Ligand mercaptoethanol

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Basic Ligand Information

Molecular Structure
Picture of mercaptoethanol (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C2H6OS
mercaptoethanol
DGVVWUTYPXICAM-UHFFFAOYSA-N
Synonyms:
1-thioglycol, 2-mercapthoethanol, 2-mercapto-ethanol, 2-mercaptoethanol, 2- mercaptoethanol, 2-sufanylethanol, 2-sulfanyl-ethanol, 3-mercaptoethanol, beta-mercaptoethanol, Mercapotoethanol, thioethanol, Thioglycol

Roles as Enzyme Ligand

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

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

Substrate in Enzyme-catalyzed Reactions (52 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2-mercaptoethanol + NAD+ = ?
show the reaction diagram
-
2-mercaptoethanol + O2 = 2-mercaptoethanal + H2O2
show the reaction diagram
-
mercaptoethanol + O2 = 2-hydroxyethanesulfinic acid
show the reaction diagram
-
beta-mercaptoethanol + O2 = 2-hydroxyethanesulfinate
show the reaction diagram
-
1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol = (Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O
show the reaction diagram
-
1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol = (Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O
show the reaction diagram
-
propanal + 2-mercaptoethanol + NAD+ = ? + NADH
show the reaction diagram
-
D-proline + beta-mercaptoethanol = ?
show the reaction diagram
-
2-mercaptoethanol + protein disulfide = 2-mercaptoethanol disulfide + protein-dithiol
show the reaction diagram
-
2-mercaptoethanol + 2-(glutathione-S-yl)-trichloro-p-hydroquinone = glutathionyl 2-mercaptoethanyl disulfide + trichloro-p-hydroquinone
show the reaction diagram
-
5-methyltetrahydrofolate + 2-mercaptoethanol = S-methylmercaptoethanol + tetrahydrofolate
show the reaction diagram
-
S-adenosyl-L-methionine + 2-mercaptoethanol = S-adenosyl-L-homocysteine + 2-methylmercaptoethanol
show the reaction diagram
-
thiamine + 2-mercaptoethanol = ?
show the reaction diagram
-
O-acetyl-L-homoserine + 2-mercaptoethanol = ?
show the reaction diagram
-
ATP + 2-mercaptoethanol = ADP + ?
show the reaction diagram
-
thiosulfate + 2-mercaptoethanol = ?
show the reaction diagram
-
3'-phosphoadenylylsulfate + mercaptoethanol = adenosine 3',5'-bisphosphate + thiosulfuric acid S-ethylester
show the reaction diagram
-
p-nitrophenyl phosphate + 2-mercaptoethanol = ?
show the reaction diagram
-
2-mercaptoethanol + L-serine + pyridoxal phosphate = S-pyruvylmercaptoethanol + pyridoxamine phosphate + H2O
show the reaction diagram
-
L-homoserine + 2-mercaptoethanol = S-hydroxyethyl-L-homocysteine
show the reaction diagram
L-Cys + 2-mercaptoethanol = S-(2-hydroxyethyl)cysteine + ?
show the reaction diagram
-
3-chloro-D-alanine + 2-mercaptoethanol = S-(2-hydroxyethyl)-D-cysteine
show the reaction diagram
-
3-chloro-L-alanine + 2-mercaptoethanol = S-2-hydroxyethyl-L-cysteine + Cl-
show the reaction diagram
-

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
show the reaction diagram
-
-
S-ethyl-acetothioacetate + H2O = 3-oxobutanoic acid + thioethanol
show the reaction diagram
-
-
gamma-thioethyl glutamate + H2O = Glu + thioethanol
show the reaction diagram
-
-

