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show all sequences of 1.8.1.18

Insights into the metabolism of elemental sulfur by the hyperthermophilic archaeon Pyrococcus furiosus: characterization of a coenzyme A-dependent NAD(P)H sulfur oxidoreductase

Schut, G.J.; Bridger, S.L.; Adams, M.W.; J. Bacteriol. 189, 4431-4441 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli with an N-terminal His-tag
Pyrococcus furiosus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
NADH
pH 7.0, 85°C
Pyrococcus furiosus
0.018
-
NADPH
pH 7.0, 85°C
Pyrococcus furiosus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Pyrococcus furiosus
5829
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
48720
-
2 * 48720, mass spectrometry
Pyrococcus furiosus
50000
-
2 * 50000, SDS-PAGE
Pyrococcus furiosus
100000
-
gel filtration
Pyrococcus furiosus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sulfur + NAD(P)H + H+
Pyrococcus furiosus
the rate of sulfide production from colloidal sulfur is linear (up to 10 min) suggesting that this is the true substrate for the enzyme. A lag phase in sulfide production would be expected if polysulfide, which is generated by the reaction of sulfide with elemental sulfur, is the natural substrate. A less-than-twofold increase in activity is observed, both at pH 7.0 and at pH 9.0, when polysulfide (11 mM) is used as the substrate compared to when elemental sulfur (6.4 g/liter) is used. Polysulfide is stable at pH 8 and readily dissociates to colloidal sulfur and sulfide at neutral pH. A much greater stimulation of activity would be observed if polysulfide is the preferred substrate, particularly at the higher pH
hydrogen sulfide + NAD(P)+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus furiosus
Q8U1M0
-
-
Oxidation Stability
Oxidation Stability
Organism
neither the native nor recombinant enzymes are oxygen sensitive, no loss of activity after exposure to air for 16 h at 23°C
Pyrococcus furiosus
Purification (Commentary)
Commentary
Organism
more than 140fold
Pyrococcus furiosus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
PF1186 is formerly proposed to function as a NAD(P)H-dependent CoA-S-S-CoA reductase (CoADR) gene (EC 1.8.1.14). The specific activity for CoA-S-S-CoA reduction (0.006 mol CoA-S-S-CoA reduced/min/mg) is about 20fold lower than the activity that this enzyme exhibits in the S(0) reduction assay. The formeryly reported CoADR activity represents only a partial reaction of its true physiological function, which is now proposed to be CoA-dependent S(0) reduction
722519
Pyrococcus furiosus
?
-
-
-
-
polysulfide(n) + NADPH + H+
-
722519
Pyrococcus furiosus
hydrogen sulfide + polysulfide(n-1) + NADP+
-
-
-
?
sulfur + NAD(P)H + H+
the rate of sulfide production from colloidal sulfur is linear (up to 10 min) suggesting that this is the true substrate for the enzyme. A lag phase in sulfide production would be expected if polysulfide, which is generated by the reaction of sulfide with elemental sulfur, is the natural substrate. A less-than-twofold increase in activity is observed, both at pH 7.0 and at pH 9.0, when polysulfide (11 mM) is used as the substrate compared to when elemental sulfur (6.4 g/liter) is used. Polysulfide is stable at pH 8 and readily dissociates to colloidal sulfur and sulfide at neutral pH. A much greater stimulation of activity would be observed if polysulfide is the preferred substrate, particularly at the higher pH
722519
Pyrococcus furiosus
hydrogen sulfide + NAD(P)+
-
-
-
?
sulfur + NADH + H+
colloidal sulfur generated from polysulfide is a better substrate than the elemental sulfur. The sulfur reductase activity requires anaerobic conditions (the product sulfide is oxidized by oxygen)
722519
Pyrococcus furiosus
hydrogen sulfide + NAD+
-
-
-
?
