Information on EC 1.8.2.6 - S-disulfanyl-L-cysteine oxidoreductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.8.2.6
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RECOMMENDED NAME
GeneOntology No.
S-disulfanyl-L-cysteine oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[SoxY protein]-S-disulfanyl-L-cysteine + 6 ferricytochrome c + 3 H2O = [SoxY protein]-S-sulfosulfanyl-L-cysteine + 6 ferrocytochrome c + 6 H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
thiosulfate oxidation III (multienzyme complex)
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Sulfur metabolism
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SYSTEMATIC NAME
IUBMB Comments
[SoxY protein]-S-disulfanyl-L-cysteine:cytochrome-c oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q47BB7 i.e. subunit SoxC, Q47BB8 i.e. subunit SoxD
Q47BB7, Q47BB8
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[SoxY protein]-S-disulfanyl-L-cysteine + 6 ferricytochrome c + 3 H2O
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 6 ferrocytochrome c + 6 H+
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c
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the cytochrome c motifs of subunit SoxD are buried in the protein core
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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recombinant SoxX, SoxY, SoxZ, SoxA, SoxB, and SoxCD protein mixture
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
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density-gradient gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
molecular docking studies and comparison of the molecular mechanism of sulfur oxidation process in Dechloromonas aromatica and Thiobacillus denitrificans, the latter using proteins SoxAX instead of proteins SoxCD for recycling of SoxY. The SoxYZ protein of SoxCD lacking Thiobacillus denitrificans is more stable and interactive, in comparison with the SoxYZ complex from SoxCD-possessing Dechloromonas aromatica
Q47BB7; Q47BB8;
crystal structure of SoxCD1, solved at 1.33 A . SoxCD1 misses the heme-2 domain D2 and is catalytically as active as SoxCD.The substrate of SoxCD is the outer (sulfane) sulfur of Cys-110-persulfide located at the C-terminal peptide swinging arm of SoxY of the SoxYZ carrier complex. The oxidation reactions of the sulfane-sulfur are initiated by the nucleophilic attack of the persulfide anion on the molybdenum atom that is, in turn, reduced. The close proximity of heme-1 to the molybdopterin allows easy acceptance of the electrons
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homology modeling of structure. SoxD belongs to the di-heme cytochrome c family of electron transport proteins whereas soxC gene product (SoxC) is a sulfur dehydrogenase
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 80
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recombinant SoxX, SoxY, SoxZ, SoxA, SoxB, and SoxCD protein mixture
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification in presece of phenylmethylsulfonyl fluoride
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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construction of a mutant lacking the heme-2 domain. Exclusively the heme-1 domain of SoxD is required for activity, substrate specificity, and electron yield of the sulfur-oxidizing system, kinetic data are similar to wild-type
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine