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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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
physiological function
drug target
immunization with alkyl hydroperoxide reductase subunit C reduces Fusobacterium nucleatum load in the intestinal tract. AhpC as a potential vaccine candidate against inhabitation or infection of Fusobacterium nucleatum in the intestinal tract, which could provide a practical strategy for the prevention of colorectal cancer associated with Fn infection
drug target
-
immunization with alkyl hydroperoxide reductase subunit C reduces Fusobacterium nucleatum load in the intestinal tract. AhpC as a potential vaccine candidate against inhabitation or infection of Fusobacterium nucleatum in the intestinal tract, which could provide a practical strategy for the prevention of colorectal cancer associated with Fn infection
-
malfunction
DELTAahpCD strain is notably more sensitive than its parent strain to hydrogen peroxide (H2O2) but not to organic peroxides (tertbutyl hydroperoxide and cumene hydroperoxide), in the early log phase. The catalase activity of the DELTAahpCD strain is affected at a relatively low level of H2O2 stress. The DELTAahpCD strain induces a reduced number of stem nodules in Sesbania rostrata with lowering of nitrogenase activity
malfunction
DELTAahpD1DELTAahpD2 mutants exhibit significantly decreased resistance to adverse stress conditions and increased accumulation of reactive oxygen species (ROS)
malfunction
DELTAohr strain presents a reduced capacity to grow in the presence of either artificial (cumene hydroperoxide and tert-butyl hydroperoxide) or fatty acid hydroperoxides compared with the wild type
malfunction
-
DELTAahpCD strain is notably more sensitive than its parent strain to hydrogen peroxide (H2O2) but not to organic peroxides (tertbutyl hydroperoxide and cumene hydroperoxide), in the early log phase. The catalase activity of the DELTAahpCD strain is affected at a relatively low level of H2O2 stress. The DELTAahpCD strain induces a reduced number of stem nodules in Sesbania rostrata with lowering of nitrogenase activity
-
malfunction
-
DELTAahpD1DELTAahpD2 mutants exhibit significantly decreased resistance to adverse stress conditions and increased accumulation of reactive oxygen species (ROS)
-
malfunction
-
DELTAohr strain presents a reduced capacity to grow in the presence of either artificial (cumene hydroperoxide and tert-butyl hydroperoxide) or fatty acid hydroperoxides compared with the wild type
-
physiological function
AhpC is a critical element of the antioxidant defense system of Mycobacterium tuberculosis
physiological function
AhpD is a critical element of the antioxidant defense system of Mycobacterium tuberculosis
physiological function
Mycobacterium tuberculosis persists in host macrophages, where it faces a nutrient-poor environment and is exposed to oxidative and nitrosative stress. The enzyme defends Mycobacterium tuberculosis against oxidative stress
physiological function
the enzyme provides antioxidant protection
physiological function
AhpCD is required for resistance to low concentrations of H2O2 in the free-living stage and during symbiosis with Sesbania rostrata. AhpCD contributes to H2O2 resistance at the early log phase of Azorhizobium caulinodans growth. ahpCD is required for stem nodulation but not root nodulation in Sesbania rostrata
physiological function
AhpD acts as a backup of thioredoxin to provide reducing power for peroxidase
physiological function
-
alkyl hydroperoxide reductase subunit C acquires chaperone activity under heat stress. High-molecular-weight oligomer formation and the chaperone-like activity of oxidized AhpC depend on the incubation temperature and the period of incubation
physiological function
Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite
physiological function
the ahpD gene is more involved in defences against H2O2 than in detoxifying alkyl hydroperoxide. It plays an important role in hydrogen peroxide-induced oxidative stress response
physiological function
the enzyme is involved in the Pseudomonas aeruginosa response to fatty acid hydroperoxides and to peroxynitrite. Therefore, Ohr plays central roles in the bacterial response to two hydroperoxides that are at the host-pathogen interface
physiological function
the enzyme is important for H2O2 detoxification in vitro and also critical for symbiosis of Azorhizobium caulinodans with Sesbania rostrate. The enzyme is required for stem nodulation and nitrogenase activity
physiological function
-
