1.11.1.28: lipoyl-dependent peroxiredoxin
This is an abbreviated version!
For detailed information about lipoyl-dependent peroxiredoxin, go to the full flat file.
Word Map on EC 1.11.1.28
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1.11.1.28
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peroxiredoxins
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xanthomonas
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campestris
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tert-butyl
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phaseoli
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tbooh
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cys-based
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xylella
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peroxidatic
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cumene
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medicine
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thiol-dependent
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fastidiosa
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glutaredoxins
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osmcs
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peroxide-sensing
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sulfenic
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lipoylated
- 1.11.1.28
- peroxiredoxins
- xanthomonas
- campestris
-
tert-butyl
- phaseoli
-
tbooh
-
cys-based
- xylella
-
peroxidatic
- cumene
- medicine
-
thiol-dependent
- fastidiosa
- glutaredoxins
-
osmcs
-
peroxide-sensing
-
sulfenic
-
lipoylated
Reaction
Synonyms
AhpC, AhpCD, AhpD, ahpD1, ahpD2, alkyl hydroperoxide reductase, alkyl hydroperoxide reductase subunit C, EC 1.11.1.15, MfOhr, Ohr, Organic hydroperoxide resistance, organic hydroperoxide resistance protein, peroxiredoxin AhpC, peroxiredoxin AhpD
ECTree
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Substrates Products
Substrates Products on EC 1.11.1.28 - lipoyl-dependent peroxiredoxin
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REACTION DIAGRAM
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + 7alpha-hydroperoxy-3beta-hydroxycholest-6-ene
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + 7alpha-hydroxy-3beta-hydroxycholest-6-ene
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cholesterol hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cholesterol hydroxide
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + 2 H2O
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + linoleic acid hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + oleic acid hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + oleic acid
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + ROOH
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ROH
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butanol
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + trans-pinocarveylhydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + trans-pinocarveyl alcohol
-
-
-
?
linoleic acid hydroperoxide + dihydrolipoamide
? + lipoamide
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
linoleic acid hydroperoxide + reduced dithiothreitol
? + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
tert-butyl hydroperoxide + dihydrolipoamide
tert-butanol + lipoamide
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complexlipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + 7alpha-hydroperoxy-3beta-hydroxycholest-6-ene
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + 7alpha-hydroxy-3beta-hydroxycholest-6-ene
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + 7alpha-hydroperoxy-3beta-hydroxycholest-6-ene
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + 7alpha-hydroxy-3beta-hydroxycholest-6-ene
-
-
-
?
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cholesterol hydroxide
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cholesterol hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cholesterol hydroxide
-
-
-
?
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
best substrate for AhpD
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
best substrate for AhpD
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
-
-
-
?
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + 2 H2O
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + 2 H2O
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + 2 H2O
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + 2 H2O
-
-
-
?
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ?
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + linoleic acid hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ?
-
-
-
?
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + oleic acid
poor substrate
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + oleic acid hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + oleic acid
poor substrate
-
-
?
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ROH
-
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + ROOH
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ROH
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + ROOH
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ROH
-
-
-
?
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butanol
fatty acid (but not cholesterol) hydroperoxides dock well into the active site of Ohr from Xylella fastidiosa and are efficiently reduced by the recombinant enzyme
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butanol
fatty acid (but not cholesterol) hydroperoxides dock well into the active site of Ohr from Xylella fastidiosa and are efficiently reduced by the recombinant enzyme
-
-
?
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
2-phenylpropan-2-ol + lipoamide
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
cumene hydroperoxide + dihydrolipoamide
2-phenylpropan-2-ol + lipoamide
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
2-phenylpropan-2-ol + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
H2O + lipoamide
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
H2O2 + dihydrolipoamide
H2O + lipoamide
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
H2O + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
tert-butanol + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complexlipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complexlipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O
-
-
-
?
?
-
-
AhpD directly interacts with AhpC as an electron donor, and the conserved Cys residues in active site of AhpD are important for enzyme reduction
-
-
-
additional information
?
-
AhpD contributes to regenerate a variety of thiol-dependent peroxidase in the decomposition of peroxide by linking a dihydrolipoamide dehydrogenase (Lpd)/dihydrolipoamide succinyltransferase (SucB)/NADH system through the cyclization of their own active site dithiol to the oxidized disulphide. The CXXC motif of AhpD is essential to maintain the peroxides reduction activity of thiol-dependent peroxidase. The AhpD system is an important redox system in cells besides the thioredoxin system. Corynebacterium glutamicum AhpD not only has the ability to reduce a variety of thioredoxin-dependent antioxidant enzymes, including mycothiol peroxidase, peroxiredoxin, and Ohr (organic Hydroperoxide Resistance), but also shows a higher affinity for Ohr than those of mycothiol peroxidase and peroxiredoxin, which is different from the only AhpC-reducing Mycobacterium tuberculosis AhpD
-
-
-
additional information
?
-
AhpD contributes to regenerate a variety of thiol-dependent peroxidase in the decomposition of peroxide by linking a dihydrolipoamide dehydrogenase (Lpd)/dihydrolipoamide succinyltransferase (SucB)/NADH system through the cyclization of their own active site dithiol to the oxidized disulphide. The CXXC motif of AhpD is essential to maintain the peroxides reduction activity of thiol-dependent peroxidase. The AhpD system is an important redox system in cells besides the thioredoxin system. Corynebacterium glutamicum AhpD not only has the ability to reduce a variety of thioredoxin-dependent antioxidant enzymes, including mycothiol peroxidase, peroxiredoxin, and Ohr (organic Hydroperoxide Resistance), but also shows a higher affinity for Ohr than those of mycothiol peroxidase and peroxiredoxin, which is different from the only AhpC-reducing Mycobacterium tuberculosis AhpD
-
-
-
additional information
?
-
AhpD contributes to regenerate a variety of thiol-dependent peroxidase in the decomposition of peroxide by linking a dihydrolipoamide dehydrogenase (Lpd)/dihydrolipoamide succinyltransferase (SucB)/NADH system through the cyclization of their own active site dithiol to the oxidized disulphide. The CXXC motif of AhpD is essential to maintain the peroxides reduction activity of thiol-dependent peroxidase. The AhpD system is an important redox system in cells besides the thioredoxin system. Corynebacterium glutamicum AhpD not only has the ability to reduce a variety of thioredoxin-dependent antioxidant enzymes, including mycothiol peroxidase, peroxiredoxin, and Ohr (organic Hydroperoxide Resistance), but also shows a higher affinity for Ohr than those of mycothiol peroxidase and peroxiredoxin, which is different from the only AhpC-reducing Mycobacterium tuberculosis AhpD
-
-
-
additional information
?
-
AhpD contributes to regenerate a variety of thiol-dependent peroxidase in the decomposition of peroxide by linking a dihydrolipoamide dehydrogenase (Lpd)/dihydrolipoamide succinyltransferase (SucB)/NADH system through the cyclization of their own active site dithiol to the oxidized disulphide. The CXXC motif of AhpD is essential to maintain the peroxides reduction activity of thiol-dependent peroxidase. The AhpD system is an important redox system in cells besides the thioredoxin system. Corynebacterium glutamicum AhpD not only has the ability to reduce a variety of thioredoxin-dependent antioxidant enzymes, including mycothiol peroxidase, peroxiredoxin, and Ohr (organic Hydroperoxide Resistance), but also shows a higher affinity for Ohr than those of mycothiol peroxidase and peroxiredoxin, which is different from the only AhpC-reducing Mycobacterium tuberculosis AhpD
-
-
-