Ligand dithiothreitol

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Basic Ligand Information

Molecular Structure
Picture of dithiothreitol (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C4H10O2S2
dithiothreitol
VHJLVAABSRFDPM-QWWZWVQMSA-N
Synonyms:
(2S,3S)-1,4-disulfanylbutane-2,3-diol, 1,4-dithiothreitol, DTT, reduced DTT

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (13 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol = 2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
show the reaction diagram
-
L-cysteine + dithiothreitol = S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
show the reaction diagram
-
adenosine 5'-phosphosulfate + dithiothreitol = AMP + ?
show the reaction diagram
-

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
show the reaction diagram
-
-

Substrate in Enzyme-catalyzed Reactions (124 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ribonucleoside triphosphate + dithiothreitol = 2'-deoxyribonucleoside triphosphate + ? + H2O
show the reaction diagram
-
insulin + dithiothreitol = ?
show the reaction diagram
-
D-proline + dithiothreitol = 5-amino pentanoic acid + ?
show the reaction diagram
-
dithiothreitol + cumene hydroperoxide = ?
show the reaction diagram
-
protochlorophyllide + dithiothreitol = chlorophyllide + oxidized dithiothreitol
show the reaction diagram
-
insulin disulfide + dithiothreitol = insulin + dithiothreitol disulfide
show the reaction diagram
-
L-methionine (S)-S-oxide + reduced DTT = L-methionine + oxidized DTT + H2O
show the reaction diagram
-
dithiothreitol + 2-(glutathione-S-yl)-trichloro-p-hydroquinone = glutathionyl dithiothreityl disulfide + trichloro-p-hydroquinone
show the reaction diagram
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
show the reaction diagram
-
S-adenosyl-L-methionine + cobalt(II)-factor-III + dithiothreitol = S-adenosyl-L-homocysteine + cobalt(II)-precorrin-4 + oxidized dithiothreitol
show the reaction diagram
-
pyruvate + dithiothreitol = S-acetyl-dithiothreitol + formate
show the reaction diagram
-
L-cysteine + dithiothreitol = S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + sulfide
show the reaction diagram
-
ATP + dithiothreitol + H2O = ?
show the reaction diagram
-
thiosulfate + dithiothreitol = ?
show the reaction diagram
-
3-mercaptopyruvate + dithiothreitol = ?
show the reaction diagram
-
thiosulfate + dithiothreitol = ?
show the reaction diagram
-
L-Cysteine + dithiothreitol = ?
show the reaction diagram
-
L-Cys + dithiothreitol = ?
show the reaction diagram
-
Ile-tRNAIle + DTT = Thioester of Ile and DTT + tRNAIle
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (8 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
dCDP + DTT disulfide + H2O = CDP + DTT
show the reaction diagram
-
-
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
show the reaction diagram
-
-
arsenate + reduced dithiothreitol = arsenite + dithiothreitol
show the reaction diagram
-
-
ubiquitin thiol ester of dithiothreitol + H2O = ubiquitin + dithiothreitol
show the reaction diagram
-
-
menadiol + oxidized dithiothreitol = menadione + dithiothreitol
show the reaction diagram
-
-

Enzyme Cofactor/Cosubstrate (29 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
DTT can replace NADPH, but is much less effective
-

Activator in Enzyme-catalyzed Reactions (862 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 123% of initial activity
-
25% activation at 10 mM
-
and the particulate fraction required for full activity
-
1 mM 24% stimulation
-
5fold activation
-
activation
-
activates 25% at 1 mM
-
activates the enzyme in healthy heart slightly, but slightly inhibits the ischemic heart enzyme
-
2.1fold activation
-
1 mM, 1.75fold increase in activity
-
activates
-
the enzyme is 2.5fold activated by the addition of 0.8 mM dithiothreitol. The activation is caused by cleavage of the disulfide bond formed between two cysteine residues in the C-terminal regions of the two subunits
-
2 mM, maximum activation
-
; decreases disulfide content of the enzyme, kinetics of enzyme mutants in presence or absence of DTT, overview
-
dithiothreitol has major positive influence on refolding
-
123% activity at 1 mM
