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Ligand dithiothreitol
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Basic Ligand Information
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open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (13 results)
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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 + H2O = 2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol = 2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
287705, 287707, 287719, 287723, 287724, 287713, 671387, 674393, 674431, 674392, 674854, 675907, 287720, 674074
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vitamin K 2,3-epoxide + dithiothreitol = vitamin K + oxidized dithiothreitol
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vitamin K1 2,3-epoxide + dithiothreitol = vitamin K1 + oxidized dithiothreitol
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2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol = 2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
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L-methionine (S)-sulfoxide + 2 dithiothreitol = L-methionine + dithiothreitol disulfide + H2O
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Hsp21 L-methionine S-oxide + dithiothreitol = Hsp21 L-methionine + dithiothreitol S-oxide
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Hsp21 L-methionine S-oxide + dithiothreitol = Hsp21 L-methionine + dithiothreitol S-oxide
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protein-L-methionine (R)-S-oxide + dithiothreitol = protein-L-methionine + dithiothreitol disulfide + H2O
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protein-L-methionine (R)-sulfoxide + dithiothreitol = protein-L-methionine + dithiothreitol disulfide + H2O
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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
-
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
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Substrate in Enzyme-catalyzed Reactions (149 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
cumene hydroperoxide + dithiothreitol = 2-phenylpropan-2-ol + oxidized dithiothreitol
-
H2O2 + dithiothreitol = H2O + oxidized dithiothreitol
-
tert-butyl hydroperoxide + dithiothreitol = tert-butanol + oxidized dithiothreitol
-
cumene hydroperoxide + dithiothreitol = 2-phenylpropan-2-ol + oxidized dithiothreitol
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carboxymethyl cellulose + dithiothreitol + O2 = carboxymethyl cellooligosaccharides + dithiothreitol disulfide + H2O
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cellulose + dithiothreitol + O2 = oligosaccharides + dithiothreitol disulfide + H2O
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glucomannan + dithiothreitol + O2 = cellooligosaccharides + dithiothreitol disulfide + H2O
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xyloglucan + dithiothreitol + O2 = xyloglucan oligosaccharides + dithiothreitol disulfide + H2O
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ribonucleoside triphosphate + dithiothreitol = 2'-deoxyribonucleoside triphosphate + ? + H2O
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2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O = 2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
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2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol = 2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
287705, 287707, 287719, 287723, 287724, 287713, 671387, 674393, 674074, 674431, 675907, 676838, 674392, 674854, 287720
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2,3-epoxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone + 1,4-dithiothreitol = vitamin K + oxidized dithiothreitol + H2O
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2,3-epoxyphylloquinone + 1,4-dithiothreitol = phylloquinone + oxidized dithiothreitol
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allylbenzene 2',3'-oxide + 1,4-dithiothreitol = allylbenzene + oxidized dithiothreitol
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vitamin K + 1,4-dithiothreitol = vitamin K hydroquinone + oxidized dithiothreitol + H2O
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2-hydroxymethyl-vitamin K 2,3-epoxide + dithiothreitol = 2-hydroxymethyl-vitamin K + oxidized dithiothreitol
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2-methyl-3-phytyl-1,4-naphthoquinone + dithiothreitol = vitamin K hydroquinone + oxidized dithiothreitol
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vitamin K 2,3-epoxide + dithiothreitol = vitamin K + oxidized dithiothreitol
696976, 696999, 701399, 701400, 711627, 287705, 287706, 287707, 287710, 287711, 287712, 287715, 287716, 287719, 287723, 701398, 287713, 287714, 287708, 287717
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vitamin K1 2,3-epoxide + dithiothreitol = vitamin K1 + oxidized dithiothreitol
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2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol = 2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
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2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol = 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
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D-proline + dithiothreitol = 5-amino pentanoic acid + ?
