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Information on EC 3.2.1.1 - alpha-amylase and Organism(s) Sus scrofa and UniProt Accession P00690

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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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Select one or more organisms in this record:
This record set is specific for:
Sus scrofa
UNIPROT: P00690
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The taxonomic range for the selected organisms is: Sus scrofa
Synonyms
1,4-alpha-D-glucan glucanohydrolase, 1,4-alpha-D-glucan glucanohydrolase and endoamylase, 1,4-alpha-D-glucan-glucanohydrolase, ABA, acid-stable amylase, acidic amylase, AGXA, AHA, alkaline alpha-amylase, alkalophilic Bacillus alpha-amylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-alpha-D-glucan glucanohydrolase
-
-
-
-
alpha-1,4-glucan-4-glucanohydrolase
249
-
alpha-amylase
249
-
Alpha-amylase carcinoid
-
-
-
-
alpha-amylase PPA
249
-
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
-
-
-
-
High pI alpha-amylase
-
-
-
-
Isozyme 1B
-
-
-
-
Kleistase L 1
-
-
-
-
LLF-alpha-amylase
295288
-
Low pI alpha-amylase
-
-
-
-
Maxamyl
-
-
-
-
Maxilase
-
-
-
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Meiotic expression upregulated protein 30
-
-
-
-
Pancreatic alpha-amylase
-
-
-
-
Pivozin
-
-
-
-
PPA-I
PPA-II
Ptyalin
-
-
-
-
Spitase CP 1
-
-
-
-
TAA
-
-
-
-
Taka-amylase A
-
-
-
-
Takatherm
-
-
-
-
Thermamyl
-
-
-
-
Thermolase
-
-
-
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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 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
-
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
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
show the reaction diagram
-
-
-
?
starch + H2O
?
show the reaction diagram
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-maltopentaoside + H2O
4-nitrophenol + alpha-D-maltopentaose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-maltoside + H2O
4-nitrophenol + alpha-D-maltose
show the reaction diagram
4-nitrophenol is bound at the ative site
-
-
?
4-nitrophenyl-alpha-D-maltoside + H2O
4-nitrophenol + maltose
show the reaction diagram
-
-
-
-
?
amylose + H2O
?
show the reaction diagram
amylose + H2O
malto-oligosaccharides
show the reaction diagram
glycogen + H2O
malto-oligosaccharides
show the reaction diagram
-
-
-
-
?
maltose + H2O
D-glucose + D-glucose
show the reaction diagram
-
-
-
-
?
starch + H2O
?
show the reaction diagram
starch + H2O
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
alpha-amylase hydrolyzes beta-cyclodextrin with difficulty, and fails to hydrolyze gamma-cyclodextrin to any appreciable extent
-
-
-
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
-
soluble substrate
-
-
?
glycogen + H2O
malto-oligosaccharides
show the reaction diagram
-
-
-
-
?
starch + H2O
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
alpha-amylase hydrolyzes beta-cyclodextrin with difficulty, and fails to hydrolyze gamma-cyclodextrin to any appreciable extent
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4',5,7-tetrahydroxyflavanone
-
identified in the Sysygium cumini seed extract which results in 98% inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
Acalpha indica leaf extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 15% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
acarbose
acarviostatin I03
-
pH 6.5, 37°C, mixed noncompetitive inhibition, substrate: soluble amlyose
acarviostatin II03
-
pH 6.5, 37°C, mixed noncompetitive inhibition, substrate: soluble amlyose
acarviostatin III03
-
pH 6.5, 37°C, mixed noncompetitive inhibition, substrate: soluble amlyose
acarviostatin IV03
-
pH 6.5, 37°C, mixed noncompetitive inhibition, substrate: soluble amlyose
Aegle marmelos leaf extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 6% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
alphaAI-PF
-
alpha amylase inhibitor from Palo Fierro seeds
-
amylase-inhibitor
-
14 kinds of alpha-amylase inhibitors from Streptomyces sp. No. 280
-
apigenin-7-glucoside
-
IC50 is 0.17 mM
betulinic acid
-
identified in the Sysygium cumini seed extract which results in 98% inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
caffeic acid
chlorogenic acid
corosolic acid
-
triterpene acid isolated from Lagerstroemia speciosa leaves, weak inhibitory activity
cynarin
-
IC50 is above 2.0 mM
dihydrocaffeic acid
-
IC50 is above 14.0 mM
ferulic acid
-
IC50 is above 5.0 mM
fisetin
-
IC50 is 0.44 mM
