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(2H)-1,4-benzoxazin-3(4H)-one
-
-
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
1-cyclohexyl-3-(morpholinyl-4-ethyl)-carbodiimide
-
40 mM, 50% inhibition after 20 min, 100 mM, 44% inhibition after 10 min in the presence of 1% starch
2,4-dihydroxy-7-methoxy-(2H)-1,4-benzoxazin-3(4H)-one
-
-
2,4-Dinitro-1-fluorobenzene
-
6 mM
2-amino-7-hydroxyphenoxazine-3-one
-
-
2-amino-7-methoxyphenoxazine-3-one
-
-
2-amino-phenoxazine-3-one
-
-
2-hydroxy-(2H)-1,4-benzoxazin-3(4H)-one
-
-
2-hydroxy-7-methoxy-(2H)-1,4-benzoxazin-3(4H)-one
-
-
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
3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate
CHAPS, 39.2% inhibition at 1% v/v
4-chloromercuribenzoate
-
98% inhibition of isozyme alpha-amylase I at 0.5 mM
4-chloromercuribenzoic acid
-
52% inhibition at 4 mM
4-hydroxy-(2H)-1,4-benzoxazin-3(4H)-one
-
-
4-hydroxy-7-methoxy-(2H)-1,4-benzoxazin-3(4H)-one
-
-
5,5'-dithiobis-[2-nitrobenzoic acid]
-
10 mM, 35% inhibition
6-methoxy-benzoxazolin-2(3H)-one
-
-
7-methoxy-(2H)-1,4-benzoxazin-3(4H)-one
-
-
acacetin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 14.1% maximum inhibition
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
-
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
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
-
AlCl3
-
5 mM, complete inhibition
alpha-acarviosinyl-1,4-alpha-D-glucopyranosyl-1,6-D-glucopyranosylidene-spiro-thiohydantoin
-
i.e. PTS-G-TH, mixed-competitive type inhibition
alpha-AI-Pc1
-
alpha-amylase inhibitors from Phaseolus coccineus
-
alpha-AI1
-
alpha-amylase inhibitor 1 from cultivated Phaseolus vulgaris
-
alpha-AI2
-
alpha-amylase inhibitor 2 from wild Phaseolus vulgaris
-
alpha-amylase inhibitors from Dipteryx alata seeds
-
alpha-D-methylglucopyranose
-
-
alpha-D-phenylglucoside
-
-
alphaAI-PF
-
alpha amylase inhibitor from Palo Fierro seeds
-
ammonium persulfate
54% inhibition at 5 mM
ammonium sulfate
non-competitive inhibitor at concentrations higher than 20 mM
amylase wheat inhibitor
-
-
-
amylase-inhibitor
-
14 kinds of alpha-amylase inhibitors from Streptomyces sp. No. 280
-
apigenin-7-glucoside
-
IC50 is 0.17 mM
ascorbate
-
28.4% inhibition at 5 mM, 34.9% at 10 mM
ATP
-
90% inhibition at 5 mM, reversible by addition of Ca2+ or Mg2+
Benzene
-
10%, 40% inhibition
benzoxazolin-2(3H)-one
-
-
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
Bi2+
-
0.5 mM BiOCl2, 16% inhibition
Bio-tex
liquid commercial detergent, 75% residual activity
-
catechin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 13.1% maximum inhibition
cetyltrimethylammonium bromide
-
CTAB
CH2ICOOH
-
10 mM, complete inhibition
Citric acid
-
25 mM, 54% inhibition
corosolic acid
-
triterpene acid isolated from Lagerstroemia speciosa leaves, weak inhibitory activity
Cs+
-
5 mM, 32% loss of activity
Cs2+
-
1 mM, 37°C, 30 min, pH 6.5, 89% relative activity
Cyclohexane
-
inhibitory effect of cyclooctane on amylase stability is stronger than that of cyclohexane
cyclooctane
-
inhibitory effect of cyclooctane on amylase stability is stronger than that of cyclohexane
cynarin
-
IC50 is above 2.0 mM
D-gluconic acid lactone
-
-
daidzein
-
a isoflavone, 0.888 mM, pH 6.0, room temperature, 23.3% maximum inhibition
dihydrocaffeic acid
-
IC50 is above 14.0 mM
diisopropyl fluorophosphate
-
1 mM, 34% inhibition of the membrane-bound enzyme
Dimethyl formamide
-
38.2% inhibition at 1 mM, 72.0% at 5 mM
diosmetin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 19.2% maximum inhibition
dodecyltrimethylammonium bromide
epicatechin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 10.3% maximum inhibition
eupafolin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 99.4% maximum inhibition
FeCl3
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 21% loss of activity, alpha-amylase I
ferulic acid
-
IC50 is above 5.0 mM
fucoidan
-
fucoidan derived from algal species Ascophyllum nodosum and Fucus vesiculosus. Fucoidan extracted from Fucus vesiculosus does not inhibit alpha-amylase activity, while fucoidan from Ascophyllum nodosum decreases alpha-amylase activity by 7100% at 5 mg/ml. Both fucoidans are inhibitory to alpha-glucosidase, EC 3.2.1.20
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
glucose
-
1 M, 34% inhibition. No inhibition up to 0.25 M
glucosyl-alpha-cyclodextrin
0.2%, 19% inhibition
Glutardialdehyde
-
0.4%, 57% loss of activity
Green Balance
solid commercial detergent, when used with tap water, 51% residual activity
-
guanidine hydrochloride
-
0.05 to 0.6 mM, as the concentraion is increased, the loss of of the whole conformational structure occurs and the relative activity decreases from 80% at 0.05 mM to 29% at 0.6 mM compared to the control, pH 8.0, 100°C
guanidinium hydrochloride
slight inhibition at 5-10 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
-
hesperetin
-
a flavanone, 0.888 mM, pH 6.0, room temperature, 39.8% maximum inhibition
Hg+
5 mM, complete inhibition
inhibitor from Amaranthus hybrid
-
no effect on alpha-amlyase at pH 6.0, but high inhibitory effect with maximal 80% at pH 9.0, 50°C
-
inhibitor from Phaseolus coccineus 35619
-
no effect at pH 9.0, inhibits the enzyme activity up to 78% at pH 6.0, 50°C
-
inhibitor from Phaseolus vulgaris cv. Radical
-
no effect at pH 9.0, inhibits the enzyme activity up to 87% at pH 6.0, 50°C
-
iodoacetamide
-
slight inhibition
isoacarbose
binding mechanism, resistance to rearrangement, enzyme-inhibitor complex crystal structure analysis, binding highly perturbs catalytic residue D300
Isoamylalcohol
-
70% inhibition at 10%, 90% at 20%
isochlorogenic acid
-
IC50 is 0.56 mM
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
KCN
-
25 mM, 70% inhibition
KI
-
0.05 to 0.6 mM, with 88% relative enzyme activity at 0.05 M decreasing to 42% at 0.6 mM compared to the control, also loss of fluorescence intensity, pH 8.0, 100°C
KSCN
-
500 mM, the reaction rate of acid-stable amylase decreases
L-Cys
-
25 mM, 26% inhibition