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5,5'-dithiobis(2-nitrobenzoic acid) + dithiothreitol = 2-nitro-5-thiobenzoate + oxidized dithiothreitol
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2 dithiothreitol + O2 = dithiothreitol disulfide + H2O2
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dithiothreitol + O2 = ? + H2O
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dithiothreitol + O2 = dithiothreitol disulfide + H2O2
657645, 657948, 659861, 670697, 670858, 669890, 742867, 670095, 668207, 659912, 668116, 743883, 742490, 659339, 660455, 657990, 658104, 692335
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dithiothreitol + reduced cytochrome c = dithiothreitol disulfide + oxidized cytochrome c
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LCSPSRGSLFTGR + O2 + dithiothreitol = leucyl-formylglycyl-SPSRGSLFTGR + sulfide + oxidized dithiothreitol + H2O
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L-methionine (S)-sulfoxide + 2 dithiothreitol = L-methionine + dithiothreitol disulfide + H2O
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ac-L-Lys-L-Asn-L-Met(O)-L-Asp-L-Lys-dinitrophenol + dithiothreitol = ac-L-Lys-L-Asn-L-Met-L-Asp-L-Lys-dinitrophenol + dithiothreitol disulfide + H2O
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ac-L-Lys-L-Asp-L-Met(O)-L-Asn-L-Lys-dinitrophenol + dithiothreitol = ac-L-Lys-L-Asp-L-Met-L-Asn-L-Lys-dinitrophenol + dithiothreitol disulfide + H2O
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ac-L-Lys-L-Asp-L-Met(O)-L-Asp-L-Lys-dinitrophenol + dithiothreitol = ac-L-Lys-L-Asp-L-Met-L-Asp-L-Lys-dinitrophenol + dithiothreitol disulfide + H2O
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ac-L-Lys-L-Phe-L-Met(O)-L-Lys-L-Lys-dinitrophenol + dithiothreitol = ac-L-Lys-L-Phe-L-Met-L-Lys-L-Lys-dinitrophenol + dithiothreitol disulfide + H2O
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dabsyl-L-methionine (S)-S-oxide + dithiothreitol = dabsyl-L-methionine + dithiothreitol disulfide + H2O
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dabsyl-L-methionine (S)-sulfoxide + dithiothreitol = dabsyl-L-methionine + dithiothreitol disulfide
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dabsyl-L-methionine (S)-sulfoxide + dithiothreitol = dabsyl-L-methionine + dithiothreitol disulfide + H2O
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dabsyl-L-methionine-(S)-S-oxide + dithiothreitol = dabsyl-L-methionine + dithiothreitol disulfide + H2O
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dabsyl-L-methionine-(S)-S-oxide + dithiothreitol = dabsyl-L-methionine + DTT disulfide + H2O
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dabsyl-L-methionine-(S)-S-sulfoxide + dithiothreitol = dabsyl-L-methionine + dithiothreitol disulfide + H2O
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Fmoc-L-methionine (S)-sulfoxide + dithiothreitol = Fmoc-L-methionine + dithiothreitol disulfide + H2O
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Hsp21 L-methionine S-oxide + dithiothreitol = Hsp21 L-methionine + dithiothreitol S-oxide
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racemic (ethanesulfinyl)benzene + dithiothreitol = (ethylsulfanyl)benzene + [(R)-ethanesulfinyl]benzene + dithiothreitol disulfide + H2O
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racemic (methanesulfinyl)benzene + dithiothreitol = (methylsulfanyl)benzene + [(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
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racemic 1-(methanesulfinyl)-4-methylbenzene + dithiothreitol = 1-methyl-4-(methylsulfanyl)benzene + 1-[(R)-methanesulfinyl]-4-methylbenzene + dithiothreitol disulfide + H2O
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racemic 1-bromo-4-(methanesulfinyl)benzene + dithiothreitol = 1-bromo-4-(methylsulfanyl)benzene + 1-bromo-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
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racemic 1-fluoro-2-(methanesulfinyl)benzene + dithiothreitol = 1-fluoro-2-(methylsulfanyl)benzene + 1-fluoro-2-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
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racemic 1-fluoro-3-(methanesulfinyl)benzene + dithiothreitol = 1-fluoro-3-(methylsulfanyl)benzene + 1-fluoro-3-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
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racemic 1-fluoro-4-(methanesulfinyl)benzene + dithiothreitol = 1-fluoro-4-(methylsulfanyl)benzene + 1-fluoro-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