AhpCD is required for resistance to low concentrations of H2O2 in the free-living stage and during symbiosis with Sesbania rostrata. AhpCD contributes to H2O2 resistance at the early log phase of Azorhizobium caulinodans growth. ahpCD is required for stem nodulation but not root nodulation in Sesbania rostrata
-
physiological function
-
Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite
-
physiological function
-
the ahpD gene is more involved in defences against H2O2 than in detoxifying alkyl hydroperoxide. It plays an important role in hydrogen peroxide-induced oxidative stress response
-
physiological function
-
AhpD acts as a backup of thioredoxin to provide reducing power for peroxidase
-
physiological function
-
Mycobacterium tuberculosis persists in host macrophages, where it faces a nutrient-poor environment and is exposed to oxidative and nitrosative stress. The enzyme defends Mycobacterium tuberculosis against oxidative stress
-
physiological function
-
the enzyme provides antioxidant protection
-
physiological function
-
AhpD is a critical element of the antioxidant defense system of Mycobacterium tuberculosis
-
physiological function
-
AhpC is a critical element of the antioxidant defense system of Mycobacterium tuberculosis
-
physiological function
-
the enzyme is important for H2O2 detoxification in vitro and also critical for symbiosis of Azorhizobium caulinodans with Sesbania rostrate. The enzyme is required for stem nodulation and nitrogenase activity
-
physiological function
-
the enzyme is involved in the Pseudomonas aeruginosa response to fatty acid hydroperoxides and to peroxynitrite. Therefore, Ohr plays central roles in the bacterial response to two hydroperoxides that are at the host-pathogen interface
-
Show AA Sequence and Transmembrane Helices (3982 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
-
the redox state of AhpC is a key factor determining the dimer-decamer equilibrium. at 25 °C exists predominantly as a decamer
dimer
-
the redox state of AhpC is a key factor determining the dimer-decamer equilibrium. at 25 °C exists predominantly as a decamer
oligomer
-
heat induces oligomerization of AhpC. At 53°C the oxidized AhpC forms an high-molecular-weight oligomer with a molecular mass of about 2.0-3.0 MDa, corresponding to 100-150 subunits
?
x * 20300, calculated from amino acid sequence
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structures of the H137F and H132Q mutants
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C130S
expressed in yield comparable to that of the wild-type protein. Mutation decreases activity to less than 5% of the wild-type enzyme
C133S
expressed in yield comparable to that of the wild-type protein. Mutation completely suppresses the activity
C174S
mutant enzyme retains about 10% of the wild-type activity
C176S
mutant enzyme retains about 10% of the wild-type activity
Cys129
mutant enzyme shows no activity with cumene hydroperoxide
Cys132
mutant enzyme retains about 5% of the wild-type activity with cumene hydroperoxide
E118F
expressed at 20% of the wild-type expression level. Mutation decreases catalytic activity
E118Q
expressed at 20% of the wild-type expression level. Mutation modestly loweres the catalytic activity
H132F
expressed in yield comparable to that of the wild-type protein. Mutation decreases the catalytic activity
H132Q
mutant tends to unfold and degrade relatively easily. Mutation decreases the catalytic activity. The H137Q mutation decreases the activity more severely than the H132Q mutation
H137F
expressed in yield comparable to that of the wild-type protein. Mutation decreases the catalytic activity
H137Q
expressed at 20% of the wild-type expression level. Mutation decreases the catalytic activity. The H137Q mutation decreases the activity more severely than the H132Q mutation
C130S
-
expressed in yield comparable to that of the wild-type protein. Mutation decreases activity to less than 5% of the wild-type enzyme
-
C133S
-
expressed in yield comparable to that of the wild-type protein. Mutation completely suppresses the activity
-
C174S
-
mutant enzyme retains about 10% of the wild-type activity
-
C176S
-
mutant enzyme retains about 10% of the wild-type activity
-
Cys129
-
mutant enzyme shows no activity with cumene hydroperoxide
-
Cys132
-
mutant enzyme retains about 5% of the wild-type activity with cumene hydroperoxide
-
E118Q
-
expressed at 20% of the wild-type expression level. Mutation modestly loweres the catalytic activity
-
H132Q
-
mutant tends to unfold and degrade relatively easily. Mutation decreases the catalytic activity. The H137Q mutation decreases the activity more severely than the H132Q mutation
-
H137Q
-
