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Literature summary for 2.8.1.2 extracted from

  • Hoefler, S.; Lorenz, C.; Busch, T.; Brinkkoetter, M.; Tohge, T.; Fernie, A.R.; Braun, H.P.; Hildebrandt, T.M.
    Dealing with the sulfur part of cysteine four enzymatic steps degrade l-cysteine to pyruvate and thiosulfate in Arabidopsis mitochondria (2016), Physiol. Plant., 157, 352-366 .
    View publication on PubMed
Search for more literature for 2.8.1.2

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
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 Arabidopsis thaliana 5739
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Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana O64530 cf. EC 2.8.1.1
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-mercaptopyruvate + 2 glutathione
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 Arabidopsis thaliana pyruvate + glutathione disulfide
-
 ?
thiosulfate + glutathione
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 Arabidopsis thaliana sulfite + glutathione disulfide
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 ?

Synonyms

Synonyms Comment Organism
AT1G79230
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 Arabidopsis thaliana

General Information

General Information Comment Organism
metabolism a mitochondrial sulfur catabolic pathway catalyzes the complete oxidation of L-cysteine to pyruvate and thiosulfate. After transamination to 3-mercaptopyruvate, the sulfhydryl group from L-cysteine is transferred to glutathione by sulfurtransferase Str1 and oxidized to sulfite by the sulfur dioxygenase Ethe1. Sulfite is then converted to thiosulfate by addition of a second persulfide group by sulfurtransferase 1. This pathway is most relevant during early embryo development and for vegetative growth under light-limiting conditions Arabidopsis thaliana
physiological function embryo development of the thiosulfate sulfurtransferase Str1/sulfur dioxygenase Ethe1 double mutant is comparable with Str1 mutant lines and severyl impaired in comparison to wild-type. Embryogenesis is severely delayed in Str1 mutants and the Ethe1/Str1 double mutant Arabidopsis thaliana