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racemic 1-methyl-4-(methanesulfinyl)benzene + dithiothreitol = 1-methyl-4-(methylsulfanyl)benzene + 1-methyl-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
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racemic 2-(methanesulfinyl)aniline + dithiothreitol = 2-(methylsulfanyl)aniline + 2-[(R)-methanesulfinyl]aniline + dithiothreitol disulfide + H2O
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racemic 2-(methanesulfinyl)naphthalene + dithiothreitol = 2-(methylsulfanyl)naphthalene + 2-[(R)-methanesulfinyl]naphthalene + dithiothreitol disulfide + H2O
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racemic 2-(methanesulfinyl)phenol + dithiothreitol = 2-(methylsulfanyl)phenol + 2-[(R)-methanesulfinyl]phenol + dithiothreitol disulfide + H2O
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racemic 3-(methanesulfinyl)aniline + dithiothreitol = 3-(methylsulfanyl)aniline + 3-[(R)-methanesulfinyl]aniline + dithiothreitol disulfide + H2O
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racemic 4-(methanesulfinyl)benzaldehyde + dithiothreitol = 4-(methylsulfanyl)benzaldehyde + 4-[(R)-methanesulfinyl]benzaldehyde + dithiothreitol disulfide + H2O
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racemic N-[2-(methanesulfinyl)phenyl]acetamide + dithiothreitol = N-[2-(methylsulfanyl)phenyl]acetamide + N-(2-[(R)-methanesulfinyl]phenyl)acetamide+ dithiothreitol disulfide + H2O
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dabsyl-L-methionine-(S)-S-oxide + DTT = dabsyl-L-methionine + DTT disulfide + H2O
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N-acetyl-L-methionine-(S)-S-oxide + DTT = N-acetyl-L-methionine + DTT disulfide + H2O
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peptide-L-methionine-(S)-S-oxide + DTT = peptide-L-methionine + DTT disulfide + H2O
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Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + DTT = Tyr-Gly-Gly-Phe-L-methionine + DTT disulfide + H2O
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dabsyl-L-methionine (R)-S-oxide + dithiothreitol = dabsyl-L-methionine + dithiothreitol disulfide + H2O
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dabsyl-L-methionine (R)-sulfoxide + dithiothreitol = dabsyl-L-methionine + dithiothreitol disulfide + H2O
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dabsyl-L-methionine-(R)-S-oxide + dithiothreitol = dabsyl-L-methionine + dithiothreitol disulfide + H2O
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dabsyl-L-methionine-(R)-S-oxide + dithiothreitol = dabsyl-L-methionine + DTT disulfide + H2O
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Hsp21 L-methionine S-oxide + dithiothreitol = Hsp21 L-methionine + dithiothreitol S-oxide
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L-methionine (R)-sulfoxide + dithiothreitol = L-methionine + dithiothreitol disulfide
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L-methionine (R)-sulfoxide + dithiothreitol = L-methionine + dithiothreitol disulfide + H2O
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L-methionine-(R)-S-oxide + dithiothreitol = L-methionine + dithiothreitol disulfide + H2O
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N-acetyl-L-methionine (R)-sulfoxide + dithiothreitol = N-acetyl-L-methionine + dithiothreitol disulfide + H2O
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protein-L-methionine (R)-S-oxide + dithiothreitol = protein-L-methionine + dithiothreitol disulfide + H2O
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protein-L-methionine (R)-sulfoxide + dithiothreitol = protein-L-methionine + dithiothreitol disulfide + H2O
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racemic (ethanesulfinyl)benzene + dithiothreitol = (ethylsulfanyl)benzene + [(S)-ethanesulfinyl]benzene + dithiothreitol disulfide + H2O
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racemic (methanesulfinyl)benzene + dithiothreitol = (methylsulfanyl)benzene + [(S)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
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racemic 1-(methanesulfinyl)-4-methylbenzene + dithiothreitol = 1-methyl-4-(methylsulfanyl)benzene + 1-[(S)-methanesulfinyl]-4-methylbenzene + dithiothreitol disulfide + H2O
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dithiothreitol + reduced bovine ribonuclease A = ? + oxidized bovine ribonuclease A
