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Literature summary for 1.8.4.11 extracted from

  • Si, M.; Zhang, L.; Chaudhry, M.T.; Ding, W.; Xu, Y.; Chen, C.; Akbar, A.; Shen, X.; Liu, S.J.
    Corynebacterium glutamicum methionine sulfoxide reductase A uses both mycoredoxin and thioredoxin for regeneration and oxidative stress resistance (2015), Appl. Environ. Microbiol., 81, 2781-2796 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.4.11

Protein Variants

Protein Variants Comment Organism
additional information site-directed mutagenesis confirms that Cys56 is the peroxidatic cysteine that is oxidized to sulfenic acid, while Cys204 and Cys213 are the resolving Cys residues that form an intramolecular disulfide bond Corynebacterium glutamicum

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q8NLL5
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Corynebacterium glutamicum DSM 20300 Q8NLL5
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information MsrA can reduce methionine sulfoxide via both the thioredoxin/thioredoxin reductase (Trx/TrxR) and mycoredoxin 1/mycothione reductase/mycothiol (Mrx1/Mtr/MSH) pathways. Mrx1 reduces the sulfenic acid intermediate via the formation of an S-mycothiolated MsrA intermediate which is then recycled by mycoredoxin and a second molecule of mycothiol, similarly to the glutathione/glutaredoxin/glutathione reductase system. Trx reduces the Cys204-Cys213 disulfide bond in MsrA produced during methionine sulfoxide reduction via the formation of a transient intermolecular disulfide bond between Trx and MsrA Corynebacterium glutamicum ?
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 ?
additional information MsrA can reduce methionine sulfoxide via both the thioredoxin/thioredoxin reductase (Trx/TrxR) and mycoredoxin 1/mycothione reductase/mycothiol (Mrx1/Mtr/MSH) pathways. Mrx1 reduces the sulfenic acid intermediate via the formation of an S-mycothiolated MsrA intermediate which is then recycled by mycoredoxin and a second molecule of mycothiol, similarly to the glutathione/glutaredoxin/glutathione reductase system. Trx reduces the Cys204-Cys213 disulfide bond in MsrA produced during methionine sulfoxide reduction via the formation of a transient intermolecular disulfide bond between Trx and MsrA Corynebacterium glutamicum DSM 20300 ?
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 ?
peptide-L-methionine (S)-S-oxide + mycothiol
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 Corynebacterium glutamicum peptide-L-methionine + mycothione + H2O
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 ?
peptide-L-methionine (S)-S-oxide + mycothiol
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 Corynebacterium glutamicum DSM 20300 peptide-L-methionine + mycothione + H2O
-
 ?
peptide-L-methionine (S)-S-oxide + thioredoxin
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 Corynebacterium glutamicum peptide-L-methionine + thioredoxin disulfide + H2O
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 ?
peptide-L-methionine (S)-S-oxide + thioredoxin
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 Corynebacterium glutamicum DSM 20300 peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?

Expression

Organism Comment Expression
Corynebacterium glutamicum induced expression under various stresses, regulated directly by the stress-responsive extracytoplasmic-function sigma factor SigH up

General Information

General Information Comment Organism
physiological function Deletion of the msrA gene results in decrease of cell viability, increase of ROS production, and increase of protein carbonylation levels under various stress conditions. MsrA can reduce methionine sulfoxide via both the thioredoxin/thioredoxin reductase (Trx/TrxR) and mycoredoxin 1/mycothione reductase/mycothiol (Mrx1/Mtr/MSH) pathways Corynebacterium glutamicum