Ligand mercaptoethanol

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

Basic Ligand Information

Molecular Structure

C₂H₆OS

mercaptoethanol

DGVVWUTYPXICAM-UHFFFAOYSA-N

Download

Synonyms:

1-thioglycol, 2-mercapthoethanol, 2-mercapto-ethanol, 2-mercaptoethanol, 2- mercaptoethanol, 2-sufanylethanol, 2-sulfanyl-ethanol, 2-sulfanylethan-1-ol, 3-mercaptoethanol, beta-mercaptoethanol, Mercapotoethanol, thioethanol, Thioglycol

close all tables

open all tables

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)

top print hide

1.14.14.40

1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol = (Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O

739318

1.14.14.45

1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol = (Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O

739318

Substrate in Enzyme-catalyzed Reactions (57 results)

top print hide

1.1.1.1

2-mercaptoethanol + NAD+ = ?

695811, 721395

1.1.3.13

2-mercaptoethanol + O2 = 2-mercaptoethanal + H2O2

484911, 484908

1.13.11.19

mercaptoethanol + O2 = 2-hydroxyethanesulfinic acid

396411

1.13.11.20

beta-mercaptoethanol + O2 = 2-hydroxyethanesulfinate

439543

1.14.14.40

1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol = (Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O

739318

1.14.14.43

1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol = (Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O

741195

1.14.14.45

1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol = (Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O

739318, 741195

1.2.1.10

acetaldehyde + 2-mercaptoethanol + NAD+ = S-acetyl-2-mercaptoethanol + NADH + H+

390176

1.2.1.27

propanal + 2-mercaptoethanol + NAD+ = ? + NADH

390219, 390218, 390220

1.21.4.1

D-proline + beta-mercaptoethanol = ?

2-mercaptoethanol + protein disulfide = 2-mercaptoethanol disulfide + protein-dithiol

394815, 394825, 394848, 394851

1.8.5.7

2-mercaptoethanol + 2-(glutathione-S-yl)-trichloro-p-hydroquinone = glutathionyl 2-mercaptoethanyl disulfide + trichloro-p-hydroquinone

740012

2.1.1.13

5-methyltetrahydrofolate + 2-mercaptoethanol = S-methylmercaptoethanol + tetrahydrofolate

441183

2.1.1.67

S-adenosyl-L-methionine + 2-mercaptoethanol = S-adenosyl-L-homocysteine + 2-methylmercaptoethanol

thiamine + 2-mercaptoethanol = ?

636860, 699702, 737686

2.5.1.48

2 entries

2.5.1.49

O-acetyl-L-homoserine + 2-mercaptoethanol = ?

ATP + 2-mercaptoethanol = ADP + ?

641302

2.8.1.1

thiosulfate + 2-mercaptoethanol = ?

3'-phosphoadenylylsulfate + mercaptoethanol = adenosine 3',5'-bisphosphate + thiosulfuric acid S-ethylester

645742

3.1.3.2

p-nitrophenyl phosphate + 2-mercaptoethanol = ?

134701

4.2.1.20

2-mercaptoethanol + L-serine + pyridoxal phosphate = S-pyruvylmercaptoethanol + pyridoxamine phosphate + H2O

L-homoserine + 2-mercaptoethanol = S-hydroxyethyl-L-homocysteine

34489

4IXZ, 3D-view

4.4.1.10

L-Cys + 2-mercaptoethanol = S-(2-hydroxyethyl)cysteine + ?

34514, 5584, 34513

4.4.1.11

4 entries

4.4.1.9

L-cysteine + 2-mercaptoethanol = ?

34716

4.5.1.2

3-chloro-D-alanine + 2-mercaptoethanol = S-(2-hydroxyethyl)-D-cysteine

34748, 34753

4.5.1.5

3-chloro-L-alanine + 2-mercaptoethanol = S-2-hydroxyethyl-L-cysteine + Cl-

648766

5.3.4.1

scrambled RNAse + 2-mercaptoethanol = ?

3083

Product in Enzyme-catalyzed Reactions (5 results)

top print hide

1.17.4.2

ribonucleoside triphosphate + 2-hydroxyethyl disulfide = 2'-deoxyribonucleoside triphosphate + 2-mercaptoethanol + H2O

1.8.1.B1

2 entries

3.1.2.32

S-ethyl-acetothioacetate + H2O = 3-oxobutanoic acid + thioethanol

3.5.1.2

gamma-thioethyl glutamate + H2O = Glu + thioethanol

Activator in Enzyme-catalyzed Reactions (724 results)

top print hide

1.1.1.103

14% activation at 10 mM

activation

protects enzyme from inhibition

reversible

strongly reducing enviroment required

activates

10 mM, 41% increase

1 mM, increases activity by 13%

1 mM, slight activation

slight activation

2 mM, 115% of initial activity

689823

1.13.11.19

stimulation at low concentration, inhibition at high concentration

stimulated by 2 mM

slight activation

reuired. About 1% residual activity in absence of 2-mercaptoethanol

746328

1.14.11.4

can replace ascorbate

439152

1.14.12.24

required for maximal activity, 292.3% activity at 1% (v/v)

maximal activation at 20 mM

0.1 mM, stimulates

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

25 mM, maximal activation, 70% of activity with dithiothreitol

activation

0.1 M required for maximal activity

288059

1.2.1.23

restores the activity after inactivation with p-chloromercuribenzoate

10 mM, activates

246% activity at 2 mM

enhances activity

1 mM, activity is enhanced more than 2fold

activates

maximal activity at 50 mM

activates

3fold activity at 1 mM

slight activation

0.175 mM restores inhibited enzyme after 3 min incubation to 90% of full activity

1%, presence of a reducing agent is essential for enzyme activity

391470

1.4.1.17

required for full activity

2fold activation

presence of 2-mercaptoethanol or dithiothreitol at 10 mM required for maximal activity

391690

1.4.4.2

thiol compound required for maximal activity on glycine-CO2 exchange reaction

slightly activating

required for the in vitro assay

656799

1.6.3.3

2 mM, stimulates up to 2fold

stimulates

enhances activity, can replace NADH

enzyme activity is strongly enhanced in presence of 5 mM 2-mercaptoethanol

increases activity at low substrate concentrations

441385

5DMM, 3D-view

2.1.1.19

reducing agent required for activity

activates

activates

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

684710

1UMY, 3D-view

2.1.1.68

7% activity increase at 20 mM

485541

2.1.1.75

5 mM, required for optimum activity

485584

2.1.1.76

relative activity 105%

stimulates

stimulates

47.8% activity in absence of both EDTA and mercaptoethanol

activation

presence required

activation

slightly activates

1 mM, activation

1 mM is required for optimal activity

activation

stimulates up to 20fold

658191

2.4.1.104

10 mM, activation to 141% of control

stimulation

detergent required for maximal activity

stimulation

without addition 73% decrease of activity, suggesting a thiol function necessary for activity

slight stimulation

relative activity 101%

5 mM, stimulation of 79%

slightly activates

14 mM, activates

14 mM, stimulates

stimulates the enzyme activity

activation

1-30 mM, 4fold-stimulation

stimulation

required for optimal activity

489774

2.4.2.31

required by AT1 transferase, activates AT2 transferase

slight stimulation

activation, together with SDS or guanidine hydrochloride

489800

2.4.2.56

strong stimulation even in the presence of Mg2+

723806

2.4.3.9

0.18 mM, 392% activation of purified sialyltransferase-1, 1120% activation of sialytransferase-1 activity in microsomes

