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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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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
- cortisol
- wheat
- aspergillus
- maltose
- pancreas
- glycogen
- oryzae
- granule
- lipase
- alpha-glucosidase
-
acid-schiff
- flour
- glucoamylase
-
amylolytic
- amylose
- aleurone
- grain
-
sympathetic
-
social
- parotid
- cereal
- acarbose
- amyloliquefaciens
-
psychological
-
anxiety
- amylopectin
- beta-amylase
- stearothermophilus
- honey
-
gibberellic
- endosperm
- phaseolus
-
psychosocial
-
bread
-
hypothalamic-pituitary-adrenal
-
alcian
-
bake
- cyclodextrins
- dextrin
- amyloglucosidase
-
pas-positive
-
transglycosylation
-
baking
- pullulanase
-
debranching
-
dough
- isoamylase
- awakening
-
eclosion
- pullulan
- brewing
- nutrition
- synthesis
- biotechnology
- pharmacology
- analysis
- medicine
- industry
- food industry
- energy production
- biofuel production
- detergent
- agriculture
The taxonomic range for the selected organisms is: Sus scrofa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-alpha-D-glucan glucanohydrolase
-
-
-
-
Alpha-amylase carcinoid
-
-
-
-
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
-
-
-
-
Low pI alpha-amylase
-
-
-
-
Maxamyl
-
-
-
-
Maxilase
-
-
-
-
Meiotic expression upregulated protein 30
-
-
-
-
Pancreatic alpha-amylase
-
-
-
-
Pivozin
-
-
-
-
PPA-I
PPA-II
Ptyalin
-
-
-
-
Spitase CP 1
-
-
-
-
TAA
-
-
-
-
Taka-amylase A
-
-
-
-
Takatherm
-
-
-
-
Thermamyl
-
-
-
-
Thermolase
-
-
-
-
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
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
PATHWAY SOURCE
PATHWAYS
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
9000-90-2
-
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
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
-
-
?
4-nitrophenyl alpha-D-maltoside + H2O
4-nitrophenol + alpha-D-maltose
4-nitrophenol is bound at the ative site
-
-
?
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
-
-
-
-
?
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
malto-oligosaccharides
-
soluble substrate, hydrolysis of alpha-1,4-linkages
-
-
?
starch + H2O
?
-
inhibition studies using extract of different medicinal plants, pH 6.9
absorbance of reaction products are measured at 540 nm
-
?
additional information
?
-
alpha-amylase hydrolyzes beta-cyclodextrin with difficulty, and fails to hydrolyze gamma-cyclodextrin to any appreciable extent
-
-
?
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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
alpha-amylase hydrolyzes beta-cyclodextrin with difficulty, and fails to hydrolyze gamma-cyclodextrin to any appreciable extent
-
-
?
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
LITERATURE
Ca2+
Ca2+
-
increases the thermostability of the enzyme, one Ca2+ ion per enzyme molecule
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
-
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
-
amylase-inhibitor
-
14 kinds of alpha-amylase inhibitors from Streptomyces sp. No. 280
-
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
corosolic acid
-
triterpene acid isolated from Lagerstroemia speciosa leaves, weak inhibitory activity
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
-
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
-
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
-
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
-
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
-
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
-
acarbose
-
pH 6.5, 37°C, mixed noncompetitive inhibition, substrate: soluble amlyose
caffeic acid
-
mixed-type inhibition, almost all activities of isozymes PPA-I and PPA-II are lost in the presence of 4 mM
chlorogenic acid
-
5-caffeoylquinic acid, mixed-type inhibition, complete inhibition of isozymes PPA-I is observed at 1.5 mM and that of isozyme PPA-II is at 2.0 mM
quinic acid
-
poor inhibitor, activities higher than 80% remain for both isozymes even in the presence of 15 mM quinic acid, while they decrease sharply when the quinic acid concentration increases from 15 to 35 mM. Complete inhibition of isozyme PPAI is given with 35.0 mM, and that of isozyme PPA-II is with 40 mM quinic acid
additional information
enzyme inhibition by lotus leaf flavonoids, LLF, commercial leaf extract preparation including the aglycones quercetin, myricetin, kaempferol, isorhamnetin and diosmetin, inhibitory kinetics and mechanism of flavonoids from lotus (Nelumbo nucifera Gaertn.) leaf against pancreatic alpha-amylase, overview. Binding analysis reveals that binding of LLF to alpha-amylase changes the conformation and microenvironment of alpha-amylase, resulting in inhibition of the enzyme activity. Thus LLF have the potential to be an ingredient in functional food for the prevention of type-2 diabetes. The crude extract of Nelumbo nucifera Gaertn. leaf flavonoids show high inhibitory activity against porcine pancreatic alpha-amylase with IC50 values of 2.20 mg/ml in vitro biochemistry tests
-
additional information
-
no inhibition with voglibose, 23-hydroxyursolic acid, maslinic acid, asiatic acid, arjunolic acid, and oleanolic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.065
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
additional information
additional information
thermodynamic and kinetic analysis, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
291
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene
pH not specified in the publication, 25°C
0.022
starch
presence of 0.4 mM neohesperidin dihydrochalcone, pH 7.2, 42°C
0.035
starch
presence of 2.4 mM neohesperidin dihydrochalcone, pH 7.2, 42°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
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
additional information
additional information
inhibitory kinetic analysis, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AMYP_PIG
511
0
57086
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
study of the role of bound carbohydrate on PPA and its isoforms. Deglycosylation by peptide-N-glycosidase F. The nature of the oligosaccharides may be probably Man-Man and Man3GlcNAc. The presence of N-acetyl glucose amine is not determined
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
-
Kluh, I.
Hog pancreatic alpha-amylase. Preparation and characterization
Collect. Czech. Chem. Commun.
44
288-294
1979
Sus scrofa
-
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
Tajiri, T.; Koba, Y.; Ueda, S.
Amylase inhibitors produced by Streptomyces sp. No. 280
Agric. Biol. Chem.
47
671-679
1983
Sus scrofa
-
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
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
-
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 subtilis, Bacillus licheniformis, Sus scrofa
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
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
Bijttebier, A.; Goesaert, H.; Delcour, J.A.
Temperature impacts the multiple attack action of amylases
Biomacromolecules
8
765-772
2007
Aspergillus oryzae, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus licheniformis, Sus scrofa, Thermoactinomyces vulgaris
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
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
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
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
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
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)
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
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
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
Sus scrofa (P00690), Drosophila melanogaster (P08144), Pseudoalteromonas haloplanktis (P29957), Thermobifida fusca (Q47R94)
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
EXTERNAL LINKS (specific for EC-Number 3.2.1.1)
Transporter Classification Database (TCDB): 8.A.9.1.3
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Release 2023.1 (January 2023)
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