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
-
linear alkylbenzene sulfonate
mutant M197A, concentration of 10% incubation at 60°C for 1 h, 71% residual relative activity, assay at 80°C and pH 5.6
luteolin-7-glucoside
-
IC50 is 0.28 mM
maltopentaose
-
30 mM, 51% inhibition
maltotetraose
-
30 mM, 51% inhibition
maltotriose
-
30 mM, 42% inhibition
MgSO4
2 mM, pH 6.5, 50°C, 75% relative activity
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
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
-
N-alpha-p-tosyl-L-lysine chloromethyl ketone
-
1 mM, 22% loss of the activity of the membrane-bound enzyme
n-hexane
Cardamine battagliae
-
-
Na2-EDTA
-
0.01 M, 1% loss of activity after 1 h, in presence of 0.01 M CaCl2, complete inactivation after 1 h
naringenin
-
a flavanone, 0.888 mM, pH 6.0, room temperature, 26.9% maximum inhibition
NiCl2
-
30 mM, 39% inhibition
NiSO4
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 79% loss of activity, alpha-amylase I
O-4,6-dideoxy-4-{[4,5,6-trihydroxy-3-hydroxymethyl-2-cyclohexen-1-yl]amino}-alpha-D-glucopyranosyl-(1-4)-O-alpha-D-glucopyranosyl-(1-4)-D-glucose
-
trivial name acarbose, uncompetitive inhibition vs. amylose and maltodextrin, mixed noncompetitive inhibition vs. maltoheptaose
p-chloromercuribenzoate
-
0.05 mM, 52% inhibition of intestine alpha-amylase, 68% inhibition of muscle alpha-amylase
p-hydroxymercuribenzoate
-
-
p-hydroxymercurybenzoate
activity severely inhibited, indicates the role of sulfydryl group in catalysis
PbCl2
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 35% loss of activity, alpha-amylase I
PEG 8000
-
15-20% inhibition at 1-2%
-
phenyl methyl sulfonyl fluoride
-
1 mM, 70% inhibition
phenylmercuric acetate
-
-
phenylmethylsulfonyl fluoride
-
60% inhibition at 4 mM
polyethylene glycol 400
-
1500 Da PEG, inhibits the enzyme activity by 14% at 0.02% w/v
-
Propanol
-
30% inhibition at 10%, 50% at 20%
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
-
protein VrD1
-
an insecticidal plant defensin
-
proteinaceous inhibitor from wheat WI-1
inhibitor of isozyme Amy2 but not Amy1
-
proteinaceous inhibitor from wheat WI-3
-
-
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
-
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
rice bifunctional alpha-amylase/subtilisin inhibitor
-
purification, crystallization and preliminary X-ray crystallographic analysis of the inhibitor
-
rosmarinic acid
-
IC50 is 1.4 mM
scutellarein
-
a flavone, 0.888 mM, pH 6.0, room temperature, 98.4% maximum inhibition
Secale cereale inhibitor
-
Sinapic acid
-
IC50 is above 6.7 mM
Sn2+
-
1 mM, complete inhibition
Sodium citrate
-
23.1% inhibition at 5 mM
Sorghum procyanidin tetramer
P04745
thermodynamics, and binding and inhibition kinetics, overview
-
starch
-
concentrations above 32 g/l
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
-
Tris
starch-hydrolyzing activity in presence of Tris of different concentrations, pH 7.4, 37°C
Vigna unguiculata defensin
-
wheat alpha-amylase inhibitor 0.19
-
inhibitor 0.19 isolated from wheat kernels, inhibits both isozymes AoA1 and AoA2 in vitro and in vivo, stoichiometry of inhibition of isozymes, biological activity of inhibitor 0.19, overview
-
wheat alpha-amylase inhibitor 0.35
-
inhibitor 0.35 isolated from wheat kernels, inhibits both isozymes AoA1 and AoA2 in vitro and in vivo, stoichiometry of inhibition of isozymes, biological activity of inhibitor 0.53, overview
-
wheat amylase inhibitor
-
wheat seed amylase inhibitor
-
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
-
(NH4)2SO4
slight inhibition at 5-10 mM
1,10-phenanthroline
-
22% inhibition at 10 mM
1,10-phenanthroline
-
10.7% inhibition at 10 mM
1,10-phenanthroline
-
1 mM, 39% loss of activity of the membrane-bound enzyme
2-mercaptoethanol
-
37.6% inhibition at 1 mM, 43.7% at 5 mM
2-mercaptoethanol
-
87% residual activity at 5 mM
2-mercaptoethanol
-
20% inhibition at 1 mM, 30% at 5 mM
2-mercaptoethanol
85.9% inhibition at 1 mM
2-mercaptoethanol
-
1 mM, 23% loss of activity
2-mercaptoethanol
59% inhibition at 10 mM
4-bromophenacyl bromide
-
4-bromophenacyl bromide
-
complete inhibition at 4 mM
4-bromophenacyl bromide
19% inhibition at 2 mM
acarbose
-
-
acarbose
a pseudotetrasaccharide inhibitor of alpha-amylase and alpha-glucosidase, binding structure, overview
acarbose
enzyme binding and docking study
acarbose
Caloglyphus redickorzevi
-
-
acarbose
binding mechanism, acarbose rearrangement mechanism implied by the kinetic and structural analysis, and potential pathways of rearrangement, enzyme-inhibitor complex crystal structure analysis
acarbose
-
0.888 mM, pH 6.0, room temperature, 99.2% maximum inhibition
acarbose
-
IC50 is 0.023 mM
acarbose
-
pH 6.5, 37°C, mixed noncompetitive inhibition, substrate: soluble amlyose
acarbose
activity is reduced to 56.4% in the presence of 0.00002 mM of inhibitor and inhibition reaches 77% at 0.00008 mM concentration
acarbose
enzyme binding and docking study
acetone
inhibits 34% at 20% v/v, and 61% at 50% v/v
Ag+
-
-
Ag+
-
2 mM, 61.2% inhibition
Ag+
-
5 mM AgNO3, 82% inhibition
Ag+
-
1 mM, 50% loss of activity
Ag+
-
1 mM, 51% inhibition
Ag+
-
0.1 mM, 11% inhibition
Ag+
-
5 mM AgNO3, 95% inhibition
Ag+
-
2 mM, complete inhibition
Ag+
-
1 mM, 37°C, 30 min, pH 6.5, 36% relative activity
Ag+
-
1 mM AgCl2, 77% loss of activity
Ag2+
activity severely inhibited, indicates the role of sulfydryl group in catalysis
AgNO3
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 12% loss of activity, alpha-amylase I
AgNO3
-
2 mM, complete inhibition
Al3+
5 mM, weak inhibition
Al3+
-
2 mM, 38.7% inhibition
Al3+
-
1 mM, pH 8.0, 24 h at 4°C, 110% and 73% residual activity for Amy I and Amy II, respectively
Al3+
-
10 mM, 86% loss of activity
Al3+
-
10 mM, 58% inhibition
Al3+
-
10 mM, 90% inhibition
Al3+
-
complete inhibition of isozyme AI-1, nearly complete inhibition of isozyme AI-2, moderate inhibition of isozyme AII, at 5 mM
alpha-amylase inhibitors from Dipteryx alata seeds
-
-
-
alpha-amylase inhibitors from Dipteryx alata seeds