Activator in Enzyme-catalyzed Reactions (611 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
5 mM, 112% of initial activity
-
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
-
stimulation at low concentration, inhibition at high concentration
-
stimulated by 2 mM
-
slight activation
-
reuired. About 1% residual activity in absence of 2-mercaptoethanol
-
can replace ascorbate
-
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
-
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
-
required for full activity
-
2fold activation
-
presence of 2-mercaptoethanol or dithiothreitol at 10 mM required for maximal activity
-
thiol compound required for maximal activity on glycine-CO2 exchange reaction
-
slightly activating
-
required for the in vitro assay
-
2 mM, stimulates up to 2fold
-
stimulates
-
enhances activity, can replace NADH
-
increases activity at low substrate concentrations
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
7% activity increase at 20 mM
-
5 mM, required for optimum activity
-
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
-
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
-
required by AT1 transferase, activates AT2 transferase
-
slight stimulation
-
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, not as effective as dithiothreitol
-
enhances activity
-
absolutely required
-
preincubation, activates
-
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 0C or -10C
-
increases activity
-
about 160% activity at 10 mM
-
1 mM, 143% of initial activity
-
esterification doubled
-
minimizes loss of activity in presence of sulfhydryl reagent
-
at 1%
-
112.2% activity at 1 mM
-
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
-
activates
-
13% activation at 1 mM
-
activation, less effective than DTT
-
2.3fold increase of activity by 1 mM
-
activation
-
activates 28% at 1 mM
-
about 120% activity at 1% (v/v)
-
maximal activation at 150 mM
-
2 mM, 143% of initial activtiy
-
1 mM, 177% of initial activity
-
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
-
blocks inhibition by Hg2+-ions
-
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
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
-
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
-
activates
-
not as effective in activation as cysteine
-
highest activity at 96 mM, at 37C and pH 7.0
-
10 mM, 300% activation
-
stimulates
-
activates
-
required for maximal activity
1 mM, activates
-
half-maximal activation at 1.4 mM
-
stimulates
-
activates
-
stimulates
-
146% activity at 0.5% (v/v)
-
1 mM, 1.19fold activation
-
138.22% activity at 100 mM
-
1 mM, activation 6%
-
slight activation
-
activates
-
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
-
activates at 1 mM
-
slight activation
-
50-500 mM, 25% stimulation
-
1 mM, 7% activation
-
stimulates
-
enhances activity
-
activates
-
maximum stimulation at 75 mM
-
increases activity
stimulates
-
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
-
50 mM, enhances activity 2fold; activates kidney enzyme
-
0.005 mM, 2.8fold stimulation
-
activation
-
required at very low concentrations of substrate
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
-
enhances activity
-
increases activity up to 3fold. Activation modulates thermotolerance at 50C
-
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
-
required for activity
-
activation
increases activity
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
-
stimulates 2-2.5fold at 0.05 M
-
stimulates
-
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
-
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 (956 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
rapid inactivation at 1 mM
-
80% inhibition at 1 mM
-
inhibits above 2 mM
-
30 mM, 50% inhibition, partially reversed by diamide
-
2.3% inhibition at 1 mM
-
6% inhibition at 10 mM
-
10% inhibition at 1 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, 22C, rapid inactivation
-
inactivation in absence of Mg2+
-
1 mM, room temperature, pH 9.0, rapid inactivation
-
competitive to ribitol
-
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
-
0.1 mM, 97% inhibition
-
the sulfoxidation of thiobenzamide, catalyzed by isoform PXG1, is completely abolished in the presence of 1 mM 2-mercaptoethanol (competitive inhibitor)
-
inhibition at high concentration, activation at low concentration
-
10 mM, 65% inhibition
-
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
-
0.1 mM, 81% inhibition
-
2.0 mM
-
2 mM, 80% inhibition
-
mild inhibition
-
strong inhibition at 10 mM
66% inhibition at 1 mM
-
non-competitive
-
10% (v/v), 55% inhibition
-
40% inhibition at 5 mM
-
0.68 mM, 50% inhibition
-
at high concentrations beta-mercaptoethanol is inhibitory
-
1 mM, 50% inhibition
-
6.6 mM, 48% inhibition
-
complete inhibition at 5 mM
-
weakly inhibitory
-
complete inhibition of isoform LAAOII and about 50% inhibition of isoform LAAOI at 5 mM
-
slight
-
53% after 30 min at 0.5 mM
-
about 60% residual activity after 1 h incubation with 0.5 mM beta-mercaptoethanol at pH 8.5 and 25C
-
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 at 50 mM
-
high concentrations
-
weak
-
10% (v/v), 9% inhibition; 91% inhibition
slight inhibition of the isozyme
-
1 mM, 87% of initial activity
-
14 mM, 30% inhibition
-
modification of alpha-lactalbumin
-
D-enzyme, slight inhibition
-
10 mM, 69% inhibition
-
120 mM, 17% inhibition
-
inactivation
-
XT-II activity is completely abolished at a concentration 1% (v/v) beta-mercaptoethanol
-
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
-
slight inhibition at 10 mM
-
slight
-
10 mM, 20% of inhibition
-
little effect on activity at 10 mM
-
required
-
prior incubation, loss of thermostability
at 37C, 1 mM reduces activity by 52%
-
weak inhibition
-
5 mM, 51% residual activity
-
23% inhibition at 1 mM
-
1 mM, 20% inhibition
-
4%, 1h, activity is decreased to 53%
10 mM
-
1 mM, 95% loss of activity
-
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, 54% residual activity
-
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
-
58% inhibition at 0.01 mM, 96% at 0.1 mM
-
1%, 56% inhibition
-
0.6 mM, complete inactivation
-
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
-
10 mM, strong
-
slight inhibition
-
incubation with 3 mM for 30 min at 25C, in 0.1 ml 0.1 M Tris buffer, pH 7.8, causes 84% loss of activity
-
inhibition at 140 mM
-
50% activity at 2 mM
-
20% inhibited by 0.01 mM, 40% inhibited by 5 mM
-
10.55% inhibition at 10 mM
-
97.7% residual activity at 5 mM
-
18.8% inhibition at 5 mM
-
27% inhibition at 50 mM
-
66% inhibition
-
19% inhibition at 5 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
-
1% w/v, 95% inhibition
-
14% inhibition at 1 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
20 mM: 100% inhibition
-
30% inhibition at 1 mM
64% inhibition at 1 mM
-
5 mM
-
21% inhibition at 1 mM
-
90.2% residual activity at 5 mM
-
5 mM, 29% inhibition
-
strong inhibition
-
weak
-
96% inhibition at concentration of 20 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
-
protection by substrate
-
1 mM, 44% loss of activity
-
1 mM, 40% inhibition
-
10 mM, 81% inhibition
-
2 mM, 21% inhibition
-
inactivation above 10 mM
-
inhibition at concentrations above 10 mM, reversed by addition of metal ion
-
weak competitive
-
30% inhibition at 10 mM, 40% at 100 mM
-
complete inhibition at 1 mM
-
-
-