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glutathionylated isocitrate lyase + dithiothreitol = glutathione dithiothreitol disulfide + isocitrate lyase
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5'-adenylylsulfate + dithiothreitol = adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
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dabsyl-L-methionine (R)-S-sulfoxide + dithiothreitol = dabsyl-L-methionine + dithiothreitol disulfide + H2O
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L-methionine (R)-S-sulfoxide + dithiothreitol = L-methionine + dithiothreitol disulfide + H2O
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L-methionine (R)-sulfoxide + dithiothreitol = L-methionine + dithiothreitol disulfide
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dithiothreitol + 2-(glutathione-S-yl)-trichloro-p-hydroquinone = glutathionyl dithiothreityl disulfide + trichloro-p-hydroquinone
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peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
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5'-adenylylsulfate + dithiothreitol = adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
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S-adenosyl-L-methionine + cobalt(II)-factor-III + dithiothreitol = S-adenosyl-L-homocysteine + cobalt(II)-precorrin-4 + oxidized dithiothreitol
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L-cysteine + dithiothreitol = S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
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Product in Enzyme-catalyzed Reactions (8 results)
EC NUMBER
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
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2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
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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
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Enzyme Cofactor/Cosubstrate (30 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
can be substituted by dithioerythritol, isozyme type II, 5-20 mM, isozyme type I, 2-5 mM
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667679, 394092, 394104, 667034, 668581, 669752, 394100, 394110, 701130, 394111, 660249, 670619, 700465, 670153
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MsrA can also utilize DTT as reductant, the membrane-isozyme shows only poor activity, while MsrA1 is not active with DTT
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MsrB can also utilize DTT as reductant, the membrane-isozyme shows only poor activity
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Activator in Enzyme-catalyzed Reactions (906 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activates the enzyme in healthy heart slightly, but slightly inhibits the ischemic heart enzyme
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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
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decreases disulfide content of the enzyme, kinetics of enzyme mutants in presence or absence of DTT, overview
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enhancement of enzyme activity of 26% and 33% in the concentration of 10 mM and 50 mM
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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
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greatly enhances the oxidation of verartryl alcohol, lignin-model compounds and lignin
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dithiothreitol is capable of reducing the oxidised form of the Prx1 to regenerate its activity
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in the H2O2 reduction assay, AbTPx1 shows the ability to remove H2O2 without the presence of dithiothreitol. However, removal of H2O2 is promoted with the presence of dithiothreitol
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in the H2O2 reduction assay, AbTPx2 shows the ability to remove H2O2 without the presence of dithiothreitol. However, removal of H2O2 is promoted with the presence of dithiothreitol
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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
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activation