-
-
-
alpha-cyclodextrin
the addition of alpha-cyclodextrin (0.1% w/v) induces a very weak inhibition of the Amy1 protein activity against soluble starch
alpha-cyclodextrin
-
weak inhibition
alpha-cyclodextrin
-
1-10 mM, 25-35% inhibition
alpha-cyclodextrin
0.2%, 10% inhibition
Ba2+
-
5.3% inhibition at 1 mM, 11.1% at 5 mM
Ba2+
-
strong inhibition of isozyme BAA
Ba2+
-
5 mM BaCl2, 28% inhibition
Ba2+
-
1 mM, 23% inhibition of wild-type enzyme, 28% inhibition of mutant enzyme L134R/S320A
Ba2+
-
1 mM, pH 8.0, 24 h at 4°C, 104% and 95% residual activity for Amy I and Amy II, respectively
Ba2+
-
80% residual activity at 10 mM
Ba2+
-
0.1 M, complete inhibition
Ba2+
-
0.1 mM, 60% inhibition
Ba2+
-
slight inhibition of isozymes AI-1 and AI-2, and AII
Ba2+
-
5 mM BaCl2, 22% inhibition
Ba2+
-
1 mM, 37°C, 30 min, pH 6.5, 29% relative activity
Ba2+
-
1 mM BaCl2, 40% loss of activity
Ba2+
2 mM, 72% residual activity
BaCl2
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 16% loss of activity, alpha-amylase I
BaCl2
-
5 mM, pH 4.0, 55°C, 25% relative activity
beta-cyclodextrin
the addition of beta-cyclodextrin (0.1% w/v) induces a very weak inhibition of the Amy1 protein activity against soluble starch
beta-cyclodextrin
-
1-10 mM, 10-25% inhibition
beta-cyclodextrin
0.2%, 19% inhibition
butanol
inhibits 15% at 20% v/v, and 21% at 50% v/v
butanol
-
10%, 80% inhibition
Ca2+
5 mM, weak inhibition
Ca2+
-
11.4% inhibition at 10 mM, 56.2% at 50 mM
Ca2+
7% inhibition at 1 mM
Ca2+
-
10 mM CaCl2, inhibition of enzyme form Amyl II and Amyl III, no inhibition of enzyme form Amyl I
Ca2+
-
0.01 M CaCl2, 3% loss of activity after 1 h, in presence of 0.01 M Na2-EDTA, complete inactivation after 1 h
Ca2+
-
16% activation at 1 mM, although Ca2+ is a good stabilizer it cannot activate the enzyme significantly, Ca2+ shows 41% inhibition of the enzyme at 10 mM
Ca2+
-
1 mM, 25-30% inhibition between pH 8.0 and 10.0
Ca2+
-
strong inhibition of isozyme BAA
Ca2+
60% inhibition at 5 mM
Ca2+
-
about 80% relative activity at 10 mM Ca2+
Ca2+
-
calcium stabilizes the conformation of alpha-amylase and also involved in substrate binding, but inhibits enzyme activity
Ca2+
-
40% residual activity at 20 mM Ca2+ for midgut alpha-amylase and 46% residual activity at 10 mM Ca2+ for salivary gland alpha-amylase
Ca2+
-
5 mM CaCl2, 21% inhibition
Ca2+
-
added alone Ca2+ is inhibitory
CaCl2
-
above 0.1 mM
CaCl2
-
4 mM, 30% inhibition
CaCl2
-
inhibition above 100 mM, approx. 50% inhibition at 500 mM
caffeic acid
-
IC50 is 4.8 mM
caffeic acid
-
mixed-type inhibition, almost all activities of isozymes PPA-I and PPA-II are lost in the presence of 4 mM
Cd2+
-
-
Cd2+
-
1 mM, 91% inhibition
Cd2+
-
2 mM, 43% inhibition
Cd2+
-
1 mM, 33% inhibition of wild-type enzyme, 48% inhibition of mutant enzyme L134R/S320A
Cd2+
-
1 mM, 40% loss of activity
Cd2+
-
10 mM, complete inhibition
Cd2+
-
complete inhibition of isozyme AII, high inhibition of isozymes AI-1 and moderate of AI-2, at 5 mM
Cd2+
-
2 mM, 65% inhibition
Cd2+
complete inhibition at 5 mM
Cd2+
Thermomonospora vulgaris
-
1 mM CdSO4, 82% inhibition
CdCl2
-
5 mM, 14% inhibition; 5 mM, 38% inhibition; 5 mM, 43% inhibition
CdCl2
-
30 mM, 95% inhibition
chlorogenic acid
-
IC50 is 1.4 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
Cl-
-
-
Co2+
63% inhibition at 1 mM
Co2+
-
11.1% inhibition at 1 mM, 89.4% at 5 mM
Co2+
-
16% residual activity at 5 mM
Co2+
27% inhibition at 1 mM, 68% at 10 mM
Co2+
-
5 mM, 16% inhibition
Co2+
-
1 mM, 17% loss of activity
Co2+
-
1 mM, pH 8.0, 24 h at 4°C, 92% and 93% residual activity for Amy I and Amy II, respectively
Co2+
-
70% residual activity at 10 mM
Co2+
-
slight activation of isozyme AI-2, slight inhibition of isozymes AI-1 and AII
Co2+
47% inhibition of wild-type and mutant enzymes at 5 mM
Co2+
-
5 mM CoCl2, 91% inhibition
Co2+
75.9% inhibition at 1 mM
Co2+
-
1 mM, 37°C, 30 min, pH 6.5, 23% relative activity
Co2+
-
1 mM CoCl2, 65% loss of activity
Co2+
inhibits 60% at 5 mM
Co2+
complete inhibition at 1 mM
Co2+
-
28% inhibition at 5 mM
CoCl2
-
30 mM, 50% inhibition
CoCl2
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 22% loss of activity, alpha-amylase I
CoCl2
-
21% inhibition of isozyme alpha-amylase I at 0.5 mM, 29% at 5 mM
CoCl2
1 mM, 52% inhibition
Cu2+
5 mM, complete inhibition
Cu2+
-
addition to growth medium in logarithmic phase, maximum inhibition of about 70-80% of enzyme expression at 0.47 mM. Addition to enzyme assay, 38.2% inhibition at 1.5 mM
Cu2+
-
76% inhibition at 0.5 mM, complete inhibition at 1 mM
Cu2+
-
10 mM, strong inhibition of enzyme form Amyl I, Amyl II and Amyl III
Cu2+
54% inhibition at 1 mM, 76% at 5 mM
Cu2+
-
29% inhibition at 1 mM
Cu2+
-
25% inhibition at 5 mM
Cu2+
-
complete inhibition at 1-5 mM
Cu2+
-
strong inhibition of isozyme BAA
Cu2+
18% inhibition at 1 mM, 48% at 10 mM
Cu2+
-
2 mM, almost complete inhibition
Cu2+
-
5 mM CuSO4, 16% inhibition
Cu2+
-
1 mM, 55% inhibition of wild-type enzyme, 49% inhibition of mutant enzyme L134R/S320A
Cu2+
-
1 mM, 99% loss of activity
Cu2+
complete inhibition at 5 mM
Cu2+
-
7% residual activity at 2 mM
Cu2+
-
1 mM, 67% loss of activity
Cu2+
-
1 mM, 52% inhibition
Cu2+
-
1 mM, pH 8.0, 24 h at 4°C, 36% and 64% residual activity for Amy I and Amy II, respectively
Cu2+
-
1 mM, 28% inhibition
Cu2+
-
complete inhibition at 5 mM, at 80°C and pH 5.0
Cu2+
-
86% residual activity at 10 mM
Cu2+
-
complete inhibition at 1 mM
Cu2+
-
10 mM, 88% loss of activity
Cu2+
-
0.1 M, complete inhibition
Cu2+
-
10 mM, 58% inhibition
Cu2+
-
10 mM, 49% inhibition
Cu2+
-
nearly complete inhibition of isozymes AI-1 and AI-2, and AII at 5 mM
Cu2+
62% inhibition of wild-type and mutant enzymes at 5 mM
Cu2+
-
1 mM, 25% residual activity
Cu2+
-
5 mM CuSO4, complete inhibition
Cu2+
64.1% inhibition at 1 mM
Cu2+
-
2 mM, complete inhibition
Cu2+
5 mM, complete inhibition
Cu2+
-
complete inhibition at 4 mM
Cu2+
-
1 mM CuCl2, 28% loss of activity
Cu2+
inhibits 75% at 5 mM
Cu2+
Thermomonospora vulgaris
-
