Information on EC 1.8.1.19 - sulfide dehydrogenase

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The expected taxonomic range for this enzyme is: Pyrococcus furiosus

EC NUMBER
COMMENTARY hide
1.8.1.19
-
RECOMMENDED NAME
GeneOntology No.
sulfide dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrogen sulfide + (sulfide)n + NADP+ = (sulfide)n+1 + NADPH + H+
show the reaction diagram
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-
-
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
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)
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
Q8U195 and Q8U194
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
Q8U195 and Q8U194
the relative activity is about 40% compared to the activity with polysulfide
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-
?
additional information
?
-
Q8U195 and Q8U194
the enzyme also catalyzes ferredoxin:NADP+ reductase activity
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-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Q8U195 and Q8U194
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
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both the alpha-subunit and the beta-subunit contains one FAD
Fe-S center
flavin
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enzyme contains flavin
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme contains no metal
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.25
(sulfide)n+1
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pH 8.0, 80°C
0.011
NADPH
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pH 8.0, 80°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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pH 8.0, 80°C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
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1 * 52000 + 1 * 29000,
30686
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1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
52000
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1 * 52000 + 1 * 29000,
52598
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1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
90000
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gel filtration
SUBUNITS
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
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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