439148, 439179, 439181, 439183, 439184, 439185, 439186, 439188, 439189, 439192, 439193, 439194, 439196, 439197, 439204, 439205, 439206, 439207, 439210, 439212, 439214, 439237, 439217, 439223, 439187, 439219, 439220, 439203, 439248
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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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in the absence of dithiothreitol the activity of recently purified PheH is 50% of that achieved when dithiothreitol is present
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or other sulfhydryl reagents like 2-mercaptoethanol and L-cysteine are essential for activation, 5fold increase in activity
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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
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enhance oxidation of dibromoacetonitrile by the hypoxanthine/xanthine oxidase/Fe system
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the rate of induction of NADH-dependent activity by dithiothreitol increases hyperbolically with respect to NADPH concentration, implying that NADPH has more than a stabilising role in the activating process
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the role of the reduction of the enzyme in vivo is to increase its sensitivity towards the activator 1,3-bisphosphoglycerate
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necessary both to maintain the activity of BADH and to prevent oligimerization of the enzyme
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the enzyme is stimulated (up to 40%) by the addition of dithiothreitol (0.1-0.2 mM)
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4-8 mM, full reactivation after inactivation due to overnight dialysis against 50 mM phosphate pH 7
-
requirement of sulfhydryl protective reagent, maximal activity with 10 mM to 0.1 M dithiothreitol or mercaptoethanol
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stimulation of the reduction of the intermediate benzoyladenosine 5'-monophosphate to benzaldehyde
-
enzyme activity increases significantly, and the enzyme becomes resistant to oxidative stress in presence of NADP+ and DTT
-
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
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increasing DTT concentration results in increasing PcpC activity, reaching a maximum at approximately 30 mM DTT and remaining high up to 100 mM DTT
-
high concentrations of cofactor increases type I activity
-
type II-like enzyme from liver microsomes: 15 mM required. Type II-like enzyme from gut and kidney microsomes: 20 mM required
-
no influence on microsomal enzyme, but slightly stimulating the solubilized enzyme
-
presence of 2-mercaptoethanol or dithiothreitol at 10 mM required for maximal activity
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without addition 7% of the maximum activity detected in the purified enzyme, 14fold activiation is observed at 20 mM
-
P and H protein alone jointly catalyze the glycine-CO2 exchange reaction in presence of pyridoxal phosphate and dithiothreitol
-
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
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at DTT concentrations of 5-10 mM Corynebacterium matruchotii doubling time increases more than 2.5-3fold, the enzyme mediates posttranslocational protein folding in Corynebacterium matruchotii
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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)
-
the higher oligomeric states of BsTrmK are formed via disulphide bonds involving the two cysteines in BsTrmK sequence at positions 35 and 152. Such bonds can be broken by addition of a reducing-agent, and addition of DTT to the MTase reaction buffer results in a dramatic increase of the enzymatic activity
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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+
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low specific activity samples can be activated by a 30 min room temperature incubation in 50 mM DTT
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required for maximum activity, without DTT the enzyme shows 40% of maximal activity
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6-8fold activation of lung transglutaminase B, no activation of transglutaminase C
-
addition of dithiothreitol results in an increase in the branching enzyme activity up to 2.4fold at concentrations greater than 1 mM. This activation is not observed if idoacetamide is simultaneously present.
