MPST and TXN2 enable the synthesis of disulfanide from CysS248-MPST

Stable Identifier
R-HSA-9035484
Type
Reaction [transition]
Species
Homo sapiens
Compartment
mitochondrial matrix
Synonyms
(thioredoxin)-dithiol + S-sulfanyl-L-cysteinyl-(protein) => (thioredoxin)-disulfide + H(+) + hydrogen sulfide + L-cysteinyl-(protein)
ReviewStatus
5/5
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MPST and TXN2 enable the synthesis of disulfanide from CysS248-MPST
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Hydrogen polysulfanides, which have diverse regulatory effects, are produced from CysS248-MPST (3-mercaptopyruvate sulfurtransferase) that has been persulfurated at cysteine residue 248. A sequence of steps, annotated here as a single event enabled by TXN2 (mitochondrial thioredoxin) associated with CysS248-MPST, restores MPST to its underivatized form while generating disulfanide (HSS-) and disulfide-bonded 2HC-TXN2 (Kimura et al. 2013, Kimura et al. 2017, Koike et al. 2017, Smeets et al. 2005, Yadav et al. 2013).
Literature References
PubMed ID Title Journal Year
23698001 Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase

Yadav, PK, Yamada, K, Chiku, T, Koutmos, M, Banerjee, R

J. Biol. Chem. 2013
23413359 Polysulfides are possible H2S-derived signaling molecules in rat brain

Kimura, Y, Mikami, Y, Osumi, K, Tsugane, M, Oka, J, Kimura, H

FASEB J. 2013
28874874 3-Mercaptopyruvate sulfurtransferase produces potential redox regulators cysteine- and glutathione-persulfide (Cys-SSH and GSSH) together with signaling molecules H2S2, H2S3 and H2S

Kimura, Y, Koike, S, Shibuya, N, Lefer, D, Ogasawara, Y, Kimura, H

Sci Rep 2017
16195549 Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2

Smeets, A, Evrard, C, Landtmeters, M, Marchand, C, Knoops, B, Declercq, JP

Protein Sci. 2005
29055825 Analysis of endogenous H2S and H2Sn in mouse brain by high-performance liquid chromatography with fluorescence and tandem mass spectrometric detection

Koike, S, Kawamura, K, Kimura, Y, Shibuya, N, Kimura, H, Ogasawara, Y

Free Radic. Biol. Med. 2017
Participants
Input
Output
Participates
as an event of
Catalyst Activity

oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor of CysS248-MPST:TXN2 [mitochondrial matrix]

Physical Entity
CysS248-MPST:TXN2 [mitochondrial matrix] (Homo sapiens)
Activity
oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor (GO:0016671)
Orthologous Events
MPST and TXN2 enable the synthesis of disulfanide from CysS248-MPST (Bos taurus)
MPST and TXN2 enable the synthesis of disulfanide from CysS248-MPST (Caenorhabditis elegans)
MPST and TXN2 enable the synthesis of disulfanide from CysS248-MPST (Danio rerio)
MPST and TXN2 enable the synthesis of disulfanide from CysS248-MPST (Dictyostelium discoideum)
MPST and TXN2 enable the synthesis of disulfanide from CysS248-MPST (Gallus gallus)
MPST and TXN2 enable the synthesis of disulfanide from CysS248-MPST (Mus musculus)
MPST and TXN2 enable the synthesis of disulfanide from CysS248-MPST (Rattus norvegicus)
MPST and TXN2 enable the synthesis of disulfanide from CysS248-MPST (Sus scrofa)
MPST and TXN2 enable the synthesis of disulfanide from CysS248-MPST (Xenopus tropicalis)
Cross References
RHEA
Authored
Jassal, B  (2018-01-23)
Reviewed
Kimura, H  (2018-01-25)
Hill, DP  (2025-02-25)
Created
Jassal, B  (2018-01-23)
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