expressed at 20% of the wild-type expression level. Mutation decreases the catalytic activity. The H137Q mutation decreases the activity more severely than the H132Q mutation
-
C154S
mutant enzyme loses peroxidase activity. The enzyme shows no activity and no formation of intramolecular disulfide bond upon treatment with hydroperoxides
C87S
mutant enzyme loses peroxidase activity. The enzyme shows no activity and no formation of intramolecular disulfide bond upon treatment with hydroperoxides
C154S
-
mutant enzyme loses peroxidase activity. The enzyme shows no activity and no formation of intramolecular disulfide bond upon treatment with hydroperoxides
-
C87S
-
mutant enzyme loses peroxidase activity. The enzyme shows no activity and no formation of intramolecular disulfide bond upon treatment with hydroperoxides
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is neither induced by H2O2 nor controlled by OxyR
expression of ohr is induced in cells exposed to 3-morpholinosydnonimine hydrochloride
induced under various stresses
enzyme expression is neither induced by H2O2 nor controlled by OxyR
enzyme expression is neither induced by H2O2 nor controlled by OxyR
-
-
expression of ohr is induced in cells exposed to 3-morpholinosydnonimine hydrochloride
expression of ohr is induced in cells exposed to 3-morpholinosydnonimine hydrochloride
expression of ohr is induced in cells exposed to 3-morpholinosydnonimine hydrochloride
-
-
expression of ohr is induced in cells exposed to 3-morpholinosydnonimine hydrochloride
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
AhpCis a critical element of the antioxidant defense system of Mycobacterium tuberculosis and may be suitable target for the development of novel anti-tuberculosis strategies
medicine
AhpD is a critical element of the antioxidant defense system of Mycobacterium tuberculosis and may be suitable target for the development of novel anti-tuberculosis strategies
medicine
immunization with alkyl hydroperoxide reductase subunit C reduces Fusobacterium nucleatum load in the intestinal tract. AhpC as a potential vaccine candidate against inhabitation or infection of Fusobacterium nucleatum in the intestinal tract, which could provide a practical strategy for the prevention of colorectal cancer associated with Fn infection
medicine
the use of AhpC as a potential vaccine candidate against inhabitation or infection of Fusobacterium nucleatum in the intestinal tract, which can provide a practical strategy for the prevention of colorectal cancer associated with Fusobacterium nucleatum infection
medicine
-
immunization with alkyl hydroperoxide reductase subunit C reduces Fusobacterium nucleatum load in the intestinal tract. AhpC as a potential vaccine candidate against inhabitation or infection of Fusobacterium nucleatum in the intestinal tract, which could provide a practical strategy for the prevention of colorectal cancer associated with Fn infection
-
medicine
-
the use of AhpC as a potential vaccine candidate against inhabitation or infection of Fusobacterium nucleatum in the intestinal tract, which can provide a practical strategy for the prevention of colorectal cancer associated with Fusobacterium nucleatum infection
-
medicine
-
AhpD is a critical element of the antioxidant defense system of Mycobacterium tuberculosis and may be suitable target for the development of novel anti-tuberculosis strategies
-
medicine
-
AhpCis a critical element of the antioxidant defense system of Mycobacterium tuberculosis and may be suitable target for the development of novel anti-tuberculosis strategies
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shi, S.; Ehrt, S.
Dihydrolipoamide acyltransferase is critical for Mycobacterium tuberculosis pathogenesis
Infect. Immun.
74
56-63
2006
Mycobacterium tuberculosis (P9WQB5), Mycobacterium tuberculosis (P9WQB7), Mycobacterium tuberculosis ATCC 25618 (P9WQB5), Mycobacterium tuberculosis ATCC 25618 (P9WQB7)
brenda
Hillas, P.J.; del Alba, F.S.; Oyarzabal, J.; Wilks, A.; Ortiz De Montellano, P.R.
The AhpC and AhpD antioxidant defense system of Mycobacterium tuberculosis
J. Biol. Chem.
275
18801-18809
2000
Mycobacterium tuberculosis (P9WQB5), Mycobacterium tuberculosis (P9WQB7), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WQB5), Mycobacterium tuberculosis ATCC 25618 (P9WQB7)
brenda
Koshkin, A.; Nunn, C.M.; Djordjevic, S.; Ortiz de Montellano, P.R.
The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics
J. Biol. Chem.
278
29502-29508
2003
Mycobacterium tuberculosis (P9WQB5), Mycobacterium tuberculosis ATCC 25618 (P9WQB5)
brenda
Cussiol, J.R.; Alegria, T.G.; Szweda, L.I.; Netto, L.E.
Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase
J. Biol. Chem.
285
21943-21950
2010
Xylella fastidiosa (Q9PCF4), Xylella fastidiosa 9a5c (Q9PCF4)
brenda
Jiang, G.; Yang, J.; Li, X.; Cao, Y.; Liu, X.; Ling, J.; Wang, H.; Zhong, Z.; Zhu2, J.
Alkyl hydroperoxide reductase is important for oxidative stress resistance and symbiosis in Azorhizobium caulinodans
FEMS Microbiol. Lett.
366
fnz014
2019
Azorhizobium caulinodans (A8HQP5), Azorhizobium caulinodans (A8HQP9 AND A8HQP5), Azorhizobium caulinodans, Azorhizobium caulinodans ORS 571 (A8HQP9 AND A8HQP5), Azorhizobium caulinodans ORS571 (A8HQP5)
brenda
Hong, E.; Jeong, H.; Lee, D.; Kim, Y.; Lee, H.
The ahpD gene of Corynebacterium glutamicum plays an important role in hydrogen peroxide-induced oxidative stress response
J. Biochem.
165
197-204
2019
Corynebacterium glutamicum (Q8NMX8), Corynebacterium glutamicum ATCC 13032 (Q8NMX8)
brenda
Su, T.; Si, M.; Zhao, Y.; Yao, S.; Che, C.; Liu, Y.; Chen, C.
Function of alkyl hydroperoxidase AhpD in resistance to oxidative stress in Corynebacterium glutamicum
J. Gen. Appl. Microbiol.
65
72-79
2019
Corynebacterium glutamicum (Q8NMX8), Corynebacterium glutamicum (Q8NN44), Corynebacterium glutamicum ATCC 13032 (Q8NMX8), Corynebacterium glutamicum ATCC 13032 (Q8NN44)
brenda
Alegria, T.; Meireles, D.; Cussiol, J.; Hugo, M.; Trujillo, M.; De Oliveira, M.; Miyamoto, S.; Queiroz, R.; Valadares, N.; Garratt, R.; Radi, R.; Di Mascio, P.; Augusto, O.; Netto, L.
Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite
Proc. Natl. Acad. Sci. USA
114
E132-E141
2017
Pseudomonas aeruginosa (A0A0H2ZCJ7), Xylella fastidiosa (Q9PCF4), Xylella fastidiosa, Xylella fastidiosa 9a5c (Q9PCF4), Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2ZCJ7)
brenda
Meireles, D.; Domingos, R.; Gaiarsa, J.; Ragnoni, E.; Bannitz-Fernandes, R.; da Silva Neto, J.; de Souza, R.; Netto, L.
Functional and evolutionary characterization of Ohr proteins in eukaryotes reveals many active homologs among pathogenic fungi
Redox Biol.
12
600-609
2017
Pseudocercospora fijiensis (N1Q9R6), Pseudocercospora fijiensis, Pseudocercospora fijiensis CIRAD86 (N1Q9R6)
brenda
Guo, S.H.; Wang, H.F.; Nian, Z.G.; Wang, Y.D.; Zeng, Q.Y.; Zhang, G.
Immunization with alkyl hydroperoxide reductase subunit C reduces Fusobacterium nucleatum load in the intestinal tract
Sci. Rep.
7
10566
2017
Fusobacterium nucleatum (Q8R6D3), Fusobacterium nucleatum subsp. nucleatum (Q8R6D3), Fusobacterium nucleatum subsp. nucleatum ATCC 25586 (Q8R6D3), Fusobacterium nucleatum ATCC 25586 (Q8R6D3)
brenda
Kamariah, N.; Eisenhaber, B.; Eisenhaber, F.; Grber, G.
Molecular mechanism of the Escherichia coli AhpC in the function of a chaperone under heat-shock conditions
Sci. Rep.
8
14151
2018
Escherichia coli
brenda
Zhang, B.; Gu, H.; Yang, Y.; Bai, H.; Zhao, C.; Si, M.; Su, T.; Shen, X.
Molecular mechanisms of AhpC in resistance to oxidative stress in Burkholderia thailandensis
Front. Microbiol.
10
1483
2019
Burkholderia thailandensis
brenda
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