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5 mM, 112% of initial activity
-
protects enzyme from inhibition
-
strongly reducing enviroment required
-
about 1575.34% activity at 1 mM
-
about 182.8% activity at 1 mM
-
1 mM, increases activity by 13%
-
1 mM, slight activation
-
2 mM, 115% of initial activity
-
stimulation at low concentration, inhibition at high concentration
-
reuired. About 1% residual activity in absence of 2-mercaptoethanol
-
required for maximal activity, 292.3% activity at 1% (v/v)
-
maximal activation at 20 mM
-
hydroxylation is not supported when NADH, NADPH, dithiothreitol, 2-mercaptoethanol and ascorbic acid are added alone to the reaction mixture, stimulation when added together with tetrahydropteridine
-
30 mM, 79.3% activity compared to activation with dithiothreitol
-
essential for activation
-
activates, optimal concentration is 3.3 mM
-
optimal concentration: 2 mM
-
required for activity with merthiolate
-
thiol compound required, optimal concentration is 0.5 mM
-
25 mM, maximal activation, 70% of activity with dithiothreitol
-
reduces lag phase before attainment of steady state rate in conjunction with NAD+
-
10 mM, 2fold activation of the oxidation of D-glyceraldehyde 3-phosphate
highest activation at 1 mM
maximal activation at 5 mM, dependent on sulfhydryl compound
convenient source of exogenous mercaptan, 5 mM
-
reactivation of purified enzyme preparation
-
0.1 M required for maximal activity
-
restores the activity after inactivation with p-chloromercuribenzoate
-
loss of about 50% of original acitivity after exhaustive dialysis, renaturation in presence of 2-mercaptoethanol
-
requirement of sulfhydryl protective reagent, maximal activity with 10 mM to 0.1 M dithiothreitol or mercaptoethanol
-
strongly dependent on presence of
-
100 mM, full activation
-
27% increased activity at 1 mM
-
about 140% activity at 5 mM
-
highest activity at 50 mM
-
161.09% activity at 1 mM
-
loss of about 80% of original acitivity after exhaustive dialysis, renaturation in presence of 2-mercaptoethanol
-
1 mM, activity is enhanced more than 2fold
-
1 mM, activity increases by 27%
-
1 mM, activity increases by 61%
-
maximal activity at 50 mM
-
0.175 mM restores inhibited enzyme after 3 min incubation to 90% of full activity
-
slight activatory effect
-
1%, presence of a reducing agent is essential for enzyme activity
-
required for full activity
-
presence of 2-mercaptoethanol or dithiothreitol at 10 mM required for maximal activity
-
thiol compound required for maximal activity on glycine-CO2 exchange reaction
-
5 to 15 mM: 1.7fold increase in activity, higher concentrations have no further effect, it may reduce oxidized Cys-707 or another important sulfhydryl group
dehydrogenase and hydrolase activities are dependent on the presence of high concentrations of 2-mercaptoethanol to prevent the oxidative degradation of the substrate 10-formyltetrahydrofolate
optimal dehydrogenase activity requires 15 mM or higher concentrations
required for the in vitro assay
-
2 mM, stimulates up to 2fold
-
enhances activity, can replace NADH
-
2 mM required for maximal activity
-
in absence of mercaptoethanol 50% of maximal velocity
-
enzyme activity is strongly enhanced in presence of 5 mM 2-mercaptoethanol
-
1 mM, stimulates about 2.1fold
-
5 mM, enhances the activity by 13%
-
increases activity at low substrate concentrations
reducing agent required for activity
-
essential for maximum activity
essential for maximum activity
essential for maximum activity
essential for maximum activity
essential for maximum activity
essential for maximum activity
essential for maximum activity
essential for maximum activity
essential for maximum activity
using a redox-inert methyl acceptor, it is shown that BHMT requires a thiol reducing agent for activity. Short-term exposure of BHMT to reducing agent-free buffer inactivates the enzyme without causing any loss of its catalytic zinc. Activity can be completely restored by the re-addition of a thiol reducing agent
7% activity increase at 20 mM
-
5 mM, required for optimum activity
-
