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Information on EC 1.8.1.19 - sulfide dehydrogenase and Organism(s) Pyrococcus furiosus and UniProt Accession Q8U194

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EC Tree
     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.1 With NAD+ or NADP+ as acceptor
                1.8.1.19 sulfide dehydrogenase
IUBMB Comments
A iron-sulfur flavoprotein. In the archaeon Pyrococcus furiosus the enzyme is involved in the oxidation of NADPH which is produced in peptide degradation. The enzyme also catalyses the reduction of sulfur with lower activity.
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This record set is specific for:
Pyrococcus furiosus
UNIPROT: Q8U194
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The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
sulfide dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
hydrogen sulfide,polysulfide(n-1):NADP+ oxidoreductase
A iron-sulfur flavoprotein. In the archaeon Pyrococcus furiosus the enzyme is involved in the oxidation of NADPH which is produced in peptide degradation. The enzyme also catalyses the reduction of sulfur with lower activity.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(sulfide)n+1 + NADPH + H+
hydrogen sulfide + (sulfide)n + NADP+
show the reaction diagram
NADH is not utilized as an electron donor for polysulfide reduction. Polysulfide reduction is catalyzed with reduced ferredoxin as an electron donor. However, the rate of sulfide production, at least in vitro, is much lower than when the enzyme uses NADPH to provide reductant for polysulfide reduction
-
-
?
colloidal sulfur + NADPH + H+
?
show the reaction diagram
the relative activity is about 40% compared to the activity with polysulfide
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(sulfide)n+1 + NADPH + H+
hydrogen sulfide + (sulfide)n + NADP+
show the reaction diagram
NADH is not utilized as an electron donor for polysulfide reduction. Polysulfide reduction is catalyzed with reduced ferredoxin as an electron donor. However, the rate of sulfide production, at least in vitro, is much lower than when the enzyme uses NADPH to provide reductant for polysulfide reduction
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
both the alpha-subunit and the beta-subunit contains one FAD
Fe-S center
flavin
enzyme contains flavin
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.25
(sulfide)n+1
pH 8.0, 80°C
0.011
NADPH
pH 8.0, 80°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q8U194: subunit beta (sudB, SuDH I)
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
NADPH-dependent S0 reduction by SuDH I and SuDH II may be a mechanism to compensate for the reduction of S0 in the absence of NADPH:sulfur oxidoreductase (NSR)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
1 * 52000 + 1 * 29000,
30686
1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
52000
1 * 52000 + 1 * 29000,
52598
1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
90000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
82
the enzyme shows a 50% increase in activity after 12 h
95
half-life: 12 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
following sulfur (S0) addition in deletion mutant MBX1 (deletion in membrane-bound oxidoreductase complex, MBX) the expression of the gene encoding sulfide dehydrogenase SuDH I (sudB) is increased 2fold, campared to 10fold increase in the parent strain
following sulfur (S0) addition in deletion mutant NSR1 (deletion in NADPH:sulfur oxidoreductase, NSR) the expression of the gene encoding sulfide dehydrogenase SuDH I (sudB) is decreased to a lesser extent (5fold less) compared to the parent strain
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ma, K.; Adams, M.W.
Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur
J. Bacteriol.
176
6509-6517
1994
Pyrococcus furiosus (Q8U195 and Q8U194), Pyrococcus furiosus
Manually annotated by BRENDA team
Bridger, S.L.; Clarkson, S.M.; Stirrett, K.; DeBarry, M.B.; Lipscomb, G.L.; Schut, G.J.; Westpheling, J.; Scott, R.A.; Adams, M.W.
Deletion strains reveal metabolic roles for key elemental sulfur-responsive proteins in Pyrococcus furiosus
J. Bacteriol.
193
6498-6504
2011
Pyrococcus furiosus (Q8U194), Pyrococcus furiosus
Manually annotated by BRENDA team
Hagen, W.R.; Silva, P.J.; Amorim, M.A.; Hagedoorn, P.L.; Wassink, H.; Haaker, H.; Robb, F.T.
Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands
J. Biol. Inorg. Chem.
5
527-534
2000
Pyrococcus furiosus (Q8U195 and Q8U194), Pyrococcus furiosus
Manually annotated by BRENDA team