1.8.98.2: sulfiredoxin

This is an abbreviated version!
For detailed information about sulfiredoxin, go to the full flat file.

Reaction

Synonyms

AtSrx, cysteine-sulfinic acid reductase, neoplastic progression 3, peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase, protein cysteine sulfinic acid reductase, Srx, Srx1, Srxn1, sulfiredoxin, sulfiredoxin 1, sulfiredoxin-1, sulphiredoxin

ECTree

     1 Oxidoreductases

         1.8 Acting on a sulfur group of donors

             1.8.98 With other, known, physiological acceptors

                1.8.98.2 sulfiredoxin

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1	Activating Compound
1793	AA Sequence
5	Application
1	CAS Registry Number
19	Cloned(Commentary)
17	Cofactor
4	Crystallization (Commentary)
228	Disease/ Diagnostics
8	Expression
18	General Information
2	IC50 Value
9	Inhibitors
8	KM Value [mM]
20	Localization
11	Metals/Ions
6	Molecular Weight [Da]
21	Natural Substrates/ Products (Substrates)
50	Organism
26	PDB ID
3	pH Optimum
3	pI Value
36	Protein Variants
9	Purification (Commentary)
1	Reaction
17	Reaction Type
44	Reference
40	Source Tissue
73	Substrates and Products (Substrate)
3	Subunits
54	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
5	Turnover Number [1/s]

Natural Substrates Products

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Natural Substrates Products on EC 1.8.98.2 - sulfiredoxin

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

8 entries

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide

3 entries

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

3 entries

additional information

?

-

6 entries

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

Arabidopsis thaliana

Q8GY89

-

764076

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

Homo sapiens

Q9BYN0

-

763914, 765061

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

Homo sapiens

-

-

765061

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

Homo sapiens

-

antioxidant protein with a role in signaling through catalytic reduction of oxidative modifications. Srx also has a role in the reduction of glutathionylation a post-translational, oxidative modification that occurs on numerous proteins and has been implicated in a wide variety of pathologies, including Parkinson‘s disease. Unlike the reduction of peroxiredoxin overoxidation, Srx-dependent deglutathionylation appears to be nonspecific

658255

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

Homo sapiens

Q9BYN0

repairs the inactivated forms of typical two-Cys peroxiredoxins implicated in hydrogen peroxide-mediated cell signaling

658132

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

Homo sapiens

-

Srx is largely responsible for reduction of the Cys-SO2H of peroxiredoxin in A549 human cells

659421

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

Rattus norvegicus

-

reduction of Cys-SO2H by Srx is specific to 2-Cys peroxiredoxin isoforms. For proteins such as Prx VI and GAPDH, sulfinic acid formation might be an irreversible process that causes protein damage

659491

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

Saccharomyces cerevisiae

-

sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine–sulphinic acid modifications, and in signalling pathways involving protein oxidation

659998

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide

Arabidopsis thaliana

-

-

742996

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide

Homo sapiens

Q9BYN0

-

765246

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide

Mus musculus

-

-

742566

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

Arabidopsis thaliana

Q8GY89

AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature

670564

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

Homo sapiens

-

-

695553, 698928, 698993, 700520

-

-

?

peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R

Saccharomyces cerevisiae

-

-

698953

-

-

?

additional information

?

-

Arabidopsis thaliana

Q8GY89

AtSrx has sulfinic acid reductase activity to catalyze the reduction of the overoxidized form of 2-Cys Prx in vitro and in vivo

764076

-

-

-

additional information

?

-

Arabidopsis thaliana

-

AtSrx has sulfinic acid reductase activity to catalyze the reduction of the overoxidized form of 2-Cys Prx in vitro and in vivo

764076

-

-

-

additional information

?

-

Homo sapiens

-

catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation

698052

-

-

?

additional information

?

-

Homo sapiens

Q9BYN0

Srx forms a complex with the endoplasmic reticulum-resident protein thioredoxin domain-containing protein 5 (TXNDC5) in vivo and in vitro. TXNDC5 directly interacts with Srx through its thioredoxin-like domains, mapping of the interacting domains between Srx and TXNDC5, the thioredoxin-like domains 1 and 3 are responsible for the binding to Srx, overview. Deletion of the first or third thioredoxin-like domain in TXNDC5 results in a significant loss of its binding to Srx, whereas deletion of the second (the one in the middle) thioredoxin-like domain does not compromise its binding to Srx. The Srx-TXNDC5 is a relatively stable complex that is not affected by the treatment with exogenous H2O2

765061

-

-

-

additional information

?

-

Homo sapiens

-

Srx forms a complex with the endoplasmic reticulum-resident protein thioredoxin domain-containing protein 5 (TXNDC5) in vivo and in vitro. TXNDC5 directly interacts with Srx through its thioredoxin-like domains, mapping of the interacting domains between Srx and TXNDC5, the thioredoxin-like domains 1 and 3 are responsible for the binding to Srx, overview. Deletion of the first or third thioredoxin-like domain in TXNDC5 results in a significant loss of its binding to Srx, whereas deletion of the second (the one in the middle) thioredoxin-like domain does not compromise its binding to Srx. The Srx-TXNDC5 is a relatively stable complex that is not affected by the treatment with exogenous H2O2

765061

-

-

-

additional information

?

-

Mus musculus

-

catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation

698052

-

-

?