-
slight activation
-
stimulation of chloroplastic form, 150% of enzyme activity
-
123% activity at 1 mM
-
1.0 mM and 10 mM, 56% increase in activity, enzyme activity in cell extracts
-
enhancement of enzyme activity of 26% and 33% in the concentration of 10 mM and 50 mM
-
activates laccase at lower concentration (0.1 mM) while inhibites the enzyme at concentrations beyond 0.1 mM in a concentration-dependent manner with complete inhibition inactivity at 10 mM
-
greatly enhances the oxidation of verartryl alcohol, lignin-model compounds and lignin
-
9% activation at 1 mM
-
Co QueD: 110% activity remains after 15 min incubation with 1 mM reagent
-
can reduce the inactive ferric form of the enzyme to the active ferrous form
-
0.05 mM, 70°C, 109.3% activity; 0.05 mM, 9.3% increase of activity
-
activates by 27% at 5 mM
-
stimulates
-
in the presence of DTT, continuous luminescence is observed over 1 h. In the absence of DTT, the luminescence activity slowly decreases with a half period of 8.3 min
-
stimulates. Stimulation is negated when added together with DTT
-
required for activity
-
sparing as well as augmenting effect
-
4 mM, slightly increases activity
-
20% increase of activity at 1 mM
-
3fold increase in activity in presence of dithiothreitol
-
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
-
48% activity without dithiotreitol
-
increases the product yield more than 72%
-
small amounts abolish the characteristic lag phase of monohydric phenol oxidation without effect on the maximum rate of reaction or on the total O2 consumption
-
activates
-
enhances activity
-
strong increase of activity
-
slight activation
-
thiol compound required
-
recovery from oxidase to dehydrogenase type
-
enhance oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
-
non-physiological cofactor
-
does require dithiothreitol for optimum activity
-
4-8 mM, full reactivation after inactivation due to overnight dialysis against 50 mM phosphate pH 7
-
slight activation
-
activation
-
stimulation of the reduction of the intermediate benzoyladenosine 5'-monophosphate to benzaldehyde
-
10 mM, activates
-
5 mM causes 58% increase in activity
-
276% activity at 2 mM
-
maximum 12% increase of activity observed with 0.1 mM
-
2fold stimulation at 5 mM
-
enhances activity
-
1 mM, activity is enhanced more than 2fold
-
enzyme activity is increased about 1.5fold by the addition of 2 mM dithiothreitol
-
stimulates
-
stimulates ArsC-dependent arsenate reduction, but not 2-mercaptoethanol or reduced glutathione
-
glutathione and dithiothreitol in combination enhance arsenate reduction in vitro more than glutathione alone
-
accumulation of 13% 4-chlorobenzoyl-CoA in cell extract
-
increasing DTT concentration results in increasing PcpC activity, reaching a maximum at approximately 30 mM DTT and remaining high up to 100 mM DTT
-
activates
-
enhancement in the range of 5-10 mM
-
slight activation
-
required for activity
-
added to the assay at 2 mM
-
0.5 mg per ml, presence of a reducing agent is essential for enzyme activity
-
can replace 2-mercaptoethanol
-
presence of 2-mercaptoethanol or dithiothreitol at 10 mM required for maximal activity
-
without addition 7% of the maximum activity detected in the purified enzyme, 14fold activiation is observed at 20 mM
-
rapidly activates sQH-AmDH, activation process involves a reduction process
-
slight activation at 1 mM
-
slightly activating
-
about 14fold increase of activity at 20 mM. Without addition of dithiothreitol to the assay mixture, only 7% of the maximum activity is detected in the purified enzyme
-
1 mM, slight stimulation to 103%
-
enhances activity, can replace NADH
-
activation
-
presence during purification preserves enzymatic activity
-
DTT can replace glutathione as reductant, 5 mM DTT increases activity 40fold
-
1 mM, stimulates about 2.7fold
-
does not reduce the plastoquinone pool directly, but is dependent on ferredoxin, consistent with the involvement of a ferredoxin-dependent reaction, most likely the ferredoxin:quinone reductase (FQR)
-
1-20 mM, slight activation
-
1 mM + 1 mM PMSF, activation to 147% of control
-
10-20 mM, up to 39% inhibition
-
activates
-
