1.8.2.6: S-disulfanyl-L-cysteine oxidoreductase
This is an abbreviated version!
For detailed information about S-disulfanyl-L-cysteine oxidoreductase, go to the full flat file.
Word Map on EC 1.8.2.6
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1.8.2.6
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sulfur-oxidizing
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pantotrophus
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paracoccus
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thiosulfate
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chemotrophic
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soxxa
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sulfane
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dissimilatory
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chemolithoautotrophic
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molybdopterin
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flavocytochrome
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allochromatium
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thioalkalivibrio
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heme-1
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haloalkaliphilic
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vinosum
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six-electron
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medicine
- 1.8.2.6
-
sulfur-oxidizing
- pantotrophus
-
paracoccus
- thiosulfate
-
chemotrophic
- soxxa
-
sulfane
-
dissimilatory
-
chemolithoautotrophic
- molybdopterin
-
flavocytochrome
-
allochromatium
- thioalkalivibrio
-
heme-1
-
haloalkaliphilic
- vinosum
-
six-electron
- medicine
Reaction
Synonyms
Daro_3133, Daro_3134, SoxCD, sulfite-dehydrogenase, sulfur dehydrogenase
ECTree
1.8.2.6 S-disulfanyl-L-cysteine oxidoreductaseAdvanced search results
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results (Subunits
Subunits on EC 1.8.2.6 - S-disulfanyl-L-cysteine oxidoreductase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
heterotetramer
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structure resembles a tight alpha2beta-complex with internal 2-fold symmetry, crystallization data
tetramer
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2 * 43000, subunit SoxC, plus 2 * 47000, subunit SoxD, SDS-PAGE
additional information
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dimerization of subunit SoxD helps to bring the two distant heme groups in close proximity, which helps in the transport of electrons efficiently from one part of the protein to the other part, structure modeling data. subunits SoxC and SoxD interact strongly with each other
