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Ligand mercaptoethanol
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Basic Ligand Information
1-thioglycol, 2-mercapthoethanol, 2-mercapto-ethanol, 2-mercaptoethanol, 2- mercaptoethanol, 2-sufanylethanol, 2-sulfanyl-ethanol, 3-mercaptoethanol, beta-mercaptoethanol, Mercapotoethanol, thioethanol, Thioglycol
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open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)
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EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol = (Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O
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1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol = (Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O
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Substrate in Enzyme-catalyzed Reactions (52 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol = (Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O
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1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol = (Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O
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1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol = (Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O
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(E)-p-hydroxyphenylacetaldoxime + NADPH + H+ + 2-mercaptoethanol = (Z)-2-hydroxyethyl N,4-dihydroxybenzene-1-carboximidothioate + NADP+ + H2O
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2-mercaptoethanol + protein disulfide = 2-mercaptoethanol disulfide + protein-dithiol
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2-mercaptoethanol + 2-(glutathione-S-yl)-trichloro-p-hydroquinone = glutathionyl 2-mercaptoethanyl disulfide + trichloro-p-hydroquinone
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5-methyltetrahydrofolate + 2-mercaptoethanol = S-methylmercaptoethanol + tetrahydrofolate
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S-adenosyl-L-methionine + 2-mercaptoethanol = S-adenosyl-L-homocysteine + 2-methylmercaptoethanol
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2-mercaptoethanol + S-adenosyl-L-methionine = S-methyl-2-mercaptoethanol + S-adenosyl-L-homocysteine
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S-tubercidinyl-L-methionine + 2-mercaptoethanol = S-tubercidinyl-L-homocysteine + S-methyl-2-mercaptoethanol
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S-3-deazaadenosyl-L-methionine + 2-mercaptoethanol = S-3-deazaadenosyl-L-homocysteine + S-methyl-2-mercaptoethanol
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S-N6-methyladenosyl-L-methionine + 2-mercaptoethanol = S-N6-methyladenosyl-L-homocysteine + S-methyl-2-mercaptoethanol
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S-8-azaadenosyl-L-methionine + 2-mercaptoethanol = S-8-azaadenosyl-L-homocysteine + S-methyl-2-mercaptoethanol
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S-3'-deoxyadenosyl-L-methionine + 2-mercaptoethanol = S-3'-deoxyadenosyl-L-homocysteine + S-methyl-2-mercaptoethanol
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S-aristeromycinyl-L-methionine + 2-mercaptoethanol = S-aristeromycinyl-L-homocysteine + S-methyl-2-mercaptoethanol
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O-acetyl-L-homoserine + 2-mercaptoethanol = S-hydroxyethyl-L-homocysteine + acetate
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(2R,3R)-beta-chloroalanine + 2-mercaptoethanol = 3-(2-hydroxyethyl)-cysteine + HCl
(2R,3R)-beta-chloroalanine + 2-mercaptoethanol = 3-(2-hydroxyethyl)-cysteine + HCl
(2R,3S)-beta-chloroalanine + 2-mercaptoethanol = (2R,3S)-3-(2-hydroxyethyl)-cysteine + HCl
(2R,3S)-beta-chloroalanine + 2-mercaptoethanol = (2R,3S)-3-(2-hydroxyethyl)-cysteine + HCl
3'-phosphoadenylylsulfate + mercaptoethanol = adenosine 3',5'-bisphosphate + thiosulfuric acid S-ethylester
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2-mercaptoethanol + L-serine + pyridoxal phosphate = S-pyruvylmercaptoethanol + pyridoxamine phosphate + H2O
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L-Cysteine + 2-mercaptoethanol = HOOC-CH(NH2)-CH2-S-CH2-CH2OH + H2S
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L-methionine + 2-mercaptoethanol = methanethiol + S-(beta-hydroxyethyl)-L-homocysteine
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Product in Enzyme-catalyzed Reactions (3 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ribonucleoside triphosphate + 2-hydroxyethyl disulfide = 2'-deoxyribonucleoside triphosphate + 2-mercaptoethanol + H2O
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Activator in Enzyme-catalyzed Reactions (611 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
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
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10 mM, 2fold activation of the oxidation of D-glyceraldehyde 3-phosphate
requirement of sulfhydryl protective reagent, maximal activity with 10 mM to 0.1 M dithiothreitol or mercaptoethanol
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loss of about 50% of original acitivity after exhaustive dialysis, renaturation in presence of 2-mercaptoethanol
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loss of about 80% of original acitivity after exhaustive dialysis, renaturation in presence of 2-mercaptoethanol
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presence of 2-mercaptoethanol or dithiothreitol at 10 mM required for maximal activity
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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
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
purified enzyme does not require 2-mecaptoethanol or anaerobic conditiones for maximal activity
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without addition 73% decrease of activity, suggesting a thiol function necessary for activity
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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
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14 mM, activation of isoenzyme F3GT1 to 160%, activation of isoenzyme F3GT2 to 136%
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0.18 mM, 392% activation of purified sialyltransferase-1, 1120% activation of sialytransferase-1 activity in microsomes
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similar effects as pyridine at 10 mM probably due to its action as secondary substrate
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reverses inhibition with p-chloromercuribenzoate and loss of activity during storage
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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)
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20-30 mM, 3fold stimulation with N-acetylneuraminate as substrate, 1.5fold increase in activity with 4-O-methyl-N-acetylneuraminate as substrate
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activates, degree of activation is more marked with preparations previously stored at 0°C or -10°C
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1% (v/v) activates carboxylesterase in a range of 136% and 244% after 0 and 30 min of incubation
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1.8fold enhancement of activity at 90% (v/v); 1.9fold enhancement of activity at 90% (v/v); 1.9fold enhancement of activity at 90% (v/v)
enzyme form H2 is inactive in absence of mercaptoethanol. No effect on enzyme form H1
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activates, enhancement of the enzyme activity by reducing agents might be expressed via the reduction of Fe2+ at the metal center
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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