1 mM CuSO4, 82% inhibition
Cu2+
-
5 mM, 90% inhibition
Cu2+
52.2% residual activity at 1 mM
Cu2+
1 mM, 99% loss of activity
Cu2+
-
25% inhibition at 5 mM
Cu2+
2 mM, no residual activity
CuCl2
-
5 mM, 88% inhibition; 5 mM, 89% inhibition; 5 mM, 94% inhibition
CuCl2
-
10 mM, 95% inhibition
CuCl2
1 mM, complete inhibition
CuCl2
-
5 mM, pH 4.0, 55°C, 26% relative activity
CuSO4
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 25% loss of activity, alpha-amylase I
CuSO4
2 mM, pH 6.5, 50°C, 50% relative activity
CuSO4
-
4 mM, complete inhibition
CuSO4
-
2 mM, 33% inhibition
Dextran
-
complete inhibition at 1%
Dextran
-
1%, 20% inhibition
dithiothreitol
inhibits the enzyme activity at concentrations higher than 80 mM
dithiothreitol
-
1 mM, 50% inhibition
DMSO
inhibits 20% at 20% v/v, and 31% at 50% v/v
dodecyltrimethylammonium bromide
-
2.5 mM, approx. 40% inhibition at 60°C
dodecyltrimethylammonium bromide
-
2.5 mM, approx. 20% inhibition at 60°C
DTNB
-
55.2% inhibition at 5 mM
DTNB
-
10 mM, complete inhibition
DTNB
-
inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
DTT
-
61.9% inhibition at 1 mM, 84.8% at 5 mM
DTT
-
20% inhibition at 1 mM
DTT
20.1% inhibition at 1 mM
DTT
74% inhibition at 1 mM
EDTA
-
63% inhibition at 10 mM
EDTA
-
0.05 mM, 64% inhibition of intestine alpha-amylase, complete inhibition of muscle alpha-amylase
EDTA
-
30% inhibition at 10 mM, 20% at 5 mM
EDTA
-
80% of the enzyme activity is lost when the enzyme is incubated with 10 mM EDTA, indicating the enzyme is a metalloenzyme, pH 5.0, 50°C
EDTA
-
resistant at 30°C, inhibition at 90°C, inhibition is partially recovered by Cu2+ or Fe2+
EDTA
-
19.3% inhibition at 5 mM
EDTA
-
12% residual activity at 5 mM; BMA.2 belongs to the EDTA-sensitive alpha-amylases
EDTA
-
10 mM, 90% inhibition
EDTA
-
85% residual activity at 10 mM EDTA
EDTA
41% inhibition at 1 mM, 79% at 10 mM
EDTA
-
0.1 mM, 61.3% inhibition
EDTA
-
10 mM, 67% inhibition
EDTA
-
nearly complete inhibition at 1 mM
EDTA
-
50 mM, abolished 50% of the activity
EDTA
50% of the activity abolished in presence of 50 mM EDTA
EDTA
-
5 M, 32% loss of activity
EDTA
-
1 mM, pH 8.0, 24 h at 4°C, 98% and 76% residual activity for Amy I and Amy II, respectively
EDTA
slight inhibition at 5-10 mM
EDTA
-
10% residual activity at 5 mM, at 80°C and pH 5.0
EDTA
-
21% residual activity at 10 mM, alpha-amylase is completely inactivated after 6 min of incubation at 80°C in the presence of 5 mM EDTA
EDTA
-
over 80% inhibition at 1 mM
EDTA
AmyUS100DELTAG retains 40 and 25% of its original activity at 40 and 60°C, respectively, when incubated with 200 mM of EDTA, compared to 12 and 0% for AmyUS100
EDTA
-
1 mM, 36% inhibition
EDTA
-
37% residual activity at 4 mM EDTA for midgut alpha-amylase and 30% residual activity at 4 mM EDTA for salivary gland alpha-amylase
EDTA
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, complete loss of activity, alpha-amylase I
EDTA
-
515 mM, with or without chloroform
EDTA
-
pH 7.5, irreversible loss of activity, half-life: 29 h at 25 mM, 64 h at 12 mM, 670 h at 6 mM and 3500 at 3 mM
EDTA
-
92% inhibition of isozyme alpha-amylase I at 1 mM
EDTA
-
10 mM, 57% inhibition
EDTA
-
strong inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
EDTA
-
25 mM, 92% inhibition
EDTA
-
5 mM, 15% inhibition
EDTA
81.9% inhibition at 1 mM
EDTA
-
1-10 mM, about 60-65% inhibition
EDTA
-
0.01 M, 58% loss of activity
EDTA
-
5, 10, and 20 mM, pH 4.0, 55°C, 95% relative activity, enzyme is not sensitive to chelating agent, probably not a metalloenzyme
EDTA
-
1 mM, 85% loss of activity
EDTA
-
reverses stimulation by Ca2+
EDTA
Thermomonospora vulgaris
-
-
EDTA
Thermomonospora vulgaris
-
inhibition is completely nullified by Ca2+
EDTA
-
complete inhibition at 0.1 mM, reversible by addition of Ca2+ or Mg2+
EDTA
-
2 mM, 25% inhibition
EDTA
1 mM, almost complete loss of activity
EDTA
-
10 mM, 5% inactivation after 5 min, complete inactivation after 4 h
EDTA
-
a distinct decrease of enzyme activity. The activity can not be regained after the addition of excess CaCl2, demonstrating the irreversibility of inactivation
EGTA
-
10 mM, 91% inhibition
EGTA
-
10 mM, 53% inhibition of the membrane-bound enzyme
EGTA
-
1-10 mM, about 50% inhibition
EGTA
-
5, 10, and 20 mM, pH 4.0, 55°C, 100% relative activity, enzyme is not sensitive to chelating agent, probably not a metalloenzyme
EGTA
-
complete inhibition at 0.1 mM, reversible by addition of Ca2+ or Mg2+
ethanol
inhibits 9% at 20% v/v, and 18% at 50% v/v
ethanol
-
20% inhibition at 10%, 40% at 20%
ethanol
-
10%, 36% inhibition
Fe2+
-
-
Fe2+
8% inhibition at 1 mM, 27% at 5 mM
Fe2+
-
90% inhibition at 1-5 mM
Fe2+
-
35% inhibition at 5 mM
Fe2+
-
94.1% inhibition at 1 mM, complete inhibition at 5 mM
Fe2+
-
5 mM FeSO4, 71% inhibition
Fe2+
-
complete inhibition at 5 and 10 mM
Fe2+
-
1 mM, 47% loss of activity
Fe2+
-
1 mM, pH 8.0, 24 h at 4°C, 68% and 24% residual activity for Amy I and Amy II, respectively
Fe2+
-
2 mM, complete inhibition
Fe2+
-
10 mM, 90% loss of activity
Fe2+
-
0.1 M, complete inhibition
Fe2+
-
0.1 mM, 23% inhibition
Fe2+
strong inhibition of wild-type and mutant enzymes at 5 mM
Fe2+
-
5 mM FeSO4, 91% inhibition
Fe2+
55.3% inhibition at 1 mM
Fe2+
-
2 mM, 49% inhibition
Fe2+
-
1 mM, 37°C, 30 min, pH 6.5, 81% relative activity
Fe2+
-
1 mM FeCl2, 38% loss of activity
Fe2+
Thermomonospora vulgaris
-
10 mM, 86% inhibition
Fe2+
1 mM, 98% loss of activity
Fe3+
-
9% inhibition at 1 mM
Fe3+
-
complete inhibition at 1-5 mM
Fe3+
30% inhibition at 1 mM, 62% at 10 mM
Fe3+
-
2 mM, almost complete inhibition
Fe3+
complete inhibition at 5 mM
Fe3+
-
1 mM, 51% loss of activity
Fe3+
-
10% residual activity at 10 mM
Fe3+
-
10 mM, 95% loss of activity
Fe3+
-
10 mM, 92% inhibition
Fe3+
-
0.1 mM, 45% inhibition
Fe3+
-
complete inhibition of isozymes AI-1 and AI-2, and AII at 5 mM
Fe3+
-
1 mM, 37°C, 30 min, pH 6.5, 57% relative activity
Fe3+
-
5 mM, 90% inhibition
Fe3+
1 mM, complete loss of activity
FeCl2
-
5 mM, complete inhibition
FeCl2
-
5 mM, pH 4.0, 55°C, 85% relative activity