-
dilution of purified enzyme with a glycine buffer, pH 8.5, containing 1.0 mM DTT, and 0.04% w/v polyvinyl alcohol 50000, produces a striking and significant increase in enzyme activity when diluted 1:2 to 1:10
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activity of RT6.1 increases fivefold, no effect on activity of RT6.2. Cys201 confers thiol sensitivity
-
similar effects as pyridine at 10 mM probably due to its action as secondary substrate
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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
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the activity of the dimer species increases nearly 40fold in the presence of 2 mM the reductant, while the monomer species is active but insensitive to DTT
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in light-adapted extracts, the presence or absence of reduced dithiothreitol has no significant effect on enzyme activity. However, the dark-adapted extracts incubated with reduced dithiothreitol exhibit a highly significant increase in enzyme activity
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the enzyme activity is about 3fold stimulated in the presence of 2 mM dithiothreitol
-
10 mM dithiothreitol activates the enzyme activity about 4fold (but relatively slow)
-
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
-
in absence of 3-phosphoglycerate, increase of acitivity for enzyme from tuber, no effect on enzyme from leaf
-
maximal incorporation of dTTP into poly(rA) template primed with oligo(dT)12 with 10 mM dithiothreitol
-
sulfhydryl reagents required for optimal activity: dithiothreitol or 2-mercaptoethanol
-
to observe full activity of the enzyme, it is necessary to treat the virions with a non-ionic detergent. If the treatment is at 40°C the presence of dithiothreitol is necessary to recover activity
-
slight enhancement of activity towards 1-alkyl-2-acetyl-sn-glycerol, inhibition of activity towards diacylglycerol
-
specific activity slightly increases at dithiothreitol (DTT) concentrations above 1 mM, optimum stimulation at 15 mM DTT, microsomal fraction of human mesangial cells
-
activates from 0.4 mM to 2 mM at a 3-mercaptopyruvate concentration of 0.625 mM, inhibition at 3 mM and 4 mM dithiothreitol
-
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
-
activates, degree of activation is more marked with preparations previously stored at 0°C or -10°C
-
5 mM dithiothreitol increases the activity at 171% after the incubation of the enzyme for 30 min
-
in combination with Mg2+ dithiothreitol can activate chlorophyllase-catalyzed chlorophyll hydrolysis
-
enhances activity at low concentrations of 0.2% (v/v) (108.1% residual activity) to 0.6% (v/v) (111.8% residual activity)
-
highly stimulating on the activity with both choloyl-CoA and chenodeoxycholoyl-CoA
-
activates, enhancement of the enzyme activity by reducing agents might be expressed via the reduction of Fe2+ at the metal center
-
the addition of at least 1 mM dithiothreitol is necessary to retain enzymatic activity during the assay
-
activation is strongly impaired by incubating oxidized enzyme in the presence of Fe2+ before addition of dithiothreitol
-
5 mM, pH 4.0, 55°C, 166% 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
-
stimulates the amylolytic activity of the Amy1 protein at concentrations as low as 0.2 mM when coincubated with thioredoxin A, but is unable to activate the Amy1 protein at concentrations lower than 5 mM, the Amy1 protein activity greatly increases in the presence of dithiothreitol with a maximum (3fold)-enhanced activity at 30 mM
-
45% stimulation at 0.1 mM, hydrolysis of cholesteryl beta-D-glucoside. No effect on hydrolysis of p-nitrophenyl beta-D-glucoside
-
dependent on reducing agents, 50 mM or more required for maximal activity, due to existence of essential sulfhydryl groups in the enzyme
-
the lower concentrations (1-10 mM) of dithiothreitol show a stimulating effect on activity
-
improves enzymatic activity by 65.9-146.2% when added at final concentrations of 10 and 1.0 mM, respectively
-
upon preincubation with both dithiothreitol and thioredoxin, the initial reaction velocity increases by a factor of two
-
dithiothreitol even at a low concentration of 10 mM increases the activity of AgaA by 21%
-
at 2 mM, isoforms agarase-a and agarase-b show 117.47% and 113.44% activity, respectively
-
requires reducing agents, only 67% of maximal activity is observable in absence, optimal concentration 2 mM
-
enhances, activation is maximal with 5-10 mM dithiothreitol and 5-10 mM MgCl2
-
required, hydrolase activity of UCH-L1 in vitro is decreased when reducing dithiothreitol is omitted from the reaction buffer
-
rapid increase in activity from 2 to 6 mM, above this concentration plateau effect
-
strongly stimulates activity of wild-type enzyme and mutant enzyme C188S and shifts the pH-optimum to higher temperatures by about 10°C
-
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
-
enzymatic activity is markedly enhanced by dithiothreitol at submillimolar level, which affects the P1 preference of OpdB synergistically in a substrate-dependent manner
-
activates
36625, 36632, 36647, 36636, 36642, 36638, 36654, 34989, 36651, 36652, 36659, 36633, 36629, 36623, 36656, 36658, 36653
-
the presence of dithiothreitol at concentrations of more than 10 mM significantly increases activity at pH 4.0
-
172% activity in the presence of 2 mM dithiothreitol and 1 mM EDTA, dithiothreitol alone does not inhibit activity
-
proteolytic activity requires presence of dithiothreitol. Autoproteolytic maturation of 68000 Da precursor to 61000 Da mature enzyme in presence of dithiothreitol
-
higher reducing potential in the buffer activates partial cleavage of poly(A) binding protein by 2Apro, no effect on 2Apro-mediated cleavage of eIF4G
-
2-5 mM activate refolded protein in a Tris, phosphate or citrate buffer containing EDTA, pH 7.0-7.5
-
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
-
the action of FheCL1 is enhanced by glutathione, the major reducing agent found in red blood cells. In the presence of DTT, GSH and L-cysteine FheCL1 exhibited similar activation curves with maximal enzyme activity observed in the presence of each reducing agent at a concentration of 0.1 to 1.0 mM
-
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
-
enzyme that has been exposed to air in solution lacking thiol compounds shows very marked stimulation of activity by low concentrations of dithiothreitol
-
near-complete conversion of the enzyme SC to a disulfide-linked DC in the presence of DTT
-
activation to 150% original activity results from addition of dithiothreitol at millimolar concentration
-
10 mM, absence causes inactivation of L-929 PNGase, suggesting S-H group essential for enzyme activity
-
20% increase of activity at 1 mM for IsoI and% increase of activity at 0.1 mM for IsoII
-
the enzyme requires reducing conditions for optimal activity. The omission of dithiothreitol from the enzymatic reactions reduces its activity by 70%
-
0.2-1 mM, slightly enhances decarboxylation of ferulic acid without affecteing decarboxylation of 4-coumarate
-
sulfhydryl compound such as dithiothreitol, activates the C-His-rMtFBA activity slightly, 25%
-
the aerobically purified enzyme is anaerobically activated in the presence of 2 mM dithiothreitol
-
increase in enzyme activity between 2.1 and 2.5fold in the presence of dithiothreitol at 1-3 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
-
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
-
enzyme activity shows marked stimulation in the presence of the thiol-reducing agent, DTT
-
the velocity of the D-Phe formation from the L-isomer is markedly affected by the concentration of DTT, whereas that of L-Phe formation from the D-isomer is less affected
-
increase in activity with increasing glutathione concentration from 0.1 mM up to 5 mM
-
the aerobically purified enzyme is anaerobically activated in the presence of 2 mM dithiothreitol
-
without 2 mM dithiothreirol or 2-mercaptoethanol in the reaction mixture, CofF activity is up to 5fold lower
-
the enzyme is markedly stimulated by dithiothreitol, which increases the activity by about 5fold
-
light enzyme is activated 2fold, dark enzyme is activated 6fold, carboxyltransferase but not biotin carboxylase reaction found to be redox regulated
-
170% increase of Cd2+ transport across plasma membranes at 5 mM. Cd transport across tonoplasts is stimulated up to 125% by 5 mM dithiothreitol
-
effect on mutant N95CC, a large stimulation of ATPase activity is only observed when both proOmpA and DTT are present
-
Inhibitor in Enzyme-catalyzed Reactions (743 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 24%
-
activates the enzyme in healthy heart slightly, but slightly inhibits the ischemic heart enzyme
-