47.8% activity in absence of both EDTA and mercaptoethanol
-
required in high concentration, 0.5 M
required in high concentration, 0.5 M
1 mM is required for optimal activity
-
2fold increase at 20 mM
-
also leads to increased formation of by-products
-
essential for arginylation of chromatin
-
requirement, 0.1 M, stabilizes the enzyme in a reduced state
-
10-20 mM, reducing reagent is required for maximal activity
-
purified enzyme does not require 2-mecaptoethanol or anaerobic conditiones for maximal activity
-
stimulates up to 20fold
-
10 mM, activation to 141% of control
-
detergent required for maximal activity
-
without addition 73% decrease of activity, suggesting a thiol function necessary for activity
-
10% stimulation at 1 mM
-
1.0 mM, relative activity 250%, 10 mM, relative activity 260%, in absence enzyme solutions will lose up to 35% activity in 1 week, activity is not recoverable by addition of 2-mercaptoethanol
-
activity dissappears in absence
-
5 mM, stimulation of 79%
-
stimulates the enzyme activity
-
1-30 mM, 4fold-stimulation
-
1 mM, activation to 120%
-
14 mM, activation of isoenzyme F3GT1 to 160%, activation of isoenzyme F3GT2 to 136%
-
14 mM, activation to 157%
-
14 mM, stimulates to 134%
-
required for optimal activity
-
required by AT1 transferase, activates AT2 transferase
-
activation, together with SDS or guanidine hydrochloride
-
strong stimulation even in the presence of Mg2+
-
0.18 mM, 392% activation of purified sialyltransferase-1, 1120% activation of sialytransferase-1 activity in microsomes
-
10 mM, 1.2fold stimulation
10 mM, 1.2fold stimulation
10 mM, 1.2fold stimulation
10 mM, 1.2fold stimulation
complete reactivation at 3.3 mM but inhibition at 33 mM
-
reactivates enzyme less effectively than dithiothreitol
-
similar effects as pyridine at 10 mM probably due to its action as secondary substrate
-
10 mM, not as effective as dithiothreitol
-
preincubation, activates
-
activation only in the presence of pyridoxal phosphate
-
1.0 mM, relative activity 101%
-
20 mM, 70% of activity with dithiothreitol
-
20 mM, increases ribulokinase activity up to 175%
-
1-2.5 mM, 40-50% activation of Pb2+-precipitated uridine kinase
-
reverses inhibition with p-chloromercuribenzoate and loss of activity during storage
-
5 mM, 2-4fold stimulation
-
activation, can replace DTT
activation, can replace DTT
activation, can replace DTT
activation, can replace DTT
at 5 mM: reduction in molecular weight from approximately 53000 Da to 17000 Da. This low molecular weight form is partially active in the presence of 2-mercaptoethanol. In absence of 2-mercaptoethanol the low molecular weight form is inactive. At 50 mM: full reactivation of the CMP(ATP) kinase activity followed by dCMP(ATP) and CMP(dCTP)
-
activation, at high concentration
-
1 mM is required for optimal activity of both crude and purified enzyme
-
20-30 mM, 3fold stimulation with N-acetylneuraminate as substrate, 1.5fold increase in activity with 4-O-methyl-N-acetylneuraminate as substrate
-
5 mM, activation to 138% of original activity
-
maximal activation, 210%, at 1 mM
-
enhances the degree of streptomycin inactivation
-
required for maximal activity
20 mM, 3fold activation
-
enhances enzyme activity
-
activates in direction of SCN-formation at low CN- concentrations
-
requires a thiol for optimal sulfur transfer
-
optimum concentration: 10 mM
-
activates, degree of activation is more marked with preparations previously stored at 0°C or -10°C
-
1 mM, Est55, 33% stimulation, Est30, 7% stimulation
-
1% v/v, 141.5% activity
-
1% (v/v) activates carboxylesterase in a range of 136% and 244% after 0 and 30 min of incubation
-
about 160% activity at 10 mM
-
1 mM, 143% of initial activity
-
13% stimulation at 1 mM, 24 h preincubation
-
subtle stimulation of enzymatic activity at 10 mM
-
1.8fold enhancement of activity at 90% (v/v)
1.9fold enhancement of activity at 90% (v/v)
minimizes loss of activity in presence of sulfhydryl reagent
-
112.2% activity at 1 mM
-
required for 100% activity
-
enzyme form H2 is inactive in absence of mercaptoethanol. No effect on enzyme form H1
-