FeSO4
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 86% loss of activity, alpha-amylase I
FeSO4
2 mM, pH 6.5, 50°C, 47% relative activity
FeSO4
-
4 mM, 80% inhibition
fisetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 85.6% maximum inhibition
fisetin
-
IC50 is 0.44 mM
gamma-cyclodextrin
the addition of gamma-cyclodextrin (0.1% w/v) induces a very weak inhibition of the Amy1 protein activity against soluble starch
gamma-cyclodextrin
0.2%, 18% inhibition
glycerol
-
0.05 mM, 68% inhibition of intestine alpha-amylase
glycerol
-
20-25% inhibition at 1-2%
glycerol
-
1%, 26% inhibition
glycine
-
almost complete inhibition at 1%
glycine
-
2%, 20% inhibition
H2O2
-
82.3% inhibition at 0.5%, 43.7% at 5 mM
Hg2+
-
addition to growth medium in logarithmic phase, 0.025 mM, no enzyme expression. Addition to enzyme assay, 69% inhibition at 0.5 mM
Hg2+
-
1 mM HgCl2, 89.5% inhibition
Hg2+
-
10 mM, strong inhibition of enzyme form Amyl I, Amyl II and Amyl III
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
complete inhibition at 5 mM, 94% inhibition at 1 mM
Hg2+
-
complete inhibition at 5 mM
Hg2+
-
partially reversed by Cys
Hg2+
-
complete inhibition at 5 mM
Hg2+
-
1 mM, complete inhibition
Hg2+
-
complete inhibition at 5 and 10 mM
Hg2+
-
2 mM, almost complete inhibition
Hg2+
-
5 mM HgCl2, 98% inhibition
Hg2+
-
1 mM, complete inhibition of wild-type enzyme and mutant enzyme L134R/S320A
Hg2+
activity severely inhibited, indicates the role of sulfydryl group in catalysis
Hg2+
-
1 mM, complete inactivation
Hg2+
-
complete inhibition at 2 mM
Hg2+
-
2 mM, complete inhibition
Hg2+
-
1 mM, 82% loss of activity
Hg2+
-
1 mM, 25% inhibition
Hg2+
-
1 mM, pH 8.0, 24 h at 4°C, 35% and 31% residual activity for Amy I and Amy II, respectively
Hg2+
-
1 mM, 66% inhibition
Hg2+
-
complete inhibition at 5 mM, at 80°C and pH 5.0
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
1 mM, complete inhibition
Hg2+
-
10 mM, 88% loss of activity
Hg2+
-
0.1 M, 98% inhibition
Hg2+
-
10 mM, 55% inhibition
Hg2+
-
complete inhibition
Hg2+
-
10 mM, 98% inhibition
Hg2+
-
complete inhibition of isozymes AI-1 and AI-2, and AII at 5 mM
Hg2+
73% inhibition of wild-type and mutant enzymes at 5 mM
Hg2+
-
1 mM, 15% residual activity
Hg2+
-
5 mM HgCl2, 99% inhibition
Hg2+
-
5 mM, 28% inhibition
Hg2+
-
2 mM, complete inhibition
Hg2+
-
5 mM, 64% loss of activity
Hg2+
-
5 mM, 85% inhibition
Hg2+
-
complete inhibition at 4 mM
Hg2+
-
1 mM, 37°C, 30 min, pH 6.5, 44% relative activity
Hg2+
-
1 mM HgCl2, 88% inhibition
Hg2+
complete inhibition at 5 mM
Hg2+
-
0.5 mM HgCl2, 60% inhibition
Hg2+
complete inhibition at 1 mM
Hg2+
-
62% inhibition at 5 mM
HgCl2
-
5 mM, complete inhibition
HgCl2
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 95% loss of activity, alpha-amylase I
HgCl2
-
10 mM, complete inhibition
HgCl2
-
4 mM, 71% inhibition
HgCl2
-
2 mM, complete inhibition
iodoacetate
-
around 100 mM
iodoacetate
-
0.5 mM, 98% inhibition
iodoacetate
-
1 mM, 60% inhibition
iodoacetate
Thermomonospora vulgaris
-
-
iodoacetic acid
5 mM
iodoacetic acid
-
0.05 mM, complete inhibition of intestine and muscle alpha-amylase
iodoacetic acid
-
88% inhibition of isozyme alpha-amylase I at 0.5 mM
iodoacetic acid
-
slight inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
K+
11% inhibition at 1 mM, 21% at 5 mM
K+
-
inhibits enzyme activity, 60 and 42% relative activity with 5 and 10 mM K+, pH 5.0, 50°C
K+
-
78% residual activity at 40 mM K+ for midgut alpha-amylase
K+
-
10 mM, 23% inhibition
K+
-
slight activation of isozymes AI-1 and AII, slight inhibition of isozyme AI-2
lauryl sulfobetaine
-
2.5 mM, approx. 30% inhibition at 60°C
lauryl sulfobetaine
-
2.5 mM, approx. 20% inhibition at 60°C
Li+
-
slight activation of isozymes AI-1 and AI-2, slight inhibition of isozyme AII
Li+
26.2% inhibition at 1 mM
luteolin
-
a flavone, 0.888 mM, pH 6.0, room temperature, 88.8% maximum inhibition
luteolin
-
IC50 is 0.17 mM
maltose
non-competitive inhibitor at concentrations higher than 20 mM
maltose
-
uncompetitive inhibition
maltose
-
0.25 M, 69% inhibition
maltose
-
86.2% relative inhibition, three concentrations of 10, 50, and 100 mM tested
maltose
-
product inhibition, the active site able to accomodate larger inhibitory complxes, resulting in a mixed type inhibition of starch hydrolysis
methanol
inhibits 7% at 20% v/v, and 13% at 50% v/v
methanol
-
20% inhibition at 10%, 40% at 20%
methanol
-
20%, 45% inhibition
Mg2+
-
-
Mg2+
22% inhibition at 1 mM
Mg2+
23% inhibition at 1 mM, 24% at 5 mM
Mg2+
-
shows no significant effect with 5 mM Mg2+, 92% relative activity, lead to inhibition with 10 mM, 48% relative activity, pH 5.0, 50°C
Mg2+
-
strong inhibition of isozyme BAA
Mg2+
-
1 mM, 11% inhibition of wild-type enzyme, 5% inhibition of mutant enzyme L134R/S320A
Mg2+
65% inhibition at 5 mM
Mg2+
-
10 mM, 50% loss of activity
Mg2+
-
82% residual activity at 2 mM
Mg2+
-
67% residual activity at 5 mM, at 80°C and pH 5.0
Mg2+
-
40% residual activity at 10 mM
Mg2+
-
30% inhibition at 1 mM, 50% at 5 mM
Mg2+
-
26% residual activity at 5 mM Mg2+ for midgut alpha-amylase and 28% residual activity at 10 mM Mg2+ for salivary gland alpha-amylase
Mg2+
-
0.1 M, 9% inhibition
Mg2+
-
10 mM, 13% inhibition
Mg2+
-
5 mM MgSO4, 18% inhibition
Mg2+
-
11% inhibition at 4 mM
Mg2+
-
1 mM MgCl2, 30% loss of activity
Mg2+
Thermomonospora vulgaris
-
10 mM MgCl2, 86% inhibition
Mg2+
-
added alone Mg2+ is inhibitory
Mg2+
69.4% residual activity at 1 mM
Mg2+
1 mM, 14% loss of activity
Mg2+
2 mM, 58% residual activity
Mn2+
5 mM, complete inhibition
Mn2+
-
inhibits enzyme activity, 50 and 21% relative activity with 5 and 10 mM Mn2+, pH 5.0, 50°C
Mn2+
-
7.1% inhibition at 1 mM, 22.4% at 5 mM
Mn2+
-
1 mM, 20% inhibition
Mn2+
-
strong inhibition of isozyme BAA
Mn2+
14% inhibition at 1 mM, 39% at 10 mM
Mn2+
-
2 mM, almost complete inhibition
Mn2+
-
complete inhibition at 1 mM
Mn2+
-
1 mM, 20% inhibition of wild-type enzyme, 15% inhibition of mutant enzyme L134R/S320A
Mn2+
70% inhibition at 5 mM