1 mM, 2 h, 20% loss of activity in the first 15 min and then the enzyme activity remains steady throughout the incubation
-
activates laccase at lower concentration (0.1 mM) while inhibits the enzyme at concentrations beyond 0.1 mM in a concentration-dependent manner with complete inhibition of activity at 10 mM
-
complete inhibition at over 10 mM with substrate 3,6-dimethoxyphenol and at over 20 mM with substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
-
enzyme form C: 100% inhibition at 0.1 mM for 5 min, 57% of the inhibition can be recovered by filtration on Sephadex G-25 and a further 14% is recovered after the addition of homocystine at 2 mM
-
98% inhibition at 1 mM; 98% inhibition at 1 mM; complete inhibition at 1 mM; complete inhibition at 1 mM
-
1 mM, complete inhibition of secretion for the first 3 h, secretion returned to normal level after 24 h
-
dithiothreitol acts as H2O2 generator and inhibits the oxygenase component of the enzyme, catalase protects the loss of activity
-
shows high-affinity binding, structure, overview. The noncoordinating thiol group of DTT is critical for its high affinity to the mammalian HO
-
2 mM, 94% inhibition, dithiothreitol induces the dissociation of iron from the enzyme, catalase and phenylalanine partially protect from inhibition
-
dithiothreitol-induced reduction of LH followed by Cd2+ treatment results in significant loss of activity in a dose-dependent manner
-
0.055 mM, 50% inhibition. The rate of conversion of violaxanthin to antheraxanthin is relatively unchanged whereas the conversion of antheraxanthin to zeaxanthin is 50-80% inhibited
-
inhibition is completely prevented by preincubation with 9,10-phenanthrenequinone but not by NADPH
-
rapid reaction studies show that dithiothreitol generates a transient mixed disulfide intermediate with sfALR signaled by a weak charge-transfer interaction between the thiolate of C145 and the oxidized flavin, reducing the transfer of reducing equivalents and reoxidation of the reduced flavin by molecular oxygen
-
TRM5 displays maximal activity above 1 mM DTT and loses 20% of its activity below that value
-
TrmD has maximal activity below 1 mM DTT and loses 20% of its activity above that value
-
reversible inactivation, deactivation is a non-destructive transfer of an H atom equivalent to quench the glycyl radical
-
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
-
light- and dark-adapted extract prepared and assayed without reducing agent, is not significantly affected by incubation with reduced dithiothreitol, however, subsequent incubation with oxidized dithiothreitol results in a significant reduction of enzyme activity under both light and dark conditions
-
0.1 mM, 81% inhibition, irreversible for isoenzyme 1 and reversible for isoenzyme 2
-
inhibition is prevented by pre- or by coincubation with 3-phophoglycerate, but incubation of already inhibited enzyme with 3-phophoglycerate may not reverse the inhibition
-
3-phosphoglycerate protects completely when added before the inhibition, but does not affect the enzyme activity after inhibition by DTT takes place
-
slight enhancement of activity towards 1-alkyl-2-acetyl-sn-glycerol, inhibition of activity towards diacylglycerol
-
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
-
1 mM, 14% loss of activity (recombinant enzyme expressed in Sulfolobus solfataricus). 1 mM, 19% loss of activity (recombinant enzyme expressed in Escherichia coli as thioredoxin-free form (EcSisEstA I)). 1 mM, 23% loss of activity (recombinant enzyme expressed in Escherichia coli as a thioredoxin-EstA fusion protein (EcSisEstA II))
-
for neutral cholesterol esterase with pH optimum at 6.0 and for acid cholesterol esterase
-
isoyzme SCO1725 shows 36% residual activity in the presence of 10 mM dithiothreitol; isozyme SCO7513 shows 86% residual activity in the presence of 10 mM dithiothreitol
-
inhibits the phosphodiesterase activity of the enzyme by reducing both the Cu2+ and disulfide bonds
-
84% inhibition by 25 mM reduced dithiothreitol, 0% inhibition by 25 mM oxidized dithiotreitol
-
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
-
82.5% residual activity and complete inhibition at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
-
1 mM, 4% loss of activity of native enzyme, 5% loss of activity of recombinant enzyme, beta-glucosidase activity
-
100 mM of dithiothreitol shows an inhibitory effect on activity (84% residual activity)
-