phosphatase activity is increased to up to 49-62% by 3 mM
phosphatase activity is increased to up to 49-62% by 3 mM
phosphatase activity is increased to up to 49-62% by 3 mM
phosphatase activity is increased to up to 49-62% by 3 mM
phosphatase activity is increased to up to 49-62% by 3 mM
phosphatase activity is increased to up to 49-62% by 3 mM
phosphatase activity is increased to up to 49-62% by 3 mM
maximal activation at 50 mM, absolute requirement for SH compounds
-
2fold activation of kcat, 14fold activition combined with trypsin cleavage
-
activates, enhancement of the enzyme activity by reducing agents might be expressed via the reduction of Fe2+ at the metal center
-
0.1 mM, 59% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
6% increase of activity at 20 mM
6% increase of activity at 20 mM
6% increase of activity at 20 mM
6% increase of activity at 20 mM
6% increase of activity at 20 mM
6% increase of activity at 20 mM
0.1 mM, 59% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
activates in vivo by severalfold
-
requirement, or other SH-reducing agents
-
activation, less effective than DTT
-
1.6fold stimulation at 10 mM, 2.5fold stimulation at 100 mM
1.6fold stimulation at 10 mM, 2.5fold stimulation at 100 mM
1.6fold stimulation at 10 mM, 2.5fold stimulation at 100 mM
1.6fold stimulation at 10 mM, 2.5fold stimulation at 100 mM
1.6fold stimulation at 10 mM, 2.5fold stimulation at 100 mM
1.6fold stimulation at 10 mM, 2.5fold stimulation at 100 mM
1.6fold stimulation at 10 mM, 2.5fold stimulation at 100 mM
1.6fold stimulation at 10 mM, 2.5fold stimulation at 100 mM
5 mM, pH 4.0, 55°C, 172% relative activity, strongly increase the activity, probably due to a better accessibility of the substrate to the catalytic site after disruption of the intersulfide bridge
5 mM, pH 4.0, 55°C, 172% relative activity, strongly increase the activity, probably due to a better accessibility of the substrate to the catalytic site after disruption of the intersulfide bridge
5 mM, pH 4.0, 55°C, 172% relative activity, strongly increase the activity, probably due to a better accessibility of the substrate to the catalytic site after disruption of the intersulfide bridge
5 mM, pH 4.0, 55°C, 172% relative activity, strongly increase the activity, probably due to a better accessibility of the substrate to the catalytic site after disruption of the intersulfide bridge
5 mM, pH 4.0, 55°C, 172% relative activity, strongly increase the activity, probably due to a better accessibility of the substrate to the catalytic site after disruption of the intersulfide bridge
5 mM, pH 4.0, 55°C, 172% relative activity, strongly increase the activity, probably due to a better accessibility of the substrate to the catalytic site after disruption of the intersulfide bridge
5 mM, pH 4.0, 55°C, 172% relative activity, strongly increase the activity, probably due to a better accessibility of the substrate to the catalytic site after disruption of the intersulfide bridge
5 mM, pH 4.0, 55°C, 172% relative activity, strongly increase the activity, probably due to a better accessibility of the substrate to the catalytic site after disruption of the intersulfide bridge
slightly activates the recombinant enzyme
slightly activates the recombinant enzyme
slightly activates the recombinant enzyme
slightly activates the recombinant enzyme
slightly activates the recombinant enzyme
slightly activates the recombinant enzyme
slightly activates the recombinant enzyme
slightly activates the recombinant enzyme
2.3fold increase of activity by 1 mM
-
about 120% activity at 1% (v/v)
-
maximal activation at 150 mM
-
2 mM, 143% of initial activtiy
-
10 mM, required for maximal activity
10 mM, required for maximal activity
1 mM, slight activation
-
131.6% activity at 5 mM
-
slight activation at 0.1-0.5 mM
-
1 mM, 177% of initial activity
-
slight activation, 600 mM are required for maximal activity, cannot substitute for DTT
-
129.9% relative activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 1-2 mM
500 mM, 2fold activation, inhibition above
slight activation at 1 mM
the purified enzyme shows 152.9% relative activity at 1% (v/v)