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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
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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
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slight activation, 600 mM are required for maximal activity, cannot substitute for DTT
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129.9% relative activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 1-2 mM
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1 mM, slight activation (6%), strain L461; 1 mM, slight activation (9%), strain L103
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the lower concentrations (1-10 mM) of 2-mercaptoethanol show a stimulating effect on activity
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enhances the activity about 1.3- and 1.6fold at the concentrations of 1 and 10 mM, respectively
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10 mM enhances the activities of XynAS27, XynAS27cd, and XynAS27cdl by about 1.5, 1.7, and 1.4fold, respectively
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beta-mercaptoethanol even at a low concentration of 10 mM increases the activity of AgaA by 23%
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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
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active-site thiol is very sensitive to oxidation and requires reductants
active-site thiol is very sensitive to oxidation and requires reductants
active-site thiol is very sensitive to oxidation and requires reductants
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
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enzyme that has been exposed to air in solution lacking thiol compounds shows very marked stimulation of activity by low concentrations of 2-mercaptoethanol
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14% increase of activity at 0.1 mM for IsoI and 11% increase of activity at 1 mM for IsoII
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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)
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sulfhydryl compound such as 2-mercaptoethanol, activates the C-His-rMtFBA activity slightly, 15%
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
sulfhydryl compounds required, 50 mM 2-mercaptoethanol in presence of 0.8 mM FeSO4 is optimal
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activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
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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
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component S requires treatment with 2-mercaptoethanol to show maximal activity. Component E does not require this treatment
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without 2 mM dithiothreirol or 2-mercaptoethanol in the reaction mixture, CofF activity is up to 5fold lower
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Inhibitor in Enzyme-catalyzed Reactions (956 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
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%
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competitive. In crystal strucuture, 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
94% inhibition at 1 mM; 94% inhibition at 1 mM; 96% inhibition at 1 mM; 96% inhibition at 1 mM
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the sulfoxidation of thiobenzamide, catalyzed by isoform PXG1, is completely abolished in the presence of 1 mM 2-mercaptoethanol (competitive inhibitor)
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1 x the Km for cysteine = 4.8% inhibition, 10 x the Km for cysteine = 11% inhibition
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YubC: 1 x the Km for cysteine = -0.7% inhibition, 10 x the Km for cysteine = 6.6% inhibition
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1 x the Km for cysteine = 5.9% inhibition, 10 x the Km for cysteine = 13% inhibition
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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
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evaluated for effectiveness as an inhibitor of PPO activity, using catechol as the substrate
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gradual inhibition by increasing concentration of 2-mercaptoethanol, 20% inhibition at 2 mM, 36% at 16 mM
25% inhibition of Mn-reconstituted wild-type enzyme at 10 mM, no inhibition at 1 mM
complete inhibition of isoform LAAOII and about 50% inhibition of isoform LAAOI at 5 mM
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about 60% residual activity after 1 h incubation with 0.5 mM beta-mercaptoethanol at pH 8.5 and 25°C
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rapid, reversible inactivation, deactivation is a non-destructive transfer of an H atom equivalent to quench the glycyl radical
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XT-II activity is completely abolished at a concentration 1% (v/v) beta-mercaptoethanol
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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))
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43% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
inactivation, reversal by the addition of 4 mM CaCl2, no inactivation if CaCl2 is present during the reducing reaction
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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)
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1 mM, 9% loss of activity of native enzyme, 10% loss of activity of recombinant enzyme, beta-glucosidase activity
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79-22% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 10-20 mM
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isoform Ag-I shows 88% residual activity and isoform Ag-II shows 74% residual activity at 5 mM 2-mercaptoethanol
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100 mM of beta-mercaptoethanol shows an inhibitory effect on activity (91% residual activity)
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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%
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0.1 mM, isoenzyme aT-I loses 90% of its activity, isoenzyme aT-II loses 93% of its activity
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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
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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
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10 mM causes 29% inhibition, suggesting that no cysteine residue is crucial for enzyme activity, although they might have a structural role
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mercaptoethanol shows no growth inhibition activity on Pseudomonas aeruginosa ATCC 27583 at all tested concentrations between 7.0 and 55 mM
mercaptoethanol shows no growth inhibition activity on Pseudomonas aeruginosa ATCC 27583 at all tested concentrations between 7.0 and 55 mM
mercaptoethanol shows no growth inhibition activity on Pseudomonas aeruginosa ATCC 27583 at all tested concentrations between 7.0 and 55 mM
mercaptoethanol shows no growth inhibition activity on Pseudomonas aeruginosa ATCC 27583 at all tested concentrations between 7.0 and 55 mM
activity is decreased to 20% of the original by treatment with cysteine plus mercaptoethanol. Most of the loss is regained on incubation with pyridoxal 5'-phosphate
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competitive inhibition; competitive inhibition; competitive inhibition; competitive inhibition
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no inhibition of wild type enzyme, inhibits activity of D56A and D56E mutant enzymes
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