Gymnema sylvestre leaf extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 3% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
isochlorogenic acid
-
IC50 is 0.56 mM
Limonia acidissimia seed extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 20% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
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luteolin
-
IC50 is 0.17 mM
luteolin-7-glucoside
-
IC50 is 0.28 mM
Moringa oleifera leaf extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 16% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
Psidium guajava var. Pomiferum leaf extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 98% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
quinic acid
rosmarinic acid
-
IC50 is 1.4 mM
Sinapic acid
-
IC50 is above 6.7 mM
Sysygium cumini seed extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, phenolics, terpenoids, and alkaloids are identified, mass spectrometry revlealed the presence of betulinic acid and 3,5,7,4'-tetrahydroxyflavanone, 98% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
Tannic acid
-
IC50 is 0.14 mM
Tinospora cordifolia leaf extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 13% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
Trigonella foenum graecum seed extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 10% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
Vigna unguiculata defensin
-
i.e. VuD1, plant defensins are small protein consisting of 45-54 amino acids, ca. 12% inhibition with 0.1 mg/ml inhibitor, pH 6.5, 37°C, low inhibition activity in pig is probably related to extended loops in the structural core of the amylase, reducing the contact between defensin VuD1 and the catalytic site
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wheat amylase inhibitor
-
alpha-amylase inhibitor from wheat kernel, purification
-
Zizyphus mauritiana seed extract
-
herbal medicine for the treatment of diabetes in Ayurvedic system of medicine, 12% relative inhibition compared to control without the addition of medicinal plant extract, non-competitive inhibition determined by a Dixon plot, pH 6.9
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
neohesperidin dihydrochalcone
-
up to 3fold activation at 4.8 mM
polyethylene glycol 1000
-
1500 Da PEG, increases the enzyme activity by 45% at 0.02% w/v
polyethylene glycol 1500
-
1500 Da PEG, increases the enzyme activity by 54% at 0.02% w/v
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polyethylene glycol 2000
-
1500 Da PEG, increases the enzyme activity by 44% at 0.02% w/v
polyethylene glycol 4600
-
1500 Da PEG, increases the enzyme activity by 41% at 0.02% w/v
polyethylene glycol 600
-
1500 Da PEG, increases the enzyme activity by 27% at 0.02% w/v
polyethylene glycol 8000
-
1500 Da PEG, increases the enzyme activity by 38% at 0.02% w/v
polyvinyl alcohol
-
10 kDa: increases the enzyme activity by 36% at 0.02% w/v, 50 kDa: increases the enzyme activity by 28% at 0.02% w/v
Triton X-100
-
increases the enzyme activity by 41% at 0.02% w/v
additional information
-
no activation by polyethylene glycol 400 0.02% w/v
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.065
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
-
pH not specified in the publication, 25°C
0.065
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
-
25°C, pH 7.2
4.48 - 4.63
4-nitrophenyl-alpha-D-maltoside
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
291
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
-
pH not specified in the publication, 25°C
0.017 - 518
starch
141 - 291
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
0.0494 - 0.0497
4-nitrophenyl-alpha-D-maltoside
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4500
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
-
pH not specified in the publication, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0021
acarbose
-
pH 6.5, 37°C, mixed noncompetitive inhibition, Ki' (dissociation constant of the enzyme-substrate-inhibitor-complex): 0.0021 mM, substrate: soluble amlyose
0.000346
acarviostatin I03
-
pH 6.5, 37°C, mixed noncompetitive inhibition, Ki' (dissociation constant of the enzyme-substrate-inhibitor-complex): 0.008057 mM, substrate: soluble amlyose
0.000013
acarviostatin II03
-
pH 6.5, 37°C, mixed noncompetitive inhibition, Ki' (dissociation constant of the enzyme-substrate-inhibitor-complex): 0.000018 mM, substrate: soluble amlyose
0.000008
acarviostatin III03
-
pH 6.5, 37°C, mixed noncompetitive inhibition, Ki' (dissociation constant of the enzyme-substrate-inhibitor-complex): 0.000018 mM, substrate: soluble amlyose