107.8% activity at 10 mM
-
required for enzymatic activity
-
activity enhanced by 2fold
-
1 mM, slight activation (6%), strain L461
-
1 mM, slight activation (9%), strain L103
-
53% rise in activity in the presence of 10 mM 2-beta-mercaptoethanol
-
the lower concentrations (1-10 mM) of 2-mercaptoethanol show a stimulating effect on activity
-
slight activation up to 2.5 mM
-
1 mM, activation to 112% of control
-
134.4% activity at 1 mM
-
12% activation at 1 mM, 20% at 10 mM
-
activates 1.2fold at 10 mM
-
9,6-10% activation at 1-5 mM
-
0.1%, 179% of initial activity
-
1 mM, 242% of initial activity
-
10 mM, 1.8fold stimulation
-
118.4% relative activity
-
129.7% relative activity
-
24.7% activation at 5 mM
-
5 mM, 174% of initial activity
-
1 mM, 131% of initial activity
-
1% v/v, 149% of initial activity
-
2 mM, 143% of initial activtiy
-
10 mM, 1.1fold asctivation
-
1 mM, 1.2fold activation
-
blocks inhibition by Hg2+-ions
-
1 mM, relative activity 102%
-
2 mM, 119% of initial activity
-
slight activation at 75 mM
-
116.31% activity at 5 mM
-
slight activation at 5 mM
-
1 mM, 115% of initial activity
-
activation to 132.1% at 5 mM
-
1 mM, 11% increase in activity
-
1 mMm, 121% of initial activity
-
123.7% activity at 1 mM
-
153% of initial activity
-
about 110% activity at 100 mM
-
moderate activation at 1 mM
-
0.5%, 155% of initial activity
-
31% increased activity at 1 mM
-
5 mM, 140% of initial activity
-
5 mM, 152% of initial activity
-
activates 1.6fold at 10 mM
-
activates 1.9fold at 10 mM
-
activates by 35% at 10 mM
-
isoform xyl I, 59% activation, xyl II, 102% activation
-
10 mM enhances the activities of XynAS27, XynAS27cd, and XynAS27cdl by about 1.5, 1.7, and 1.4fold, respectively
-
10 mM enhances the activity about 1.6fold
-
52.66% increase of activity at 2 mM
-
enhances the activity about 1.3- and 1.6fold at the concentrations of 1 and 10 mM, respectively
-
30% increase in activity
-
beta-mercaptoethanol even at a low concentration of 10 mM increases the activity of AgaA by 23%
-
lower effect on P-beta-gal II than P-beta-gal I
-
136.5% activity at 0.5 mM
-
ovalbumin, fetuin, bromelain, ovomucoid, alpha1-acid glycoprotein, immunoglobulin G and influenza virus hemagglutinin are susceptible only after reduction and alkylation or in presence of 1% 2-mercaptoethanol
-
1 mM, 110% of initial activity
-
103.1% activity at 10 mM
-
141.05% activity at 0.5% (v/v)
-
about 135% activity at 10 mM
-
increases of the hydrolysis activity
-
enzyme activity stabilized by
-
requires reducing agents, only 67% of maximal activity is observable in absence
-
activates, 30% activation at 17 mM
-
5 mM, 2fold stimulation
-
11% activation at 10 mM
-
3.9fold activation at 1.0 mM
-
restores activity after deactivation with p-chloromercuribenzoate
-
1 mM, activation to 160% of control
-
SH compound required, efficient activator at 25 mM
-
0.1 mM, 108% of initial activity
-
active-site thiol is very sensitive to oxidation and requires reductants
active-site thiol is very sensitive to oxidation and requires reductants
activation of the cytsolic isozyme, but not of the extracellular isozyme
-
94% activation at 1 mM, 70% at 5 mM
-
2.0 mM, 1.75fold activation
-
activates
36625, 36619, 36636, 36638, 34989, 36652, 35024, 36629, 36656, 36658, 36653
-
reduction is essential for catalytic activity, once the enzyme is activated by the reducing agent, the presence of the activator is no longer necessary for catalytic activity
-
strong activation of hydrolysis of insulin or albumin, at pH 4.0 and at pH 5.5
-
activates, synergistic with EDTA
-
not as effective in activation as cysteine
-
highest activity at 96 mM, at 37°C and pH 7.0
-
weak activation, a concentration above 100 mM is required
-
30 mM, 197% increase in activity
-
required for maximal activity
half-maximal activation at 1.4 mM
-
activates at low concentrations
-
enzyme that has been exposed to air in solution lacking thiol compounds shows very marked stimulation of activity by low concentrations of 2-mercaptoethanol
-
146% activity at 0.5% (v/v)
-
1 mM, 113% of initial activity