Mn2+
-
12% residual activity at 2 mM
Mn2+
-
2 mM, about 70% inhibition
Mn2+
-
80% inhibition at 1-5 mM
Mn2+
-
0.1 M, 85% inhibition
Mn2+
-
complete inhibition
Mn2+
-
5 mM MnCl2, 73% inhibition
Mn2+
49.1% inhibition at 1 mM
Mn2+
-
22% inhibition at 4 mM
Mn2+
-
1 mM, 55% loss of activity
Mn2+
inhibits 11% at 5 mM
Mn2+
Thermomonospora vulgaris
-
1 mM MnSO4, 84% inhibition
Mn2+
complete inhibition at 1 mM
Mn2+
1 mM, complete loss of activity
MnCl2
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 46% loss of activity, alpha-amylase I
MnCl2
2 mM, pH 6.5, 50°C, 40% relative activity
MnCl2
1 mM, 55% inhibition
MnCl2
-
5 mM, pH 4.0, 55°C, 44% relative activity
myricetin
-
pH 7.0
myricetin
-
a flavonol, 0.888 mM, pH 6.0, room temperature, 79% maximum inhibition
N-bromosuccinimide
1 mM
N-bromosuccinimide
-
6 mM
N-bromosuccinimide
-
0.1 mM, complete inhibition
N-bromosuccinimide
-
strong
N-bromosuccinimide
-
in the presence of 14 mM N-bromosuccinimide alpha-helix content and alpha-amlyase gt activity decrease with no observable change in beta-sheets, pH 8.0, 100°C
N-bromosuccinimide
-
1 mM, complete inhibition after 5 min
N-ethylmaleimide
-
slight inhibition
N-ethylmaleimide
-
1 mM, complete inhibition
N-ethylmaleimide
-
10 mM, 22% inhibition
Na+
-
-
Na+
12% inhibition at 1 mM, 28% at 5 mM
Na+
-
86% residual activity at 5 mM
Na+
-
alpha-amylase in 1 M NaCl and 5 mM NaCl retains 73% and 43% of its original activity after 24 h at 4ºC, respectively
Na+
-
25% residual activity at 5 mM Na+ for midgut alpha-amylase and 32% residual activity at 5 mM Na+ for salivary gland alpha-amylase
NaCl
83% of the initial activity remains in 2 M NaCl
NaCl
-
52% inhibition at 500 mM
NaCl
enzyme AmyD-1 displays extreme salt tolerance, with the highest activity in the presence of 2.0 M NaCl and 60.5% of activity in 5.0 M NaCl, 40% inhibition at 5 M
NaCl
-
the enzyme retains 63% and 40% of its original activity after 24 h at 4ºC, when NaCl concentration is 3 M and 5 M, respectively
NaCl
-
50% inhibition at 50 mM
NEM
-
-
NEM
-
inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
Ni2+
-
addition to growth medium in logarithmic phase, maximum inhibition of enzyme expression of about 70-80% at 0.85 mM. Addition to enzyme assay, 11.5% inhibition at 1.5 mM
Ni2+
-
1 mM, 82% inhibition
Ni2+
-
5 mM NiCl2, 52% inhibition
Ni2+
-
complete inhibition at 1 mM
Ni2+
-
1 mM, 23% inhibition of wild-type enzyme, 24% inhibition of mutant enzyme L134R/S320A
Ni2+
-
73% residual activity at 2 mM
Ni2+
-
1 mM, 37% loss of activity
Ni2+
-
2 mM, about 15% inhibition
Ni2+
-
60% residual activity at 10 mM
Ni2+
-
no inhibition at 1 mM, 50% at 5 mM
Ni2+
-
10 mM, 58% loss of activity
Ni2+
-
10 mM, 42% inhibition
Ni2+
-
complete inhibition
Ni2+
-
10 mM, 59% inhibition
Ni2+
-
high inhibition of isozymes AI-1 and AI-2, and AII
Ni2+
-
5 mM NiCl2, 91% inhibition
Ni2+
65.9% inhibition at 1 mM
Ni2+
1 mM, 99% loss of activity
Pb2+
5 mM, complete inhibition
Pb2+
-
74.5% inhibition at 1 mM, complete inhibition at 5 mM
Pb2+
-
2 mM, 38% inhibition
Pb2+
-
1 mM, 48% loss of activity
Pb2+
-
1 mM, pH 8.0, 24 h at 4°C, 101% and 87% residual activity for Amy I and Amy II, respectively
Pb2+
-
90% inhibition at 1 mM
Pb2+
-
5 mM, 80% inhibition
Pb2+
-
10 mM, 45% inhibition
Pb2+
-
0.1 mM, 11% inhibition
Pb2+
80.6% inhibition at 1 mM
Pb2+
-
2 mM, 53% inhibition
Pb2+
-
1 mM, 50% loss of activity
Pb2+
1 mM, complete loss of activity
Pb2+
-
20% inhibition at 5 mM
PCMB
-
-
PCMB
-
0.5 mM, 20% inhibition
PCMB
-
1 mM, 92% loss of activity
PHMB
-
-
PMSF
-
36.5% inhibition at 1mM, 53.7% at 5 mM
PMSF
-
1 mM, 14% loss of activity of the membrane-bound enzyme
PMSF
-
complete inhibition at 1.5 mM
PMSF
-
10% inhibition at 1 mM, 90% at 5 mM
PMSF
-
inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
PMSF
21.2% inhibition at 1 mM
quinic acid
-
IC50 is above 13.0 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
Rb+
-
20 mM
Rb+
-
5 mM, 33% inhibition
Rb+
-
5 mM, 30% loss of activity
SDS
with 0.1%, 0.2% and 0.5% SDS, the enzyme shows 64%, 43% and 33% activity as compared with the activity in the absence of SDS
SDS
non-reversible inactivation
SDS
39% inhibition at 10%
SDS
-
61.8% inhibition at 0.1% w/v
SDS
-
retains 30 and 12% relative activity after inhibition with 5 and 10 mM SDS, respectively, pH 5.0, 50°C
SDS
-
14.9% inhibition at 2%
SDS
-
71% residual activity at 1% (v/v)
SDS
-
90% inhibition at 20 mM, complete inhibition at 80 mM
SDS
slight inhibition at 5-10 mM
SDS
-
40% inhibition at 0.1-0.2%
SDS
mutant M197A, concentration of 10% incubation at 60°C for 1 h, 45% residual relative activity, assay at 80°C and pH 5.6
SDS
-
25% residual activity at 2 mM SDS for midgut alpha-amylase and 49% residual activity at 4 mM SDS for salivary gland alpha-amylase
SDS
71.0% inhibition at 1 mM
SDS
-
2%, pH 4.0, 55°C, 11% relative activity
SDS
1%, complete inactivation
SDS
39% inhibition at 60 mM
Secale cereale inhibitor
-
inhibitor is isolated from rye, Secale cereale, and active against alpha-amylase, dimeric crystal structure determination at 2.21 A resolution, overview
-
Secale cereale inhibitor
-
inhibitor is isolated from rye, Secale cereale, and active against alpha-amylase, dimeric crystal structure determination at 2.21 A resolution, overview
-
Sodium dodecyl sulfate
-
2.5 mM, approx. 60% inhibition at 60°C
Sodium dodecyl sulfate
-
2.5 mM, approx. 20% inhibition at 60°C
Sodium dodecyl sulfate
-
0.2%, 58% inhibition
sodium dodecylsulfate
-
-
sodium dodecylsulfate
0.1%, almost complete loss of activity
Sr2+
-
5 mM SrCl2, 36% inhibition
Sr2+
-
slight inhibition of isozymes AI-1 and AI-2, and AII
Sr2+
-
5 mM SrCl2, 28% inhibition
Triton X-100
45% inhibition at 10%
Triton X-100
-
12.4% inhibition at 10%
Triton X-100
-
83% residual activity at 5% (v/v)
Triton X-100
17% inhibition at 1 mM, 51.5% at 10 mM
Triton X-100
-
15% inhibition at 0.1%, 20% at 0.2%
Triton X-100
mutant M197A, concentration of 10% incubation at 60°C for 1 h, 71% residual relative activity, assay at 80°C and pH 5.6
Triton X-100
-