0.000033
acarviostatin IV03
-
pH 6.5, 37°C, mixed noncompetitive inhibition, Ki' (dissociation constant of the enzyme-substrate-inhibitor-complex): 0.000033 mM, substrate: soluble amlyose
1.12 - 1.64
caffeic acid
0.21 - 0.23
chlorogenic acid
additional information
additional information
-
inhibitory kinetic analysis, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023
acarbose
Sus scrofa
-
IC50 is 0.023 mM
0.17
apigenin-7-glucoside
Sus scrofa
-
IC50 is 0.17 mM
0.37 - 4.8
caffeic acid
0.07 - 1.4
chlorogenic acid
2
cynarin
Sus scrofa
-
IC50 is above 2.0 mM
14
dihydrocaffeic acid
Sus scrofa
-
IC50 is above 14.0 mM
5
ferulic acid
Sus scrofa
-
IC50 is above 5.0 mM
0.44
fisetin
Sus scrofa
-
IC50 is 0.44 mM
0.56
isochlorogenic acid
Sus scrofa
-
IC50 is 0.56 mM
0.17
luteolin
Sus scrofa
-
IC50 is 0.17 mM
0.28
luteolin-7-glucoside
Sus scrofa
-
IC50 is 0.28 mM
13 - 26.5
quinic acid
1.4
rosmarinic acid
Sus scrofa
-
IC50 is 1.4 mM
6.7
Sinapic acid
Sus scrofa
-
IC50 is above 6.7 mM
0.14
Tannic acid
Sus scrofa
-
IC50 is 0.14 mM
additional information
additional information
Sus scrofa
-
IC50: 100.23 microg/ml for corosolic acid, 1.82 microg/ml for acarbose
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1701
-
-
additional information
-
microplate-reader based kinetic assay
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
-
assay at
7.2 - 7.5
-
-
5.5
-
assay at
6.5
-
assay at
6.9
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
AMYP_PIG
511
0
57086
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
-
enzyme form AII, sedimetation measurement
48700
-
enzyme form AI, sedimentation measurement
55400
-
SDS-PAGE
63000
-
x * 63000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 63000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
no modification
-
carbohydrate not detected
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
alpha-amylase complexed with alpha-cyclodextrin
-
enzyme complexed with 4-nitrophenyl alpha-D-maltoside, X-ray diffraction structure determination and analysis at 2.40 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
melting temperature
40
-
the deglycosylated enzymes are slightly less thermo-stable than the glycosylated forms. PPA, PPA-I, and PPA-II retain more than 95% activities up to 40°C and the activities decrease with the increase in temperature. The difference is marginal in the mid-point of thermal transition shifting by 1-2°C
60
-
approx. 50% loss of activity after 30 min in the presence of 2% starch, approx. 85% loss of activity after 30 min in the absence of starch
additional information
-
analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
porcine salivary amylase 1 and 2: PSA1 and PSA2
-
TSKgel BioAssist Q column chromatography, gel filtration
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
the enzyme is a possible target for treatment of diabetes type 2
pharmacology
-
the enzyme is a target for development of specific inhibitors for diabetes type 2 therapy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Furuichi, Y.; Takahashi, T.
Purification and characterization of porcine salivary amylase
Agric. Biol. Chem.
53
293-294
1989
Sus scrofa
-
Manually annotated by BRENDA team
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
Kluh, I.
Hog pancreatic alpha-amylase. Preparation and characterization
Collect. Czech. Chem. Commun.
44
288-294
1979
Sus scrofa
-
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, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus subtilis, Drosophila melanogaster, Escherichia coli, Geobacillus stearothermophilus, Homo sapiens, Hordeum vulgare, Mus musculus, Oryza sp., Saccharomycopsis fibuligera, Streptomyces hygroscopicus, Sus scrofa, Triticum aestivum, Vigna radiata, Xanthomonas campestris
Manually annotated by BRENDA team
Tajiri, T.; Koba, Y.; Ueda, S.
Amylase inhibitors produced by Streptomyces sp. No. 280
Agric. Biol. Chem.
47
671-679
1983
Sus scrofa
-
Manually annotated by BRENDA team
D'Amico, S.; Gerday, C.; Feller, G.
Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase
J. Mol. Biol.
332
981-988
2003
Pseudoalteromonas haloplanktis, Sus scrofa
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
Duy, C.; Fitter, J.
Thermostability of irreversible unfolding alpha-amylases analyzed by unfolding kinetics
J. Biol. Chem.
280
37360-37365
2005
Aspergillus oryzae, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus subtilis, Sus scrofa
Manually annotated by BRENDA team
Funke, I.; Melzig, M.F.