1 mM, 1.19fold activation
-
2 mM, 2fold increase in activity
-
138.22% activity at 100 mM
-
10 mM, 108% of initial activity
-
14% increase of activity at 0.1 mM for IsoI and 11% increase of activity at 1 mM for IsoII
-
1 mM, relative activity 108%
-
enzyme requires dCTP, Zn2+, and 2-mercaptoethanol
-
restores activity of pCMB treated enzyme up to 75%
-
1.4fold at 50 mM, 1.6fold activation at 100 mM
-
50-500 mM, 25% stimulation
-
maximum stimulation at 75 mM
-
absolute requirement for activity
absolute requirement for activity
reducing agents in optimal concentrations of 20 mM or above are a prerequisite for high CO2 fixation turnovers, with dithiothreitol enhancing the carboxylation 16.2fold compared with a control without reducing agent, followed by ascorbate (15.5fold), Na2S2O5 (13.6fold) and 2-mercaptoethanol (7.2fold)
-
slight stimulation of activity at 10 mM
-
sulfhydryl compound such as 2-mercaptoethanol, activates the C-His-rMtFBA activity slightly, 15%
10 mM: 103% of maximal activity, slight activation
-
stimulation at 3.05 and 6.1 mM
-
41% increase of activity at 1 mM
-
50 mM, enhances activity 2fold
-
activates kidney enzyme
-
0.005 mM, 2.8fold stimulation
-
increases the activity of isozyme CAH7 by 69% but has no effect on the activity of isozyme CAH8
increases the activity of isozyme CAH7 by 69% but has no effect on the activity of isozyme CAH8
increases the activity of isozyme CAH7 by 69% but has no effect on the activity of isozyme CAH8
increases the activity of isozyme CAH7 by 69% but has no effect on the activity of isozyme CAH8
increases the activity of isozyme CAH7 by 69% but has no effect on the activity of isozyme CAH8
increases the activity of isozyme CAH7 by 69% but has no effect on the activity of isozyme CAH8
increases the activity of isozyme CAH7 by 69% but has no effect on the activity of isozyme CAH8
increases the activity of isozyme CAH7 by 69% but has no effect on the activity of isozyme CAH8
required at very low concentrations of substrate
sulfhydryl compound is required for maximal activity
-
sulfhydryl compounds required, 50 mM 2-mercaptoethanol in presence of 0.8 mM FeSO4 is optimal
-
increases activity up to 3fold. Activation modulates thermotolerance at 50°C
-
10 mM, 124% of initial activity
-
10 mM, 135% of initial activity
-
1 mM, slight stimulation
-
5 mM, required for full activity
-
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
activates at concentrations up to 10 mM
-
0.5 mM, enhances activity
-
2-mercaptoethanol or thiols like such as dithiothreitol are required for the isomerization reaction of the lyase: without, only the phycocyanobilin addition product is formed, but no [phycoerythrocyanin alpha-subunit]-Cys84-phycoviolobilin. Too much 2-mercaptoethanol will cause the loss of chromophore, in a reaction requiring oxygen. When Mg2+ is used as the activator, the optimal concentration of 2-mercaptoethanol is 5 mM, with Mn2+ it is 3 mM
-
activates, (Z)-phenylacetaldoxime dehydration, 1 mM, 2.13fold
-
the enzyme activity is enhanced 1.8fold by 1 mM
-
stimulates 2-2.5fold at 0.05 M
-
optimal concentration: 0.02 M
-
activates isomerase III and IV
-
100% activity at 0.5 mM
-
stimulates, 2.25fold stimulation at 20-30 mM
-
component S requires treatment with 2-mercaptoethanol to show maximal activity. Component E does not require this treatment
-
5 mM, required for full activity
-
0.01 mM, 100% stimulation
0.01 mM, 100% stimulation
0.01 mM, 100% stimulation
45 mM: 3.5fold enhancement of activity, 200 mM: 25% decrease in activity
-
inhbibition above 100 mM
-
maximal activity at 30-50 mM
-
maximal stimulation at 25 mM
-
without 2 mM dithiothreirol or 2-mercaptoethanol in the reaction mixture, CofF activity is up to 5fold lower
-
maximal concentration 2.5 mM
required for optimal activity, above 50 mM increase activity to 221%
-
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60% inhibition at 10 mM
-
rapid inactivation at 1 mM
-
0.5 mM, complete inhibition
-
inhibits 38% at 25 mM, reduction reaction
-
1 mM, 20.3% residual activity
-
17% reduced activity; 87% residual activity
-