the optimum ratio of dithiothreitol to divalent metal ion is about 10:1. The maximal methyltransferase activity is achieved at 10 mM dithiothreitol and 1 mM Zn2+
-
7% activity increase at 20 mM
-
low specific activity samples can be activated by a 30 min room temperature incubation in 50 mM DTT
-
stimulates
-
1 mM, slightly stimulates
-
essential to maintain enzyme activity
-
activation
-
activation
-
activates
-
activation
-
1 mM, 82% activation
-
required for maximum activity, without DTT the enzyme shows 40% of maximal activity
-
stimulates
-
activation, microsomal preparation
-
activates
-
stimulates
-
10 mM: stimulation, 100 mM: inhibition
-
required for enzyme activity
-
4fold increase at 20 mM
-
maxmimum activity in the presence of 1 mM dithiothreitol
-
slight increase in activity
-
activation
-
requirement, 0.01 M stabilizes the enzyme in a reduced state
-
stimulates up to 20fold
-
10 mM, 3fold stimulation
-
absolute requirement
-
10 mM: increase of activity by about 30%
-
25% stimulation at 1 mM
-
63% activation at 10 mM
-
30% increase of activity at 1 mM
-
increases the activity of wild type OGT
-
1 mM, 125% of initial activity
-
0.1-3 mM, about 5fold stimulation
-
required, best at 2 mM
-
activation, optimal concentration: 1 mM
-
10 mM, stimulation to 120% of the original activity
-
requirement, 5 mM
-
stimulating
-
enhances activity together with urea
-
10 mM, required for maximal stability
-
activates, best at 10 mM
-
activates
-
slight activation
-
2 mM, catalytic activity 124%
-
required for alpha and beta isoenzymes activity, not required for gamma enzyme
-
slightly activates the O-phospho-L-serine sulfhydrylation reaction
-
included in the assay reaction mixture
-
stimulates activity
-
1 mM, activates 1.8fold
-
activation
-
slight stimulation of activity
-
activity is 10fold elevated by addition of 5 mM dithiothreitol to the enzyme assay
-
enzyme is inactive in absence either EDTA or a thiol such as reduced monosodium glutathione or dithiothreitol
-
10 mM dithiothreitol activates the enzyme activity about 4fold (but relatively slow)
-
activation
-
1-2.5 mM, 40-50% activation of Pb2+-precipitated uridine kinase
-
5 mM, 2-4fold stimulation
-
activation
-
requirement
-
required
-
presence of a reducing agent is required
-
once treated with 5,5'-dithiobis-2-nitrobenzoic acid, the enzyme activity can be recovered more than 95% after incubation for 20 min with 0.15 mM dithiothreitol
-
requirement
-
stimulates the catalytic activity of NMNAT-2 up to 30%
-
most effective in activation
-
20 mM
-
required
-
highly stimulating
-
activates
-
similar activation as with 2-mercaptoethanol
-
1 mM
-
activation up to 0.005 mM
-
activates, degree of activation is more marked with preparations previously stored at 0°C or -10°C
-
enhances activity at low concentrations of 0.2% (v/v) (108.1% residual activity) to 0.6% (v/v) (111.8% residual activity)
-
10 mM, activation to 122% of control at pH 5.0, LPL1
-
5 mM, 40% stimulation
-
at 1%
-
required
-
oxidized, activation
-
stimulation
-
highly stimulating on the activity with both choloyl-CoA and chenodeoxycholoyl-CoA
-
maximal activation at 1 mM, absolute requirement for SH compounds
-
the addition of at least 1 mM dithiothreitol is necessary to retain enzymatic activity during the assay
-
stimulates
-
stimulation up to 1.3fold
-
tumor cell line, N-ethylmaleimide-sensitive
-
required
-
stimulation
-
activates
-
28% activation at 1 mM
-
activation
-
45% stimulation at 0.1 mM, hydrolysis of cholesteryl beta-D-glucoside. No effect on hydrolysis of p-nitrophenyl beta-D-glucoside
-
activation
-
dithiothreitol-dependent; dithiothreitol-dependent
-
activates
-
40% activation by 1 mM, 180% activation by 5 mM
-
1 mM, 158% of initial activity
-
strong activation of isozyme TR-BAMY
-
or similar reducing agent, required
-
1 mM, activation to 154% of control
-
activates
-
13% activation at 0.2 mM
-
stimulates N-acetylglucosaminidase even at low concentrations
-
recombinant enzyme
-
124% activity at 1 mM
-
activation to 165.2% at 5 mM
-
increases the hydrolysis activity
-
10 mM, about 1.1fold activation
-
10 fold activation
-
requires reducing agents, only 67% of maximal activity is observable in absence, optimal concentration 2 mM