10 mM, not as effective as dithiothreitol

enhances activity

absolutely required

preincubation, activates

639938

2.6.1.40

activation only in the presence of pyridoxal phosphate

activation

20 mM, 70% of activity with dithiothreitol

slight stimulation

20 mM, increases ribulokinase activity up to 175%

above 2 mM

activation

1-2.5 mM, 40-50% activation of Pb2+-precipitated uridine kinase

5 mM, 2-4fold stimulation

enhances activity

stimulates

activation

slight stimulation

activation, at high concentration

enhances the degree of streptomycin inactivation

20 mM, 3fold activation

enhances enzyme activity

requires a thiol for optimal sulfur transfer

activation

activates, degree of activation is more marked with preparations previously stored at 0°C or -10°C

increases activity

about 160% activity at 10 mM

753524

3.1.1.112

1 mM, 143% of initial activity

752576

3.1.1.13

esterification doubled

minimizes loss of activity in presence of sulfhydryl reagent

66.7% activation at 0.5% v/v

at 1%

required

required for 100% activity

stimulation

slight activation

1 mM, stimulates

maximal activation at 50 mM, absolute requirement for SH compounds

stimulates

activates

required

stimulates

stimulation

requirement, or other SH-reducing agents

646471

3.1.6.1

1 mM, enhances activity

activates

13% activation at 1 mM

2.3fold increase of activity by 1 mM

activation

about 120% activity at 1% (v/v)

732767

3.2.1.139

maximal activation at 150 mM

2 mM, 143% of initial activtiy

1 mM, 177% of initial activity

742545

3.2.1.178

110.76% activity at 5 mM

1 mM, activates

slight activation, 600 mM are required for maximal activity, cannot substitute for DTT

134.4% activity at 1 mM

activates 1.2fold at 10 mM

activation

9,6-10% activation at 1-5 mM

1 mM, 1.2fold activation

752101

3.2.1.52

blocks inhibition by Hg2+-ions

393656

3.2.1.54

5 mM, 24% increase in enzyme activity

10 mM, 230.21% of initial activity

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

increases of the hydrolysis activity

increases activity

10 fold activation

activates, 30% activation at 17 mM

81192

3.4.11.14

5 mM, 2fold stimulation

stimulates at 1 mM

activates

SH compound required, efficient activator at 25 mM

slight activation

94% activation at 1 mM, 70% at 5 mM

754276

3.4.21.66

50% activation at 1 % v/v

771971

3.4.21.B65

about 2fold activation

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

activation, 4 mM

not as effective in activation as cysteine

30285

3.4.22.33

highest activity at 96 mM, at 37°C and pH 7.0

682716

3.4.22.34

10 mM, 300% activation

stimulates

activates

required for maximal activity

1 mM, activates

half-maximal activation at 1.4 mM

stimulates

32.16% activation at 2 mg/ml

activates

stimulates

146% activity at 0.5% (v/v)

1 mM, 1.19fold activation

2 mM, 2fold increase in activity

1 mM, activation 6%

slight activation

activates

112.2% activity at 1 mM, substrate N-(3-oxooctanoyl)-L-homoserine lactone

774102

3.5.2.2

10 mM, 108% of initial activity

712887

3.5.2.5

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%

209490

3.5.4.12

enzyme requires dCTP, Zn2+, and 2-mercaptoethanol

activates at 1 mM

slight activation

50-500 mM, 25% stimulation

1-5 mM, activates

activation, less effective than DTT

1 mM, 7% activation

stimulates

enhances activity

activates

maximum stimulation at 75 mM

increases activity

stimulates

648364, 648365, 648366

4.1.1.93

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)

711888

4.1.1.98

slight stimulation of activity at 10 mM

729319

4.1.2.13

sulfhydryl compound such as 2-mercaptoethanol, activates the C-His-rMtFBA activity slightly, 15%

