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Information on EC 1.11.1.28 - lipoyl-dependent peroxiredoxin
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1.11.1.28 lipoyl-dependent peroxiredoxinIUBMB Comments
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins . The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see {single/111115a::mechanism}). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Two types of lipoyl-dependent peroxiredoxins have been reported from bacteria. One type is the AhpC/AhpD system, originally described from Mycobacterium tuberculosis. In that system, AhpC catalyses reduction of the substrate, resulting in an intramolecular disulfide. AhpD then forms an intermolecular disulfide crosslink with AhpC, reducing it back to active state. AhpD is reduced in turn by lipoylated proteins. The second type, which has been characterized in Xylella fastidiosa, consists of only one type of subunit, which interacts directly with lipoylated proteins.
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Word Map
- 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
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
=
+
+
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine
+
=
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine
+
+
Synonyms
organic hydroperoxide resistance, organic hydroperoxide resistance protein, peroxiredoxin ahpc, ahpcd, mfohr, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AhpC
AhpCD
AhpD
ahpD1
ahpD2
alkyl hydroperoxide reductase
alkyl hydroperoxide reductase subunit C
EC 1.11.1.15
-
-
formerly, part transferred
-
MfOhr
Ohr
Organic hydroperoxide resistance
organic hydroperoxide resistance protein
peroxiredoxin AhpC
peroxiredoxin AhpD
AhpC
-
-
-
-
AhpD
-
-
-
-
alkyl hydroperoxide reductase subunit C
-
-
Ohr
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + ROOH = a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ROH
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
lipoyl:hydroperoxide oxidoreductase
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins [2]. The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see {single/111115a::mechanism}). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Two types of lipoyl-dependent peroxiredoxins have been reported from bacteria. One type is the AhpC/AhpD system, originally described from Mycobacterium tuberculosis. In that system, AhpC catalyses reduction of the substrate, resulting in an intramolecular disulfide. AhpD then forms an intermolecular disulfide crosslink with AhpC, reducing it back to active state. AhpD is reduced in turn by lipoylated proteins. The second type, which has been characterized in Xylella fastidiosa, consists of only one type of subunit, which interacts directly with lipoylated proteins.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-[(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 + 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 + 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-[(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-[(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 + 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
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-[(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-[(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
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-[(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 + tert-butyl hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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-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
-
-
?
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
-
-
-
?
additional information
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + ROOH
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ROH
-
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tween-20
0.25%, the enzyme retains more than 80% of its original activity toward tert-butyl hydroperoxide. The activity toward LAOOH is maximal
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Immunization of Mice with Recombinant Brucella abortus Organic Hydroperoxide Resistance (Ohr) Protein Protects Against a Virulent Brucella abortus 544 Infection.
Tuberculosis
Structure and mechanism of the alkyl hydroperoxidase AhpC, a key element of the Mycobacterium tuberculosis defense system against oxidative stress.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03851
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine
pH 7.4, 37°C
-
0.01093
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complexlipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine
pH 7.4, 37°C
-
0.091
7alpha-hydroperoxy-3beta-hydroxycholest-6-ene
pH 7.0, 25°C
0.132
7alpha-hydroperoxy-3beta-hydroxycholest-6-ene
pH 7.0, 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.95
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine
pH 7.4, 37°C
-
9.5
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complexlipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine
pH 7.4, 37°C
-
0.147
7alpha-hydroperoxy-3beta-hydroxycholest-6-ene
pH 7.0, 25°C
0.178
7alpha-hydroperoxy-3beta-hydroxycholest-6-ene
pH 7.0, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
460
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine
pH 7.4, 37°C
-
870
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complexlipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine
pH 7.4, 37°C
-
1.35
7alpha-hydroperoxy-3beta-hydroxycholest-6-ene
pH 7.0, 25°C
1.62
7alpha-hydroperoxy-3beta-hydroxycholest-6-ene
pH 7.0, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
alkyl hydroperoxide reductase C (ahpC)
SwissProt
brenda
alkyl hydroperoxide reductase D (ahpD)
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme is preferentially located in mitochondrion
brenda
-
the enzyme is preferentially located in mitochondrion
-
brenda
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