preincubation of gamma-hydroxybutyrate reductase revealed no inhibitory effect
-
in 100 mM MES buffer (pH 6.5) with 200 mM NADPH, 0.25 mM decanal, and 125 microg of FALDR fusion protein. 1 mM inhibits by 25%
-
30 mM, 50% inhibition, partially reversed by diamide
-
2.3% inhibition at 1 mM
-
inhibition level depends on the substrate used, about 40% inhibition at 10 mM
-
activates at 1 mM, inhibitory at 10 mM
-
inhibits both the reductase and dehydrogenase reactions by 30% at 1 mM
-
1 mM, pH 9, 22°C, rapid inactivation
-
inactivation in absence of Mg2+
-
1 mM, room temperature, pH 9.0, rapid inactivation
-
strong inhibition, IC50 0.3 mM
-
strongly inhibitory at 100 mM, but slight activation in lower concentration, 1 mM
-
competitive inhibition; competitive inhibitor
-
competitive. In crystal structure, the mercaptoethanol molecule is located in the catalytic cleft formed by residues Ser141, Ileu142, Ala143, Phe148, Tyr154, Pro184, Gly185, Ileu186, Met191, Trp192 and Ile195. These residues may also be involved in substrate recognition and in stereospecific redox reactions
-
5 mM, 37% inhibition, incubation for 1 min
-
isoenzyme 1, 1 mM, 19% inhibition
-
10% inhibition at 1 mM, 95% inhibition at 10 mM
-
1%, 40% loss of activity
-
25% inhibition at 0.01 mM
-
complete inhibition at 0.02 mM
-
0.05 mM, 29% loss of activity
-
0.1 mM, 65.5% inhibition
-
1 mM, complete inactivation
-
12.5 mM, complete inhibition
-
5 mM, 15% loss of activity
-
competitive, complete inhibition
-
complete inhibition at 0.1 mM
-
complete inhibition of laccase activity at 0.1% concentration
-
70.3% activity remaining at 1 mM
-
enzyme form C: 50% inhibition at 5 mM, 6 min, 100% inhibition after 18 min
-
not inhibitory at 0.5 mM, 31% inhibition at 5 mM
-
5 mM, about 60% inhibition
-
85% inhibition at 0.1 mM, complete inhibition at 1 mM
-
2 mM, complete inhibition
-
55% residual activity at 1 mM; 70% residual activity at 1 mM
-
30 mM, 14% residual activity
-
complete inhibition at 23 mM, summation effect with p-chloromercuribenzoate
-
slight inhibition for all three isoforms at 10 mM
-
4 mM, 80% without substrate, 78% inhibition in presence of substrate
-
94% inhibition at 1 mM; 94% inhibition at 1 mM; 96% inhibition at 1 mM; 96% inhibition at 1 mM
-
2 mM, 23% residual activity
-
complete inhibition at 1 mM
-
the sulfoxidation of thiobenzamide, catalyzed by isoform PXG1, is completely abolished in the presence of 1 mM 2-mercaptoethanol (competitive inhibitor)
-
0.1 mM, 10 min, 98% inhibition
-
0.0005 mM, 64.5% inhibition
-
0.5 mM, 80% inhibition, Cu2+ protects
-
inhibition at high concentration, activation at low concentration
-
1 x the Km for cysteine = 4.8% inhibition, 10 x the Km for cysteine = 11% inhibition
-
1 x the Km for cysteine = 5.9% inhibition, 10 x the Km for cysteine = 13% inhibition
-
SCO3035: 1 x the Km for cysteine = 8.6% inhibition, 10 x the Km for cysteine = 15% inhibition; SCO5772: 1 x the Km for cysteine = 2.6% inhibition, 10 x the Km for cysteine = 13% inhibition
-
YubC: 1 x the Km for cysteine = -0.7% inhibition, 10 x the Km for cysteine = 6.6% inhibition
-
2 mM, total activity loss
-
preincubation with substrate protects against inactivation
-
5 mM, 2% residual activity; 5 mM, complete inhibition
-
1 mM, relative activity remaining 2%
-
67.3% inhibition at 0.5 mM
-
0.029 mM, 50% inhibition
-
0.1 mM, complete inhibition
-
1 mM, complete inhibition
-
evaluated for effectiveness as an inhibitor of PPO activity, using catechol as the substrate
-
complete inhibition at 1.0 mM
-
complete inhibition at 10 mM
-
uncompetitive inhibition
-
25% inhibition of Mn-reconstituted wild-type enzyme at 10 mM, no inhibition at 1 mM
gradual inhibition by increasing concentration of 2-mercaptoethanol, 20% inhibition at 2 mM, 36% at 16 mM
strong inhibition at 10 mM
10% (v/v), 55% inhibition
-
0.5 mM concentration 40% inhibition
-
100% inhibition at 0.01 mM concentration
-
0.68 mM, 50% inhibition
-
at high concentrations beta-mercaptoethanol is inhibitory
-
15.21% residual activity at 5 mM
-
complete inhibition at 5 mM
-
complete inhibition of isoform LAAOII and about 50% inhibition of isoform LAAOI at 5 mM
