BRENDA - Enzyme Database
show all sequences of 1.8.1.19

Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur

Ma, K.; Adams, M.W.; J. Bacteriol. 176, 6509-6517 (1994)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.011
-
NADPH
pH 8.0, 80°C
Pyrococcus furiosus
1.25
-
(sulfide)n+1
pH 8.0, 80°C
Pyrococcus furiosus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Pyrococcus furiosus
5737
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
enzyme contains no metal
Pyrococcus furiosus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29000
-
1 * 52000 + 1 * 29000,
Pyrococcus furiosus
52000
-
1 * 52000 + 1 * 29000,
Pyrococcus furiosus
90000
-
gel filtration
Pyrococcus furiosus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(sulfide)n+1 + NADPH + H+
Pyrococcus furiosus
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
hydrogen sulfide + (sulfide)n + NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus furiosus
Q8U195 and Q8U194
Q8U195: subunit alpha, and Q8U194: subunit beta
-
Purification (Commentary)
Commentary
Organism
-
Pyrococcus furiosus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
7
-
pH 8.0, 80°C
Pyrococcus furiosus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(sulfide)n+1 + NADPH + H+
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
722483
Pyrococcus furiosus
hydrogen sulfide + (sulfide)n + NADP+
-
-
-
?
colloidal sulfur + NADPH + H+
the relative activity is about 40% compared to the activity with polysulfide
722483
Pyrococcus furiosus
?
-
-
-
?
additional information
the enzyme also catalyzes ferredoxin:NADP+ reductase activity
722483
Pyrococcus furiosus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
heterodimer
1 * 52000 + 1 * 29000,
Pyrococcus furiosus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
82
-
the enzyme shows a 50% increase in activity after 12 h
Pyrococcus furiosus
95
-
half-life: 12 h
Pyrococcus furiosus
Cofactor
Cofactor
Commentary
Organism
Structure
Fe-S center
the enzyme contains approximately four iron-sulfur centers, 11 iron and 6 acid-labile sulfide atoms per mol
Pyrococcus furiosus
flavin
enzyme contains flavin
Pyrococcus furiosus
NADPH
NADH was not utilized as an electron donor for polysulfide reduction
Pyrococcus furiosus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Fe-S center
the enzyme contains approximately four iron-sulfur centers, 11 iron and 6 acid-labile sulfide atoms per mol
Pyrococcus furiosus
flavin
enzyme contains flavin
Pyrococcus furiosus
NADPH
NADH was not utilized as an electron donor for polysulfide reduction
Pyrococcus furiosus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.011
-
NADPH
pH 8.0, 80°C
Pyrococcus furiosus
1.25
-
(sulfide)n+1
pH 8.0, 80°C
Pyrococcus furiosus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Pyrococcus furiosus
5737
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
enzyme contains no metal
Pyrococcus furiosus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29000
-
1 * 52000 + 1 * 29000,
Pyrococcus furiosus
52000
-
1 * 52000 + 1 * 29000,
Pyrococcus furiosus
90000
-
gel filtration
Pyrococcus furiosus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(sulfide)n+1 + NADPH + H+
Pyrococcus furiosus
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
hydrogen sulfide + (sulfide)n + NADP+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pyrococcus furiosus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
7
-
pH 8.0, 80°C
Pyrococcus furiosus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(sulfide)n+1 + NADPH + H+
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
722483
Pyrococcus furiosus
hydrogen sulfide + (sulfide)n + NADP+
-
-
-
?
colloidal sulfur + NADPH + H+
the relative activity is about 40% compared to the activity with polysulfide
722483
Pyrococcus furiosus
?
-
-
-
?
additional information
the enzyme also catalyzes ferredoxin:NADP+ reductase activity
722483
Pyrococcus furiosus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
heterodimer
1 * 52000 + 1 * 29000,
Pyrococcus furiosus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
82
-
the enzyme shows a 50% increase in activity after 12 h
Pyrococcus furiosus
95
-
half-life: 12 h
Pyrococcus furiosus
Other publictions for EC 1.8.1.19
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
722535
Bridger
Deletion strains reveal metabo ...
Pyrococcus furiosus
J. Bacteriol.
193
6498-6504
2011
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2
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2
1
1
2
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722825
Hagen
Novel structure and redox chem ...
Pyrococcus furiosus
J. Biol. Inorg. Chem.
5
527-534
2000
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2
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6
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1
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3
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3
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2
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1
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722483
Ma
Sulfide dehydrogenase from the ...
Pyrococcus furiosus
J. Bacteriol.
176
6509-6517
1994
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2
1
1
3
1
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4
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1
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1
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3
1
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2
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3
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3
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2
1
1
3
1
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1
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1
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3
1
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2
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