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Information on EC 1.11.1.28 - lipoyl-dependent peroxiredoxin and Organism(s) Azorhizobium caulinodans and UniProt Accession A8HQP5

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.28 lipoyl-dependent peroxiredoxin
IUBMB 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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Azorhizobium caulinodans
UNIPROT: A8HQP5
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The taxonomic range for the selected organisms is: Azorhizobium caulinodans
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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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
+
=
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine
+
+
Synonyms
organic hydroperoxide resistance, peroxiredoxin ahpc, organic hydroperoxide resistance protein, ahpcd, mfohr, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkyl hydroperoxide reductase
-
AhpC
-
-
-
-
AhpD
-
-
-
-
alkyl hydroperoxide reductase
-
Ohr
-
-
-
-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 20300, calculated from amino acid sequence
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is neither induced by H2O2 nor controlled by OxyR
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team