692126

4D2J, 3D-view

4.1.2.33

10 mM: 103% of maximal activity, slight activation

648382

4.1.2.35

stimulation at 3.05 and 6.1 mM

648385

4.1.2.48

about 12% activation at 30 mM

0.005 mM, 2.8fold stimulation

activation

required at very low concentrations of substrate

210707

1OHL, 3D-view

4.2.1.35

sulfhydryl compound is required for maximal activity

2.8 mM, activation

sulfhydryl compounds required, 50 mM 2-mercaptoethanol in presence of 0.8 mM FeSO4 is optimal

5900

4.2.1.8

100% activity in the presence of 2-mercaptoethanol

enhances activity

increases activity up to 3fold. Activation modulates thermotolerance at 50°C

732214

4.2.2.10

10 mM, 124% of initial activity

1 mM, slight stimulation

5 mM, required for full activity

680552

4.3.1.24

activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive

required for activity

activation

increases activity

0.5 mM, enhances activity

34507

4.4.1.31

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

stimulates 2-2.5fold at 0.05 M

stimulates

100% activity at 0.5 mM

746733

5.4.4.2

stimulates, 2.25fold stimulation at 20-30 mM

492271

5.4.99.1

component S requires treatment with 2-mercaptoethanol to show maximal activity. Component E does not require this treatment

3452

5.5.1.13

5 mM, required for full activity

stimulates

stimulates

without 2 mM dithiothreirol or 2-mercaptoethanol in the reaction mixture, CofF activity is up to 5fold lower

Inhibitor in Enzyme-catalyzed Reactions (1098 results)

92% inhibition at 5 mM

760730

1.1.1.118

rapid inactivation at 1 mM

80% inhibition at 1 mM

inhibits above 2 mM

30 mM, 50% inhibition, partially reversed by diamide

286404

1.1.1.263

2.3% inhibition at 1 mM

10% inhibition at 1 mM

711181

1.1.1.278

activates at 1 mM, inhibitory at 10 mM

inhibits both the reductase and dehydrogenase reactions by 30% at 1 mM

724489

1.1.1.359

1 mM, pH 9, 22°C, rapid inactivation

639110

1.1.1.40

inactivation in absence of Mg2+

1 mM, room temperature, pH 9.0, rapid inactivation

competitive to ribitol

slight inhibition

slight inhibition

competitive

10% inhibition at 1 mM, 95% inhibition at 10 mM

25% inhibition at 0.01 mM

55% residual activity at 1 mM; 70% residual activity at 1 mM

2 mM, 23% residual activity

764056

1.11.1.B8

0.1 mM, 97% inhibition

inhibition at high concentration, activation at low concentration

10 mM, 65% inhibition

727448

1.13.11.28

preincubation with substrate protects against inactivation

5 mM, 2% residual activity; 5 mM, complete inhibition

weak

67.3% inhibition at 0.5 mM

24% inhibition at 1 mM

636335

1.14.14.18

0.1 mM, 81% inhibition

2.0 mM

2 mM, 80% inhibition

mild inhibition

strong inhibition at 10 mM

688953

2I5P, 3D-view

1.2.1.19

66% inhibition at 1 mM

non-competitive

10% (v/v), 55% inhibition

722210

1.2.3.1

40% inhibition at 5 mM

0.68 mM, 50% inhibition

660276

1.3.1.86

at high concentrations beta-mercaptoethanol is inhibitory

6.6 mM, 48% inhibition

739868

1.4.1.16

complete inhibition at 5 mM

weakly inhibitory

391965, 391966, 391967

slight

53% after 30 min at 0.5 mM

1 mM, 20.2% residual activity

5 mM, 9% inhibition

1 mM, 16% inhibition, production of methyl iodide

inhibitory in excess

1 mM, total inhibition

slightly inhibitory

at high concentration

above 5 mM

rapid, reversible inactivation, deactivation is a non-destructive transfer of an H atom equivalent to quench the glycyl radical

