 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, is mixed with 0.001 ml of precipitation solution, three different successful variations, overview, 1 week, X-ray diffraction structure determination and analysis at 3.0 A resolution
-
purified recombinant wild-type pancreatic enzyme, in complex with inhibitors acarbose, isoacarbose, or acarviosine-glucose, hanging drop vapour diffusion method, 0.005 ml of protein solution containing 16.3 mg/ml protein is mixed with 0.005 ml of reservoir solution containing 60% 2-methyl-2,4-pentanediol and 100 mM cacodylate, pH 7.5, 1 month, X-ray diffraction structure determination and analysis at 1.9-2.2 A resolution
recombinant wild-type and N298S variant HPAs are crystallized using the hanging drop vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
W134A/W203A/Y276A/W284A/W316A/W388A
P04745
HSAmy-ar, multiple mutant, 10fold reduction of activity compared with wild-type enzyme and also sigificant reductaion of starch binding activity
W203A
P04745
2fold reduction of activity compared to the wild-type enzyme, similar starch-binding activity like the wild-type enzyme
W284A
P04745
similar specific activity and similar starch-binding activity like the wild-type enzyme
W316A/W388A
P04745
similar specific activity and similar starch-binding activity like the wild-type enzyme
Y276/W284A
P04745
similar specific activity and similar starch-binding activity like the wild-type enzyme
Y276A
P04745
similar specific activity and similar starch-binding activity like the wild-type enzyme
D197A
-
no activity
D197N
-
no activity
D300A
-
0.0005% of wild-type starch hydrolyzing activity
D300N
-
0.0005% of wild-type starch hydrolyzing activity
E233A
-
0.005% of wild-type starch hydrolyzing activity
E233A/D300A
-
0.001% of wild-type starch hydrolyzing activity
E233Q
-
0.0005% of wild-type starch hydrolyzing activity
N298S
variant of the enzyme has an approximate 200fold reduction in affinity for chloride ion
W58L
-
reduced inhibitory efficiency of the mutants W58L and Y151M with 92 and 97% remaining enzyme activity at 0.00235 mM pentagalloyl glucose inhibitor concentration, respectively, pH 6.0, 37°C
Y151M
-
reduced inhibitory efficiency of the mutants W58L and Y151M with 92 and 97% remaining enzyme activity at 0.00235 mM pentagalloyl glucose inhibitor concentration, respectively, pH 6.0, 37°C
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
30 min, about 80% loss of the activity of isoenzymes A and B, complete inactivation after 90 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
resistant to protease denaturation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4°C or -20°C, stable for months
-
4°C or -20°C, parotid enzyme is extremely stable for several months, pancreatic enzyme is stable for 7-9 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
accidental co-purification of the native alpha-amylase with carbonic anhydrase VI from saliva by 4-aminobenzenesulfonamide affinity chromatography
-
recombinant alpha-amylase
-
recombinant alpha-amylase, Phenyl Sepharose, Q-Sepharose
-
recombinant protein, expression and purification carried out using a Bac-To-Bac Baculovirus Expression System
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression and purification carried out using a Bac-To-Bac Baculovirus Expression System
-
expression in Pichia pastoris
-
expression in Sf9 insect cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
the inhibition of alpha-amylase can significantly reduce the post-prandial increase of blood glucose and therefore can be an important strategy in the management of blood glucose level in type 2 diabetic and borderline patients
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Buonocore, V.; De Biasi, M.G.; Giardina, P.; Poerio, E.; Silano, V.
Purification and properties of an alpha-amylase tetrameric inhibitor from wheat kernel
Biochim. Biophys. Acta
831
40-48
1985
Gallus gallus, Homo sapiens, Sus scrofa, Tenebrio molitor
-
Manually annotated by BRENDA team
Pierre, K.J.; Tung, K.K.
alpha-Amylase. UV-method with maltotetraose
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
4
146-151
1984
Homo sapiens
-
Manually annotated by BRENDA team
Rauscher, E.
alpha-Amylase. UV-method with maltoheptaose
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
4
152-157
1984
Homo sapiens
-
Manually annotated by BRENDA team
Rauscher, E.
alpha-Amylase. Colorimetric method
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
4
157-161
1984
Homo sapiens
-
Manually annotated by BRENDA team
Wahlefeld, A.W.
alpha-Amylase. Determination with coloured insoluble substrates
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
4
161-167
1984
Homo sapiens
-
Manually annotated by BRENDA team
Foo, Y.; Rosalki, S.B.
Isoenzymes of alpha-amylase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
4
167-177
1984
Homo sapiens
-
Manually annotated by BRENDA team
Svensson, B.
Protein engineering in the alpha-amylase family: catalytic mechanism, substrate specificity and stability
Plant Mol. Biol.
25
141-157
1994
Aspergillus oryzae, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus licheniformis, Drosophila melanogaster, Escherichia coli, Saccharomycopsis fibuligera, Homo sapiens, Hordeum vulgare, Mus musculus, Oryza sp., Vigna radiata, Streptomyces hygroscopicus, Sus scrofa, Triticum aestivum, Xanthomonas campestris
Manually annotated by BRENDA team
Rick, W.; Stegbauer, H.P.
alpha-Amylase. Messung der reduzierenden Gruppen
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
919-923
1974
Homo sapiens
-
Manually annotated by BRENDA team
Stiefel, D.J.; Keller, P.J.
Preparation and some properties of human pancreatic amylase including a comparison with human parotid amylase
Biochim. Biophys. Acta
302
345-361
1973
Homo sapiens
Manually annotated by BRENDA team
Keller, P.J.; Kauffman, D.L.; Allan, B.A.; Williams, B.L.
Further studies on the structural differences between the isoenzymes of human parotid alpha-amylase
Biochemistry
10
4867-4874
1971
Homo sapiens
Manually annotated by BRENDA team
Hobbs, J.R.; Aw, S.E.
Messung nach elektrophoretischer Trennung
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
943-949
1974
Homo sapiens
-
Manually annotated by BRENDA team
Nahoum, V.; Roux, G.; Anton, V.; Rouge, P.; Puigserver, A.; Bischoff, H.; Henrissat, B.; Payan, F.
Crystal structures of human pancreatic alpha-amylase in complex with carbohydrate and proteinaceous inhibitors
Biochem. J.
346
201-208
2000
Homo sapiens
Manually annotated by BRENDA team
Bank, R.A.; Hettema, E.H.; Arwert, F.; Nieuw Amerongen, A.V.; Pronk, J.C.
Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase
Electrophoresis
12
74-79
1991
Homo sapiens
Manually annotated by BRENDA team
Rauscher, E.
Messung der Abbauprodukte Maltose und Glucose
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
923-927
1974
Homo sapiens
-
Manually annotated by BRENDA team
Wahlefeld, A.W.
Messung mit gefärbten unlösliche Substraten
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
927-931
1974
Homo sapiens
-
Manually annotated by BRENDA team
Street, H.V.
Messung des Jod-Stärke-Komplexes
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
931-936
1974
Cavia porcellus, Homo sapiens, Mus musculus, Rattus norvegicus
-
Manually annotated by BRENDA team
Hillmann, G.
Messung durch Endpunktbestimmung auf Papier
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
936-943
1974
Homo sapiens
-
Manually annotated by BRENDA team
Ramasubbu, N.; Sundar, K.; Ragunath, C.; Rafi, M.M.
Structural studies of a Phe256Trp mutant of human salivary alpha-amylase: implications for the role of a conserved water molecule in enzyme activity
Arch. Biochem. Biophys.
421
115-124
2004
Homo sapiens
Manually annotated by BRENDA team
Rydberg, E.H.; Li, C.; Maurus, R.; Overall, C.M.; Brayer, G.D.; Withers, S.G.
Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids
Biochemistry
41
4492-4502
2002
Homo sapiens
Manually annotated by BRENDA team
Fisher, S.Z.; Govindasamy, L.; Tu, C.; Agbandje-McKenna, M.; Silverman, D.N.; Rajaniemi, H.J.; McKenna, R.
Structure of human salivary alpha-amylase crystallized in a C-centered monoclinic space group
Acta Crystallogr. Sect. F
62
88-93
2006
Homo sapiens
Manually annotated by BRENDA team
Kandra, L.; Zajacz, A.; Remenyik, J.; Gyemant, G.
Kinetic investigation of a new inhibitor for human salivary alpha-amylase
Biochem. Biophys. Res. Commun.
334
824-828
2005
Homo sapiens
Manually annotated by BRENDA team
Li, C.; Begum, A.; Numao, S.; Park, K.H.; Withers, S.G.; Brayer, G.D.
Acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts
Biochemistry
44
3347-3357
2005
Homo sapiens (P04746), Homo sapiens
Manually annotated by BRENDA team
Yoon, S.; Robyt, J.F.
Activation and stabilization of 10 starch-degrading enzymes by Triton X-100, polyethylene glycols, and polyvinyl alcohols
Enzyme Microb. Technol.
37
556-562
2005
Aspergillus oryzae, Bacillus amyloliquefaciens, Bacillus licheniformis, Homo sapiens, Sus scrofa
-
Manually annotated by BRENDA team
Hirtz, C.; Chevalier, F.; Centeno, D.; Rofidal, V.; Egea, J.C.; Rossignol, M.; Sommerer, N.; Deville de Periere, D.
MS characterization of multiple forms of alpha-amylase in human saliva
Proteomics
5
4597-4607
2005
Homo sapiens (P04745), Homo sapiens
Manually annotated by BRENDA team
Granger, D.A.; Kivlighan, K.T.; el-Sheikh, M.; Gordis, E.B.; Stroud, L.R.
Salivary alpha-amylase in biobehavioral research: recent developments and applications
Ann. N. Y. Acad. Sci.
1098
122-144
2007
Homo sapiens
Manually annotated by BRENDA team
Maurus, R.; Begum, A.; Williams, L.K.; Fredriksen, J.R.; Zhang, R.; Withers, S.G.; Brayer, G.D.
Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity
Biochemistry
47
3332-3344
2008
Homo sapiens (P04746), Homo sapiens
Manually annotated by BRENDA team
Fontanini, D.; Capocchi, A.; Muccilli, V.; Saviozzi, F.; Cunsolo, V.; Saletti, R.; Foti, S.; Galleschi, L.
Dimeric inhibitors of human salivary alpha-amylase from emmer (Triticum dicoccon Schrank) seeds
J. Agric. Food Chem.
55
10452-10460
2007
Homo sapiens
Manually annotated by BRENDA team
Gyemant, G.; Zajacz, A.; Becsi, B.; Ragunath, C.; Ramasubbu, N.; Erdodi, F.; Batta, G.; Kandra, L.
Evidence for pentagalloyl glucose binding to human salivary alpha-amylase through aromatic amino acid residues
Biochim. Biophys. Acta
1794
291-296
2009
Homo sapiens
Manually annotated by BRENDA team
Tarling, C.A.; Woods, K.; Zhang, R.; Brastianos, H.C.; Brayer, G.D.; Andersen, R.J.; Withers, S.G.
The search for novel human pancreatic alpha-amylase inhibitors: high-throughput screening of terrestrial and marine natural product extracts
ChemBioChem
9
433-438
2008
Homo sapiens
Manually annotated by BRENDA team
Lo Piparo, E.; Scheib, H.; Frei, N.; Williamson, G.; Grigorov, M.; Chou, C.J.
Flavonoids for controlling starch digestion: structural requirements for inhibiting human alpha-amylase
J. Med. Chem.
51
3555-3561
2008
Homo sapiens
Manually annotated by BRENDA team
Ragunath, C.; Manuel, S.G.; Venkataraman, V.; Sait, H.B.; Kasinathan, C.; Ramasubbu, N.
Probing the role of aromatic residues at the secondary saccharide-binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding
J. Mol. Biol.
384
1232-1248
2008
Homo sapiens (P04745), Homo sapiens
Manually annotated by BRENDA team
Pelegrini, P.B.; Lay, F.T.; Murad, A.M.; Anderson, M.A.; Franco, O.L.
Novel insights on the mechanism of action of alpha-amylase inhibitors from the plant defensin family
Proteins
73
719-729
2008
Aspergillus fumigatus, Homo sapiens, Zabrotes subfasciatus, Acanthoscelides obtectus, Callosobruchus maculatus, Sus scrofa (P00690)
Manually annotated by BRENDA team
Tundis, R.; Loizzo, M.R.; Menichini, F.
Natural products as alpha-amylase and alpha-glucosidase inhibitors and their hypoglycaemic potential in the treatment of diabetes: an update
Mini Rev. Med. Chem.
10
315-331
2010
Homo sapiens
Manually annotated by BRENDA team
Meng, P.; Xie, C.; Geng, P.; Qi, X.; Zheng, F.; Bai, F.
Inhibitory effect of components from Streptomyces species on alpha-glucosidase and alpha-amilase of different origin
Prikl. Biokhim. Mikrobiol.
49
181-189
2013
Homo sapiens
Manually annotated by BRENDA team
Zhao, L.; Wang, F.; Lu, Q.; Liu, R.; Tian, J.; Huang, Y.
Study on interaction between human salivary alpha-amylase and Sorghum procyanidin tetramer binding characteristics and structural analysis
Int. J. Biol. Macromol.
118
1136-1141
2018
Homo sapiens (P04745)
Manually annotated by BRENDA team