-
activates, 23% activation at 0.021 mM, inhibition above
-
activates
-
weak activation
-
maintains catalytic activity of PMH
-
only when incubated in the presence of 20 mM dithiothreitol, which reduces the structural disulfide bonds and unfold the protein, and above 34°C, is CtHtrA able to proteolyse alpha-lactalbumin
-
addition of 2 mM dithiothreitol greatly enhances the tryptic activity
-
required for maximal activity
-
increases activity
-
2.5fold activation at 1 mM
-
reduction is essential for catalytic activity
-
activates
-
higher reducing potential in the buffer activates partial cleavage of poly(A) binding protein by 2Apro, no effect on 2Apro-mediated cleavage of eIF4G
-
not as effective in activation as cysteine
-
highest activity at 2.5 mM, at pH 7.0 and 37°C
-
activation
-
activates
-
activates
-
1 mM, activates
-
half-maximal activation at 1.1 mM
-
2 milliM, pH 5.0, 48 h, 37°C, enzymatic activity depends on reducing agents
-
no activity in buffer lacking DTT
-
the cathepsins L needed the presence of dithiothreitol to digest IgG1, IgG2, and IgG4 whereas IgG3 was identically cleaved under both reducing and nonreducing conditions
-
activation
-
stimulates
-
1 mM, stimulates 1.3fold
-
assay with
-
stimulates
-
activates enzymatic activity up to 0.1 mM
-
enhances activity
-
ArfB is not active in the absence of 2 mM dithiothreitol
-
enhances activity
-
slight activation
-
0.1-1 mM: slight activation, 10 mM: high activation
-
activates
-
10 mM, 111% of initial activity
-
20% increase of activity at 1 mM for IsoI and% increase of activity at 0.1 mM for IsoII
-
1 mM, 130% of initial activity
-
the enzyme requires the presence of dithiothreitol for maximum activity
-
activation
-
1 mM, 23% inhibition; activates at 1 mM
-
about 50% stimulation of activity at 1 mM
-
slight activation
-
2 mM, 1.9fold activation
-
activity increases in presence of 1 mM dithiothreitol
-
170% increase of Cd2+ transport across plasma membranes at 5 mM. Cd transport across tonoplasts is stimulated up to 125% by 5 mM dithiothreitol
-
0.2-1 mM, slightly enhances decarboxylation of ferulic acid without affecteing decarboxylation of 4-coumarate
-
1 mM, 7% activation
-
activates
-
enhances activity
-
maximum at 10-40 mM, 30% stimulation
-
increases activity
-
activates
-
1 mM, 116% of initial activity
-
stimulates
-
activates 8fold at 5-7 mM
-
maximum stimulation of activity at more than 5 mM dithiothreitol
-
maximal stimulation of activity at about 10 mM
-
1 mM, 17.9% increase of activity
-
5 mM, required for optimal ativity
-
activates, 900% stimulation at 1 mM
-
2.8 mM, activation
-
1 mM, 7fold stimulation
-
optimal activity in the presence of 5 mM DTT and 5% glycerol
-
stimulates over 100% at 1 mM
-
increase in enzyme activity between 2.1 and 2.5fold in the presence of dithiothreitol at 1-3 mM
-
activates
-
activity is strongly dependent on the presence of dithiothreitol, with activity increasing up to 46% when the reductant is present in the reaction mixture. Concentrations higher than 5 mM cause an inhibitory effect
-
the air-inactivated enzyme is activated by reaction with Fe2+ and dithiothreitol in the absence of air
-
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
-
optimal activation at 40 mM
-
150% activity at 2 mM
-
preincubation for 30 min at 30 C stimulates
-
up to 50% stimulation
-
activates
-
required
-
activates
-
166% activity at 1 mM
-
increase in activity with increasing glutathione concentration from 0.1 mM up to 5 mM
-
phosphoglycerate mutase activity requires the reductant dithiothreitol, cysteine hydrochloride, or glutathione for full activity
-
1 mM, required for maximal activity
-
100% activity at 0.5 mM
-
stimulates, 2fold stimulation at 1 mM
-
the aerobically purified enzyme is anaerobically activated in the presence of 2 mM dithiothreitol
-
stimulates
-
the optimum concentration for enzyme activity is 1 mM
-
activates
-
activates 30fold the aminoacylation raection
-
stimulates
-
0.01 mM, 80% stimulation
-
stimulation
-
activation
-
stimulates
-
maximal stimulation at 2.5 mM
-
essential for activity
-
without 2 mM dithiothreirol or 2-mercaptoethanol in the reaction mixture, CofF activity is up to 5fold lower