0.2%, 40% inhibition
Triton X-100
-
18% inhibition
Tween 20
-
8.9% inhibition at 20%, 9.2% activation at 10%
Tween 20
-
85% residual activity at 5% (v/v)
Tween 20
-
20% inhibition at 0.1-0.2%
Tween 20
89.4% inhibition at 1% v/v
Tween 20
-
26% inhibition
Tween 80
-
8.3% inhibition at 20%
Tween 80
-
10% inhibition at 0.1%, 25% at 0.2%
Tween 80
adversely affects alpha-amylase in the immobilized state as compared to the free enzyme
Tween 80
-
22% inhibition
Tween-20
-
-
Tween-20
mutant M197A, concentration of 10% incubation at 60°C for 1 h, 94% residual relative activity, assay at 80°C and pH 5.6
Tween-80
-
-
Tween-80
mutant M197A, concentration of 10% incubation at 60°C for 1 h, 88% residual relative activity, assay at 80°C and pH 5.6
Urea
-
91% inhibition at 2 mM
Urea
64.5% inhibition at 1%
Urea
-
retains 58 and 16% relative activity after inhibition with 5 and 10 mM urea, respectively, pH 5.0, 50°C
Urea
-
8 M, 86% inhibition
Urea
-
87.5% inhibition at 8 M
Urea
slight inhibition at 5-10 mM
Urea
-
0.6 M, 50% decrease of enzyme activity compared to control, the circular dichroism spectra in the presence of urea reveals the unfolding of the enzyme which leads to changes in both alpha-helices as well as beta-sheets content. These conformational chages could be responsible for the decline in the alpha-amylase activity
Urea
-
19% residual activity at 8 mM urea for midgut alpha-amylase and 62% residual activity at 4 mM urea for salivary gland alpha-amylase
Urea
-
inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
Urea
58.5% inhibition at 1 mM
Urea
-
5 M, pH 4.0, 55°C, 63% relative activity
Urea
51% inhibition at 6 M
Urea
25.8% residual activity at 1 mM
Vigna unguiculata defensin
-
i.e. VuD1, plant defensins are small protein consisting of 45-54 amino acids, below 62% inhibition with 0.1 mg/ml inhibitor, pH 6.5, 37°C
-
Vigna unguiculata defensin
-
i.e. VuD1, plant defensins are small protein consisting of 45-54 amino acids, below 5% inhibition with 0.1 mg/ml inhibitor, pH 6.5, 37°C
-
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
-
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
-
Vigna unguiculata defensin
-
i.e. VuD1, plant defensins are small protein consisting of 45-54 amino acids, below 60% inhibition with 0.1 mg/ml inhibitor, pH 6.5, 37°C, Lys1 from the defensin VuD1 appears to interact with residue Asp204 from the anylase ZSA, which is located inside the catalytic site, analyzed by in silico docking experiments
-
wheat amylase inhibitor
-
maximal inhibition at pH 7
-
wheat amylase inhibitor
a proteinaceous inhibitor
-
wheat amylase inhibitor
-
alpha-amylase inhibitor from wheat kernel, purification
-
wheat amylase inhibitor
from Triticum aestivum; from Triticum aestivum
-
wheat amylase inhibitor
-
alpha-amylase inhibitor from wheat kernel, purification
-
wheat amylase inhibitor
-
-
-
wheat amylase inhibitor
-
alpha-amylase inhibitor from wheat kernel, purification
-
wheat amylase inhibitor
-
alpha-amylase inhibitor from wheat kernel, purification
-
wheat amylase inhibitor
-
wheat flour protein inhibitor, formation of an enzyme-inhibitor complex
-
wheat amylase inhibitor
a proteinaceous inhibitor
-
wheat seed amylase inhibitor
-
-
-
wheat seed amylase inhibitor
-
-
-
wheat seed amylase inhibitor
-
-
Zn2+
5 mM, weak inhibition
Zn2+
-
addition to growth medium in logarithmic phase, 0.03 mM, about 50% inhibition of enzyme expression, at 1 mM 100% inhibition. Addition to enzyme assay, 36.3% inhibition at 1.5 mM
Zn2+
-
93% inhibition at 1 mM
Zn2+
36% inhibition at 1 mM
Zn2+
-
10 mM, strong inhibition of enzyme form Amyl I, Amyl II and Amyl III
Zn2+
26% inhibition at 1 mM, 73% at 5 mM
Zn2+
-
25% inhibition at 1 mM
Zn2+
-
88% inhibition at 1-5 mM
Zn2+
-
shows no significant effect with 5 mM Zn2+, 90% relative activity, lead to inhibition with 10 mM, 56% relative activity
Zn2+
-
59.2% inhibition at 1 mM, 94.3% at 5 mM
Zn2+
-
16% residual activity at 5 mM
Zn2+
-
1 mM, complete inhibition
Zn2+
-
strong inhibition of isozyme BAA
Zn2+
-
about 30% residual activity at 10 mM
Zn2+
-
2 mM 30.3% inhibition
Zn2+
-
5 mM ZnSO4, 95% inhibition
Zn2+
-
1 mM, 28% inhibition of wild-type enzyme, 37% inhibition of mutant enzyme L134R/S320A
Zn2+
-
1 mM, 87% inactivation
Zn2+
20% inhibition at 5 mM
Zn2+
-
22% residual activity at 10 mM
Zn2+
-
5% residual activity at 2 mM
Zn2+
-
1 mM, 78% loss of activity
Zn2+
-
1 mM, 87.6% inhibition
Zn2+
-
1 mM, pH 8.0, 24 h at 4°C, 94% and 64% residual activity for Amy I and Amy II, respectively
Zn2+
-
2 mM, about 85% inhibition
Zn2+
-
50% residual activity at 5 mM, at 80°C and pH 5.0
Zn2+
-
64% residual activity at 10 mM
Zn2+
-
10 mM, 80% loss of activity
Zn2+
-
0.1 M, 85% inhibition
Zn2+
-
10 mM, 60% inhibition
Zn2+
-
0.1 mM, 30% inhibition
Zn2+
-
complete inhibition of isozyme AI-1, high inhibition of isozymes AII and AI-2, at 5 mM
Zn2+
54% inhibition of wild-type and mutant enzymes at 5 mM
Zn2+
-
1 mM, 53% residual activity
Zn2+
-
5 mM ZnSO4, complete inhibition
Zn2+
80.5% inhibition at 1 mM
Zn2+
5 mM, complete inhibition
Zn2+
-
80% inhibition at 4 mM
Zn2+
-
1 mM, 37°C, 30 min, pH 6.5, 83% relative activity
Zn2+
-
1 mM ZnCl2, 45% loss of activity
Zn2+
inhibits 79% at 5 mM
Zn2+
-
0.5 mM ZnSO4, 43% inhibition
Zn2+
Thermomonospora vulgaris
-
10 mM, 84% inhibition
Zn2+
70.4% residual activity at 1 mM
Zn2+
-
35% inhibition at 5 mM
Zn2+
2 mM, no residual activity
ZnCl2
-
5 mM, 37% inhibition
ZnCl2
-
5 mM, 70% inhibition; 5 mM, 74% inhibition; 5 mM, 80% inhibition
ZnCl2
-
30 mM, complete inhibition
ZnCl2
-
10 mM, 93% inhibition
ZnCl2
1 mM, complete inhibition
ZnSO4
Halalkalibacterium halodurans
-
1 mM, 40°C, 30 min, 47% loss of activity, alpha-amylase I
ZnSO4
2 mM, pH 6.5, 50°C, 37% relative activity
additional information
-
the enzyme activity is significantly inhibited by some proteinaceous extracts from common bean cultivars, and it declines with increasing proteinaceous concentration. Proteinaceous extracts from Phaseolus vulgaris seeds are made from bean flour through heat treatment and dialysis