74% inhibition at 5 mM

membrane-bound enzyme is insensitive, solubilized enzyme is inactivated

above 50 mM

slight inhibition of free and immobilized enzyme

slight inhibition at 50 mM

high concentrations

weak

10% (v/v), 9% inhibition; 91% inhibition

727099

5DX9, 3D-view

2.4.1.173

slight inhibition of the isozyme

737041

2.4.1.18

29.65% residual activity at 1 mM

756764

2.4.1.19

1 mM, 87% of initial activity

719615

2.4.1.209

14 mM, 30% inhibition

288689

2.4.1.22

modification of alpha-lactalbumin

488939

2.4.1.25

D-enzyme, slight inhibition

488998

2.4.1.271

10 mM, 69% inhibition

716627

2.4.1.5

120 mM, 17% inhibition

inactivation

XT-II activity is completely abolished at a concentration 1% (v/v) beta-mercaptoethanol

684886

2.4.2.31

marked decrease in activity, NAD+ and dithiothreitol protects

slight inhibition

5 mM

slightly inhibits NADH kinase

0.4 mM

2 mM, 25% inhibition

high concentrations

96% residual activity at 1 mM

50% residual activity at 1 mM

1 mM, 28-30% inhibition

771959

3.1.1.6

1 mM, 28-30% inhibition

slight inhibition at 10 mM

slight

little effect on activity at 10 mM

required

prior incubation, loss of thermostability

at 37°C, 1 mM reduces activity by 52%

weak inhibition

5 mM, 51% residual activity

23% inhibition at 1 mM

80.4% residual activity at 1 mM

1 mM, 20% inhibition

4%, 1h, activity is decreased to 53%

10 mM

1 mM, 95% loss of activity

750572

3.2.1.35

651601, 666984, 749985

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, 54% residual activity

1 mM, inhibition to 86.70% of control

771499

3.2.1.97

reduced the activities of Tn0153 and Tn2105 to a lesser extent

770087

3.2.1.99

IFO 3134, slight inhibition

50% inhibition at 0.6 mM

21.6% inhibition at 10 mM; 78.4% residual activity in the presence of 10 mM

1%, 56% inhibition

137173, 137174, 137178

0.6 mM, complete inactivation

81225, 81242, 81269

inhibition of prekallikrein activation

651467

3.4.21.35

65% residual activity at 15 mM

696026

3.4.21.4

0.1 mM, isoenzyme aT-I loses 90% of its activity, isoenzyme aT-II loses 93% of its activity

10 mM, strong

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

inhibition at 140 mM

inhibits by 81.62% at 5 mM

50% activity at 2 mM

20% inhibited by 0.01 mM, 40% inhibited by 5 mM

97.7% residual activity at 5 mM

18.8% inhibition at 5 mM

717673

3.4.24.28

27% inhibition at 50 mM

733130

3.4.24.3

37094, 37101, 37105, 37106, 37108

3.4.24.32

66% inhibition

651751

3.4.24.37

19% inhibition at 5 mM

683560

3.4.24.46

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

moderate inhibition

1% w/v, 95% inhibition

even in the presence of 43 mM 2-mercaptoethanol (0.3% v/v), the substrate digestion can still proceed by more than 35%

14% inhibition at 1 mM

the enzyme shows 10% activity in the presence of 0.1% (v/v) 2-mercaptoethanol. Higher concentrations completely inactivate the enzyme. However, the activity of the enzyme is recovered when 2-mercaptoethanol was removed by dialysis

93% residual activity at 10 mM

90% inhibition at 0.1%, v/v

20% inhibition at 2 mM

strong inhibition

slight inhibition at 1 mM

20% inhibition at 100 mM

733540

3.5.1.71

20 mM: 100% inhibition

30% inhibition at 1 mM

393805

4AL3, 3D-view

3.5.1.91

64% inhibition at 1 mM

5 mM

21% inhibition at 1 mM

90.2% residual activity at 5 mM

strong inhibition

weak

96% inhibition at concentration of 20 mM

strong inhibition

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

5199