-
2.94% residual activity at 0.5 mM
-
72% residual activity at 0.2% (v/v)
-
73.3% residual activity at 0.2% (v/v)
-
53% after 30 min at 0.5 mM
-
62.98% residual activity at 20% (v/v)
-
about 60% residual activity after 1 h incubation with 0.5 mM beta-mercaptoethanol at pH 8.5 and 25°C
-
1 mM, 20.2% residual activity
-
1 mM, 16% inhibition, production of methyl iodide
-
slightly at high concentration, 10 mM
-
rapid, reversible inactivation, deactivation is a non-destructive transfer of an H atom equivalent to quench the glycyl radical
-
membrane-bound enzyme is insensitive, solubilized enzyme is inactivated
-
slight inhibition of free and immobilized enzyme
-
slight inhibition at 50 mM
-
10% (v/v), 9% inhibition; 91% inhibition
slight inhibition of the isozyme
-
29.65% residual activity at 1 mM
-
1 mM, 87% of initial activity
-
modification of alpha-lactalbumin
-
D-enzyme, slight inhibition
-
1 mM: 50% loss of activity, 10 mM: 90% inhibition
-
complete inhibition of activity with lacto-N-biose I
-
XT-II activity is completely abolished at a concentration 1% (v/v) beta-mercaptoethanol
-
marked decrease in activity, NAD+ and dithiothreitol protects
-
slightly inhibits NADH kinase
-
5 mM, 15% loss of activity (recombinant enzyme expressed in Sulfolobus solfataricus). 5 mM, 25% loss of activity (recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I)). 5 mM, 22% loss of activity (recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II))
-
96% residual activity at 1 mM
-
10 mM, 16% loss of activity; 16% inhibition at 10 mM
-
1 mM, 77% residual activity
-
1 mM, 94% residual activity
-
1 mM, 16% of initial activity
-
73.5% residual activity at 5 mM
-
1 mM, 68.3% remaining activity
-
16% residual activity at 1 mM
-
complete inhibition at 1%
-
inhibits both isozymes TAH I and TAH II
-
1 mM inhibits activity by 85%
-
37.07% residual activity at 20 mM
-
59.4% residual activity at 1 mM
-
63% residual activity at 1 mM
-
about 10% residual activity at 1 mM
-
50% residual activity at 1 mM
-
45% inhibition between 2-10 mM
-
traces of activity remain with 10 mM at pH 7.5
-
43% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
BTID-A, 26% inhibition at 1% w/v
maximal inhibition of 32% at 1 mM of recombinant refolded enzyme
reduces the enzyme activity to 48% after 1 h
about 75% inhibition at 1 mM, about 99% inhibition at 5 mM
1 mM, 83% of initial activity
-
slight inhibition at 10 mM
-
1% (v/v): 20% activity, compared to no addition
-
strong inhibition at 4 mM
-
0.5%, 47% loss of activity
-
complete inhibition at 0.1 M
-
10 mM, 20% of inhibition
-
inactivation, reversal by the addition of 4 mM CaCl2, no inactivation if CaCl2 is present during the reducing reaction
-
inhibition after treatment with EGTA
-
inhibition, but reversal by addition of 3 mM CaCl2
-
little effect on activity at 10 mM
-
10 mM, 70% decrease in activity
-
68% inhibition at 1 mM, 86% inhibition at 10 mM
-
the P2 isoenzyme is more sensitive to 2-mercaptoethanol than P1
-
phosphatase activity is decreased by 5 mM
phosphatase activity is decreased by 5 mM
phosphatase activity is decreased by 5 mM
phosphatase activity is decreased by 5 mM
phosphatase activity is decreased by 5 mM
phosphatase activity is decreased by 5 mM
phosphatase activity is decreased by 5 mM
72.72% residual activity at 0.1% (w/v); 75.98% residual activity at 0.1% (w/v); 92.8% residual activity at 0.1% (w/v)
-
20% inhibition at 1 mM, 66% at 5 mM
-
inhibits 20% at 1 mM and 60% at 5 mM
-
low inhibition at 1-10 mM
-
with 1 mM stabilization of activity at pH 3.5 and 4.0
-
with 4 mM 50% of activity with denaturated DNA
-
inactivation reversed by Zn2+
-
substrate: sphingomyelin
-
46% inhibition at 25 mM
-
prior incubation, loss of thermostability
1 mM, 70% residual activity, both free and immobilized enzyme
-
1 mM, 81% of initial activity, mutant H260L
-
10 mM, 43% residual activity
-
at 37°C, 1 mM reduces activity by 52%
-
58% inhibition at 10 mM
-
73% inhibition at 10 mM
-
1 mM, 23% loss of activity
1 mM, 23% loss of activity
1 mM, 23% loss of activity
1 mM, 23% loss of activity
1 mM, 23% loss of activity
1 mM, 23% loss of activity
