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Information on EC 1.11.1.25 - glutaredoxin-dependent peroxiredoxin
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1.11.1.25 glutaredoxin-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. To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Glutaredoxin-dependent peroxiredoxins have been reported from bacteria, fungi, plants, and animals. These enzymes are often able to use an alternative reductant such as thioredoxin or glutathione.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
peroxiredoxin-glutaredoxin, prxiib, prx5-grx, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PRXIIB
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
glutaredoxin: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. To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Glutaredoxin-dependent peroxiredoxins have been reported from bacteria, fungi, plants, and animals. These enzymes are often able to use an alternative reductant such as thioredoxin or glutathione.
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
glutaredoxin + benzoquinone
glutaredoxin disulfide + H2O + hydroquinone
-
-
-
?
glutaredoxin 2 + H2O2
glutaredoxin 2 disulfide + 2 H2O
-
-
-
?
glutaredoxin 3 + H2O2
glutaredoxin 3 disulfide + 2 H2O
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
glutaredoxin 2
pH and temperature not specified in the publication
-
0.018
glutaredoxin 3
pH and temperature not specified in the publication
-
0.0133
H2O2
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
52.8
benzoquinone
pH and temperature not specified in the publication
0.27
H2O2
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20.3
H2O2
pH and temperature not specified in the publication
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
detoxification system, the enzyme prevents the damages caused by hydroperoxides
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q9WYL7_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
321
0
37186
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Couturier, J.
Prosper, P.M.; Winger, A.M.; Hecker, A.; Hirasawa, M. Knaff, D.B.; Gans, P.; Jacquot, J.P.; Navaza, A.; Haouz, A.; Rouhier, N. In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima
Antioxid. Redox Signal.
18
1613-1622
2013
Thermotoga maritima (Q9WYL7), Thermotoga maritima (Q9WZN7), Thermotoga maritima ATCC 43589 (Q9WYL7), Thermotoga maritima ATCC 43589 (Q9WZN7)
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