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Information on EC 1.11.1.26 - NADH-dependent peroxiredoxin and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9I6Z2

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.26 NADH-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. This bacterial peroxiredoxin differs from most other forms by comprising two types of subunits. One subunit (AhpC) is a typical 2-Cys peroxiredoxin. Following the reduction of the substrate, one AhpC subunit forms a disulfide bond with an identical unit. The disulfide bond is reduced by the second type of subunit (AhpF). This second subunit is a flavin-containing protein that uses electrons from NADH to reduce the cysteine residues on the AhpC subunits back to their active state.
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Pseudomonas aeruginosa
UNIPROT: Q9I6Z2
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide
NADH
+
ROOH
+
H+
=
NAD+
+
H2O
+
ROH
+
+
=
+
+
Synonyms
ahpcf, alkylhydroperoxide reductase, ahpc1, alkyl hydroperoxidase, alkyl hydroperoxide reductase subunit f, nadh peroxidase alkyl hydroperoxide reductase, nadh-dependent peroxiredoxin, alkyl-hydroperoxide reductase c1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkyl hydroperoxide reductase subunit F
-
AhpC
-
-
-
-
AhpF
-
-
-
-
alkyl hydroperoxide reductase
-
-
-
-
alkyl-hydroperoxide reductase C1
-
SYSTEMATIC NAME
IUBMB Comments
NADH: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 [1]. 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. This bacterial peroxiredoxin differs from most other forms by comprising two types of subunits. One subunit (AhpC) is a typical 2-Cys peroxiredoxin. Following the reduction of the substrate, one AhpC subunit forms a disulfide bond with an identical unit. The disulfide bond is reduced by the second type of subunit (AhpF). This second subunit is a flavin-containing protein that uses electrons from NADH to reduce the cysteine residues on the AhpC subunits back to their active state.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NADH + H2O2 + H+
NAD+ + 2 H2O
show the reaction diagram
-
-
-
?
NADH + urate hydroperoxide + H+
?
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
dual function of Pseudomonas aeruginosa AhpF (PaAhpF) as a reductase and a molecular chaperone. The reductase and foldase chaperone function of PaAhpF predominated for its low-molecular-weight form, whereas the holdase chaperone function of PaAhpF is associated with its high-molecular-weight complex. PaAhpF has multiple function in controlling oxidative and heat stresses in Pseudomonas aeruginosa resistance to oxidative and heat stress
malfunction
enzyme deletion leads to a higher sensitivity to hypochlorous acid, hydrogen peroxide and urate hydroperoxide. The enzyme-deficient strain is more sensitive to the killing by isolated neutrophils and less virulent in a mice model of infection
physiological function
the enzyme is a relevant scavenger of oxidants generated during inflammatory oxidative burst and a mechanism of Pseudomonas aeruginosa escaping from killing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
158000
gel filtration, low-molecular-weight complex
57000
reducing and non-reducing SDS-PAGE
660000
gel filtration, high-molecular-weight complex
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hong, S.H.; Singh, S.; Tripathi, B.N.; Mondal, S.; Lee, S.; Jung, H.S.; Cho, C.; Kaur, S.; Kim, J.H.; Lee, S.; Bai, H.W.; Bae, H.J.; Lee, S.Y.; Lee, S.S.; Chung, B.Y.
Functional properties and the oligomeric state of alkyl hydroperoxide reductase subunit F (AhpF) in Pseudomonas aeruginosa
Protoplasma
257
807-817
2020
Pseudomonas aeruginosa (Q9I6Z2), Pseudomonas aeruginosa
Manually annotated by BRENDA team
Rocha, L.S.; Silva, B.P.D.; Correia, T.M.L.; Silva, R.P.D.; Meireles, D.A.; Pereira, R.; Netto, L.E.S.; Meotti, F.C.; Queiroz, R.F.
Peroxiredoxin AhpC1 protects Pseudomonas aeruginosa against the inflammatory oxidative burst and confers virulence
Redox Biol.
46
102075
2021
Pseudomonas aeruginosa (A0A072ZH89), Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14 (A0A072ZH89)
Manually annotated by BRENDA team