Effect of different phenolic compounds on alpha-amylase activity: screening by microplate-reader based kinetic assay
Pharmazie
60
796-797
2005
Sus scrofa
Manually annotated by BRENDA team
Zhuo, H.; Payan, F.; Qian, M.
Crystal structure of the pig pancreatic alpha-amylase complexed with rho-nitrophenyl-alpha-D-maltoside-flexibility in the active site
Protein J.
23
379-387
2004
Sus scrofa (P00690), Sus scrofa
Manually annotated by BRENDA team
Bijttebier, A.; Goesaert, H.; Delcour, J.A.
Temperature impacts the multiple attack action of amylases
Biomacromolecules
8
765-772
2007
Aspergillus oryzae, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus subtilis, Geobacillus stearothermophilus, Sus scrofa, Thermoactinomyces vulgaris
Manually annotated by BRENDA team
Guzman-Partida, A.M.; Jatomea-Fino, O.; Robles-Burgueno, M.R.; Ortega-Nieblas, M.; Vazquez-Moreno, L.
Characterization of alpha-amylase inhibitor from Palo Fierro seeds
Plant Physiol. Biochem.
45
711-715
2007
Sus scrofa, Zabrotes subfasciatus
Manually annotated by BRENDA team
Geng, P.; Qiu, F.; Zhu, Y.; Bai, G.
Four acarviosin-containing oligosaccharides identified from Streptomyces coelicoflavus ZG0656 are potent inhibitors of alpha-amylase
Carbohydr. Res.
343
882-892
2008
Sus scrofa
Manually annotated by BRENDA team
Karthic, K.; Kirthiram, K.S.; Sadasivam, S.; Thayumanavan, B.
Identification of alpha amylase inhibitors from Syzygium cumini Linn seeds
Indian J. Exp. Biol.
46
677-680
2008
Sus scrofa
Manually annotated by BRENDA team
Gopal, B.A.; Singh, S.A.; Muralikrishna, G.
Porcine pancreatic alpha amylase and its isoforms--effect of deglycosylation by peptide-N-glycosidase F
Int. J. Biol. Macromol.
43
100-105
2008
Sus scrofa
Manually annotated by BRENDA team
Hou, W.; Li, Y.; Zhang, Q.; Wei, X.; Peng, A.; Chen, L.; Wei, Y.
Triterpene acids isolated from Lagerstroemia speciosa leaves as alpha-glucosidase inhibitors
Phytother. Res.
23
614-618
2008
Sus scrofa
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
Acanthoscelides obtectus, Aspergillus fumigatus, Callosobruchus maculatus, Homo sapiens, Sus scrofa (P00690), Zabrotes subfasciatus
Manually annotated by BRENDA team
Larson, S.B.; Day, J.S.; McPherson, A.
X-ray crystallographic analyses of pig pancreatic alpha-amylase with limit dextrin, oligosaccharide, and alpha-cyclodextrin
Biochemistry
49
3101-3115
2010
Sus scrofa (P00690), Sus scrofa
Manually annotated by BRENDA team
Narita, Y.; Inouye, K.
Kinetic analysis and mechanism on the inhibition of chlorogenic acid and its components against porcine pancreas alpha-amylase isozymes I and II
J. Agric. Food Chem.
57
9218-9225
2009
Sus scrofa
Manually annotated by BRENDA team
Cipolla, A.; Delbrassine, F.; Da Lage, J.L.; Feller, G.
Temperature adaptations in psychrophilic, mesophilic and thermophilic chloride-dependent alpha-amylases
Biochimie
94
1943-1950
2012
Drosophila melanogaster (P08144), Pseudoalteromonas haloplanktis (P29957), Sus scrofa (P00690), Thermobifida fusca (Q47R94)
Manually annotated by BRENDA team
Kashani-Amin, E.; Larijani, B.; Ebrahim-Habibi, A.
Neohesperidin dihydrochalcone: presentation of a small molecule activator of mammalian alpha-amylase as an allosteric effector
FEBS Lett.
587
652-658
2013
Sus scrofa (P00690), Sus scrofa
Manually annotated by BRENDA team
Wang, M.; Shi, J.; Wang, L.; Hu, Y.; Ye, X.; Liu, D.; Chen, J.
Inhibitory kinetics and mechanism of flavonoids from lotus (Nelumbo nucifera Gaertn.) leaf against pancreatic alpha-amylase
Int. J. Biol. Macromol.
120
2589-2596
2018
Sus scrofa (P00690)
Manually annotated by BRENDA team
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