-
stimulates; stimulates; the enzyme is markedly stimulated by dithiothreitol, which increases the activity by about 5fold
-
stimulates
-
required for optimal activity, above 50 mM increase activity to 223% mM
-
stimulates
-
light enzyme is activated 2fold, dark enzyme is activated 6fold, carboxyltransferase but not biotin carboxylase reaction found to be redox regulated
-
10 mM, stimulating
-
2 mM, 26% stimulation
-
GSH, dithiothreitol or dithioerythritol are required for activity
-
effect on mutant N95CC, a large stimulation of ATPase activity is only observed when both proOmpA and DTT are present
-
partially stimulates
-

Inhibitor in Enzyme-catalyzed Reactions (691 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
25% inhibition at 10 mM
-
46.0% inhibition at 10 mM of the reverse reaction
-
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 24%
-
50% inhibition at 5 mM
-
0.57 mM, 50% inhibition, reversed by diamide
-
1 mM, 50% inhibition
-
45% inhibition at 1 mM
-
35% inhibition at 5 mM
-
19% inhibition at 1 mM
-
inhibits both the reductase and dehydrogenase reactions by 30% at 1 mM
-
1 mM, 10% inhibition
-
10 mM, 28% inhibition
-
slight
-
10% inhibition at 1 mM, 95% inhibition at 10 mM
-
85% residual activity at 0.5 mM
-
complete inhibition at 2 mM
-
7% inhibition at 0.5 mM
-
40% inhibition at 1 mM
-
26.5% inhibition at 0.01 mM
-
81% residual activity at 1 mM
-
0.0005 mM, 97% inhibition
-
23% inhibition at 1 mM
-
10 mM, 61% inhibition
-
preincubation with substrate protects against inactivation
-
5 mM, 6% residual activity; 5 mM, 94% inhibition
-
10 mM, 90% inhibition
-
slight inhibition
-
strong inhibition
-
strongly inhibitory, inhibition is reversible after desalting
-
dithiothreitol acts as H2O2 generator and inhibits the oxygenase component of the enzyme, catalase protects the loss of activity
-
50% inhibition at 1 mM
-
2.0 mM
-
inactivates the enzyme, synergistically with tetrahydrobiopterin
-
81% inhibition at 1 mM
-
1.0 mM, 55% inhibition
-
mild inhibition
-
inhibition of prostaglandin G1 synthesis
-
54.75% residual activity at 1.0 mM
-
dithiothreitol-induced reduction of LH followed by Cd2+ treatment results in significant loss of activity in a dose-dependent manner
-
slight inhibition
-
higher than 10 mM, activation below
-
high concentration
-
inhibits the enzyme at 5 mM
-
above 10 mM
-
at high concentrations dithiothreitol is inhibitory
-
inhibits activity of N-terminally processed-like enzyme form
-
1 mM, 30.7% residual activity
-
10 mM, 12% inhibition
-
up to 0.010 mM increase the enzyme activity, higher concentrations inhibited it
-
up to 0.010 mM increase the enzyme activity, higher concentrations inhibit
-
80% residual activity at 1 mM
-
2 mM, rapid decrease in activity to less than 10% of the activity
-
rate of inactivation is increased by NAD+, but not by NADP+
-
inhibits cytochrome c formation
-
5 mM, 28% inhibition, production of methyl iodide
-
strong inhibition
-
1 mM, total inhibition
-
palmitoyl-CoA-specific isozyme
-
at high concentration
-
10 mM: stimulation, 100 mM: inhibition
-
reversible inactivation, deactivation is a non-destructive transfer of an H atom equivalent to quench the glycyl radical
-
0.5 mM 47% activity
-
30% inhibition
-
98% inhibition at 5 mM
-
60% inhibition
-
solubilized protein
-
concentration above 5 mM results in a marked inhibition of activity
-
1.5 mM, 42% inhibition, 16.5 mM, 40% inhibition
-
slight inhibition at 5 mM
-
1 mM, 56% inhibition
-
high concentrations
-
4 mM, slight
-
1 mM, 68% of initial activity
-
strong inhibition in the presence of Mg2+ and Mn2+
-
the rate of reduction of the disulfide bond in alpha-lactalbumin is much faster with dithiothreitol than mercaptoethanol, and at 24°C proceeds to completion within minutes at pH 8
-
D-enzyme, slight inhibition
-
10 mM, 61% inhibition
-
100 mM, 41% inhibition
-
XT-II activity is completely abolished at a concentration of 1 mM dithiothreitol
-
0.8 M, reduction of thermostability
-
20% inhibition by 5 mM, 25% inhibition by 10 mM
-
0.1 mM, 89% inhibition of purified sialyltransferase-1
-
10% inhibition of beta-elimination from O-succinyl-L-serine