1 mM, 23% loss of activity
1 mM, 23% loss of activity
20% inhibition at 1 mM, 30% at 5 mM
20% inhibition at 1 mM, 30% at 5 mM
20% inhibition at 1 mM, 30% at 5 mM
20% inhibition at 1 mM, 30% at 5 mM
20% inhibition at 1 mM, 30% at 5 mM
20% inhibition at 1 mM, 30% at 5 mM
20% inhibition at 1 mM, 30% at 5 mM
20% inhibition at 1 mM, 30% at 5 mM
37.6% inhibition at 1 mM, 43.7% at 5 mM
37.6% inhibition at 1 mM, 43.7% at 5 mM
37.6% inhibition at 1 mM, 43.7% at 5 mM
37.6% inhibition at 1 mM, 43.7% at 5 mM
37.6% inhibition at 1 mM, 43.7% at 5 mM
37.6% inhibition at 1 mM, 43.7% at 5 mM
37.6% inhibition at 1 mM, 43.7% at 5 mM
37.6% inhibition at 1 mM, 43.7% at 5 mM
87% residual activity at 5 mM
87% residual activity at 5 mM
87% residual activity at 5 mM
87% residual activity at 5 mM
87% residual activity at 5 mM
87% residual activity at 5 mM
87% residual activity at 5 mM
87% residual activity at 5 mM
69.9% residual activity at 10 mM
-
20% residual activity at 10 mM
-
about 10% residual activity at 5 mM
-
5 mM, 51% residual activity
-
67.5% residual activity at 10 mM
-
4%, 1h, activity is decreased to 53%
1 mM, 9% loss of activity of native enzyme, 10% loss of activity of recombinant enzyme, beta-glucosidase activity
2 mM, 80% residual activity
3 mM, 48% residual activity
79-22% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 10-20 mM
the mycelial extract shows 87.1% residual activity at 1% (v/v)
98.66% activity at 10 mM
-
isoform Ag-I shows 88% residual activity and isoform Ag-II shows 74% residual activity at 5 mM 2-mercaptoethanol
-
10 mM, 22% inhibition, strain 461
-
41.5% residual activity at 10 mM
-
100 mM of beta-mercaptoethanol shows an inhibitory effect on activity (91% residual activity)
-
2 mM, 50.3% loss of activity
-
87.8% residual activity at 10 mM
-
1 mM, complete loss of activity
-
40% residual activity; no residual activity
-
1 mM, 95% loss of activity
-
10 mM, 42% residual activity
-
1 mM concentration, activity loss 49%
-
33.7% residual activity at 10 mM
-
41% residual activity at 10 mM
-
10 mM, 51% residual activity
-
5 mM, 82.3% residual activity, 50%, 48 h, crude enzyme preparation
-
70% of initial activity
-
1 mM, slight inhibition
-
5 mM, 51% residual activity
-
with 2 mM hydrolysis of p-nitrophenyl-beta-2-acetamido-2-deoxy-D-glucopyranoside is reduced to 22%, hydrolysis of p-nitrophenyl-beta-2-acetamido-2-deoxy-D-galactopyranoside to 20%
-
1 mM, 93% residual activity
-
75% loss of activity by 1%
-
89.7% residual activity at 4 mM
-
0.5%, 42% residual activity
-
inhibits activity at a concentration of 5%
-
inhibits the enzyme activity at 4 mM by 82.7%
-
1 mM, 54% residual activity
-
1 mM, 88% residual activity
-
22% inhibition at 10 mM
-
IFO 3134, slight inhibition
-
50% inhibition at 0.6 mM
-
complete inhibition at 10 mM
complete inhibition at 10 mM
21.6% inhibition at 10 mM; 78.4% residual activity in the presence of 10 mM
-
58% inhibition at 0.01 mM, 96% at 0.1 mM
-
1 mM ZnCl2 and 5 mM beta-mercapthoethanol, respectively, relative activity: 61%
-
20% inhibition at 10 mM
-
58% inhibition at 0.01 mM, 96% at 0.1 mM
-
50% inhibition at 0.043 mM
-
1 mM, 55% residual activity
-
0.6 mM, complete inactivation
-
1 mM, 13% inhibition, isoenzyme MpiCP-2
-
inhibition of prekallikrein activation
-
65% residual activity at 15 mM
-
0.1 mM, isoenzyme aT-I loses 90% of its activity, isoenzyme aT-II loses 93% of its activity
-
incubation with 3 mM for 30 min at 25°C, in 0.1 ml 0.1 M Tris buffer, pH 7.8, causes 84% loss of activity
-
49% and 62% inhibition at 1 mm and 5 mM
-
5 mM, 61% loss of activity in absence of CaCl2
-
20% inhibited by 0.01 mM, 40% inhibited by 5 mM
-
10.55% inhibition at 10 mM
-
97.7% residual activity at 5 mM
-
81% inhibition at 1150 mM
-
weak, caseinolytic activity
-
18.8% inhibition at 5 mM
-
27% inhibition at 50 mM
-
2 mM Zn2+ protects at 2 mM 2-mercaptoethanol, 2 mM Zn2+ partially protects at 10-50 mM 2-mercaptoethanol, 2 mM Ca2+ partially protects at 2-10 mM 2-mercaptoethanol, no protection at 50 mM 2-mercaptoethanol
-
36.2% residual activity at 5 mM
-
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