-
additional information
beta-mercaptoethanol, mannitol, glycerol, polyethylene glycol, and Triton X-100 do not have any significant effect even at high concentration
-
additional information
-
Cr6+ addition to growth medium in logarithmic phase, maximum inhibition of about 70-80% at 1.15 mM; effect of a combination of different concentrations of two (Ni2+ + Zn2+, Cu2+ + Zn2+, Hg2+ + Ni2+, Hg2+ + Zn2+) or three metals (Hg2+ + Zn2+ + Ni2+) added to the logarithmic growth phase examined: in all cases an inhibitory effect higher than of the single metal is observed; Mn2+ addition to growth medium in logarithmic phase, 10% inhibition at about 1.1 mM of enzyme expression
-
additional information
-
Vigna unguiculata defensin i.e. VuD1, plant defensins are small protein consisting of 45-54 amino acids, no inhibition with 0.1 mg/ml inhibitor, pH 6.5, 37°C
-
additional information
-
no inhibition by Mn2+
-
additional information
-
the enzyme activity is not affected by Tween 20, Tween 40, Tween 60, and Tween 80 at 0.1% w/v
-
additional information
-
no or poor inhibition by Ba2+, K+, Ca2+, Mn2+, and Co2+ at 5-50 mM and by SDS, PMSF, Triton X-100, and Tween 20 at 1-5%
-
additional information
-
no effect by 5-10 mM of urea and glycerol, poor effects by 0.5-1% sodium tetraborate
-
additional information
-
no inhibition by PMSF; not inhibited by phenylmethylsulfonyl fluoride
-
additional information
-
not inhibited by 100 mM EDTA
-
additional information
-
not affected by NaCl, KCl, phenylmethylsulfonyl fluoride, and beta-mercaptoethanol
-
additional information
-
no inhibition by EGTA or EDTA at 1-10 mM
-
additional information
-
wild-type and mutant enzymes exhibit sensitivity towards GdnHCl-induced denaturation, effects of several commercial detergent products on the activities of the enzyme mutants, overview
-
additional information
-
the enzyme is resistant to SDS
-
additional information
-
mo inhibition by EDTA or EGTA
-
additional information
no effect by 5 mM EDTA
-
additional information
-
not inhibitory: EDTA, Ca2+
-
additional information
-
isozyme Amy3 is not inhibited by the proteinaceous inhibitor from bean alphaAI-1; isozymes Amy1 and Amy2 are not inhibited by the proteinaceous inhibitor from bean alphaAI-1 and by the proteinaceous inhibitor from wheat WI-3
-
additional information
isozyme Amy3 is not inhibited by the proteinaceous inhibitor from bean alphaAI-1; isozymes Amy1 and Amy2 are not inhibited by the proteinaceous inhibitor from bean alphaAI-1 and by the proteinaceous inhibitor from wheat WI-3
-
additional information
no or poor effects by glucose, sucrose, maltose, mannitol, trehalose, sorbitol, myo-inositol, and iodoacetate at 5-10 mM
-
additional information
-
not inhibited by phytic acid
-
additional information
-
no or poor effect by 10-20% of acetone and benzol
-
additional information
-
no inhibition by phytate at up to 10 mM
-
additional information
-
not inhibited by aromatic hydrocarbon (benzene, etc.)
-
additional information
isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview; isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview
-
additional information
isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview; isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview
-
additional information
-
isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview; isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview
-
additional information
-
no effect by the addtion of 0.1% dimethyl sulfoxide and 0.01% Triton X-100
-
additional information
-
the inhibitory activity of the flavonoids toward human alpha-amylase depends on the formation of 1. hydrogen bonds between the hydroxyl groups in position R7 and/or R4' of the polyphenol ligands and the catalytic residues of the binding site Asp197 and Glu233 and 2. formation of a conjugated pi-system between either the AC- or B-ring system and Trp59, that stabilizes the interaction with the active site
-
additional information
-
structure-activity relationship of benzoxazinones and related compounds in inhibition of the enzyme, overview
-
additional information
-
not inhibitory: D-glucose
-
additional information
not inhibitory: NaCl up to 250 mM
-
additional information
-
not inhibitory: NaCl up to 250 mM
-
additional information
-
treatment with glycosidases leads to loss of 50% activity
-
additional information
-
no inhibition with Murraya koenigii leaf extract
-
additional information
-
no inhibition with voglibose, 23-hydroxyursolic acid, maslinic acid, asiatic acid, arjunolic acid, and oleanolic 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 by the plant defensin VrD2. A VrD2 chimera that is produced by transferring the proposed functional loop of VrD1 onto the structurally equivalent loop of VrD2 inhibits alpha-amylase activity
-
additional information
enzyme TfAmy48 shows excellent compatibility with some commercial laundry detergents, overview. No or poor effects by 1 mM PMSF, 2 mM diiodopropyl fluorophosphate, 10 mM EDTA, or 1 mm EGTA
-
additional information
-
enzyme TfAmy48 shows excellent compatibility with some commercial laundry detergents, overview. No or poor effects by 1 mM PMSF, 2 mM diiodopropyl fluorophosphate, 10 mM EDTA, or 1 mm EGTA
-
additional information
-
the enzyme is inhibited by several metal ions
-
additional information
EDTA, dithiothreitol, N-bromosuccinimide, 2-mercaptoethanol (1 mM), and SDS (2% (w/v)) have no effect on activity
-
additional information
-
EDTA, dithiothreitol, N-bromosuccinimide, 2-mercaptoethanol (1 mM), and SDS (2% (w/v)) have no effect on activity
-
additional information
Li+ and Na+ do not show significant inhibitory effect
-
additional information
-
Li+ and Na+ do not show significant inhibitory effect
-
additional information
-
from Peganum harmala, Centaurium erythraea and Aristolochia baetica causes strong inhibition of alpha-amylase activity
-
additional information
-
no inhibitionj by alphaAI-PF, i.e. alpha amylase inhibitor from Palo Fierro seeds
-