-
0.1 mM, 81% inhibition, irreversible for isoenzyme 1 and reversible for isoenzyme 2
-
conformational change and inactivation
-
in the presence of 0.01 M DTT enzyme shows 20% activity loss
-
inhibits from 3 mM to 4 mM at a 3-mercaptopyruvate concentration of 15 mM
-
activity is strongly dependent on the presence of dithiothreitol, with activity increasing up to 46% when the reductant is present in the reaction mixture. Concentrations higher than 5 mM cause an inhibitory effect
-
inhibition above 0.005 mM
-
19.4% residual activity at 5 mM
-
1 mM, complete inhibition
-
10 mM, 26% inhibition
-
50% loss of activity at 5 mM, 75% at 10 mM
-
inhibits the phosphodiesterase activity of the enzyme by reducing both the Cu2+ and disulfide bonds
-
1 mM, 20% inhibition
-
1.25 mM, 60% inhibition
-
complete inhibition at 50 mM
-
phosphatase activity is decreased by 5 mM
-
slight
-
84% inhibition by 25 mM reduced dithiothreitol, 0% inhibition by 25 mM oxidized dithiotreitol
-
prior incubation, 12% of activity remains, loss of thermostability
-
5 mM, 45% residual activity
-
weak inhibition
-
slight
-
50 mM, required for maximal activity
-
strong inhibition of formation of allyl isothiocyanate in presence of Fe2+ at pH 6.5 and at pH 5.0, little influence on glucose production from sinigrin
-
90% residual activity at 1 mM
-
2 mM, 10% residual activity
-
loss of activity with first-order kinetics
-
54% residual activity at 0.4 mM
-
1%, 22% inhibition
-
49.2% residual activity at 50 mM
-
10 mM, 77% residual activity
-
1 mM, 22% inhibition
-
83.3% residual activity at 4 mM
-
incubation in 20 mM at 37°C leads to rapid loss of activity but addition of Mg2+ stabilizes the hydrolase against thermal inactivation
-
20 mM, 74% residual activity
-
60% inhibition if enzyme is preincubated with 10 mM
-
50% inhibition at 0.1 mM
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30°C, 10 min, 1 mM, 63% loss of activity
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slight
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0.6 mM, complete inactivation
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52% inhibition at 1 mM
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1 mM, 94.8% inhibition
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2 mM, complete inhibition
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erythrocyte isozyme ISOT-S and ISOT-L, inhibition by chelating of Zn2+
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94% inhibition at 10 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
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partial inhibition at very high concentrations
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inhibition of prekallikrein activation
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complete inhibition at 3 mM
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1 mM, no residual activity
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1 mM, strong
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slight inhibition at 1-10 mM
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at 2 mM completely inhibits coagulant and protease activities of RVBCMP
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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 a complete loss of activity. Alterates the molecular structure probably associated with an altered loading of the protein with dodecyl sulfate anions. Inactivation of the enzyme appears to follow an all-or-none reaction. Residues Cys22-Cys157 and Cys191-Cys220 are dithiothreitol-sensitive
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10% loss of activity, thiobenzyl benzyloxycarbonyl-L-lysinate as substrate
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inhibition at 10 mM
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80% of enzyme activity inhibited in the presence of 2.5 mM DTT
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isoforms nethepsin I, IIa and IIb are completely inactivated in the presence of 40-70 mM dithiothreitol
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100 mM, 50% residual activity
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