sulfur + NADPH + H+
colloidal sulfur generated from polysulfide is a better substrate than the elemental sulfur. The sulfur reductase activity requires anaerobic conditions (the product sulfide is oxidized by oxygen)
722519
Pyrococcus furiosus
hydrogen sulfide + NADP+
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 48720, mass spectrometry; 2 * 50000, SDS-PAGE
Pyrococcus furiosus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
85
-
assay at
Pyrococcus furiosus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
sulfide production
Pyrococcus furiosus
7
-
assay at
Pyrococcus furiosus
Cofactor
Cofactor
Commentary
Organism
Structure
CoA
the activity is dependent on CoA, Km: 8.5 mM
Pyrococcus furiosus
FAD
PF1186 is a member of a large family of flavin adenine dinucleotide (FAD)-dependent pyridine nucleotide-disulfide oxidoreductase genes
Pyrococcus furiosus
NADH
activity with NADH is 50% compared to the activity with NADPH
Pyrococcus furiosus
NADPH
activity with NADH is 50% compared to the activity with NADPH
Pyrococcus furiosus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli with an N-terminal His-tag
Pyrococcus furiosus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
CoA
the activity is dependent on CoA, Km: 8.5 mM
Pyrococcus furiosus
FAD
PF1186 is a member of a large family of flavin adenine dinucleotide (FAD)-dependent pyridine nucleotide-disulfide oxidoreductase genes
Pyrococcus furiosus
NADH
activity with NADH is 50% compared to the activity with NADPH
Pyrococcus furiosus
NADPH
activity with NADH is 50% compared to the activity with NADPH
Pyrococcus furiosus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
NADH
pH 7.0, 85°C
Pyrococcus furiosus
0.018
-
NADPH
pH 7.0, 85°C
Pyrococcus furiosus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Pyrococcus furiosus
5829
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
48720
-
2 * 48720, mass spectrometry
Pyrococcus furiosus
50000
-
2 * 50000, SDS-PAGE
Pyrococcus furiosus
100000
-
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
sulfur + NAD(P)H + H+
Pyrococcus furiosus
the rate of sulfide production from colloidal sulfur is linear (up to 10 min) suggesting that this is the true substrate for the enzyme. A lag phase in sulfide production would be expected if polysulfide, which is generated by the reaction of sulfide with elemental sulfur, is the natural substrate. A less-than-twofold increase in activity is observed, both at pH 7.0 and at pH 9.0, when polysulfide (11 mM) is used as the substrate compared to when elemental sulfur (6.4 g/liter) is used. Polysulfide is stable at pH 8 and readily dissociates to colloidal sulfur and sulfide at neutral pH. A much greater stimulation of activity would be observed if polysulfide is the preferred substrate, particularly at the higher pH
hydrogen sulfide + NAD(P)+
-
-
?
Oxidation Stability (protein specific)
Oxidation Stability
Organism
neither the native nor recombinant enzymes are oxygen sensitive, no loss of activity after exposure to air for 16 h at 23°C
Pyrococcus furiosus
Purification (Commentary) (protein specific)
Commentary
Organism
more than 140fold
Pyrococcus furiosus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
PF1186 is formerly proposed to function as a NAD(P)H-dependent CoA-S-S-CoA reductase (CoADR) gene (EC 1.8.1.14). The specific activity for CoA-S-S-CoA reduction (0.006 mol CoA-S-S-CoA reduced/min/mg) is about 20fold lower than the activity that this enzyme exhibits in the S(0) reduction assay. The formeryly reported CoADR activity represents only a partial reaction of its true physiological function, which is now proposed to be CoA-dependent S(0) reduction
722519
Pyrococcus furiosus
?
-
-
-
-
polysulfide(n) + NADPH + H+
-
722519
Pyrococcus furiosus
hydrogen sulfide + polysulfide(n-1) + NADP+
-
-
-
?
sulfur + NAD(P)H + H+
the rate of sulfide production from colloidal sulfur is linear (up to 10 min) suggesting that this is the true substrate for the enzyme. A lag phase in sulfide production would be expected if polysulfide, which is generated by the reaction of sulfide with elemental sulfur, is the natural substrate. A less-than-twofold increase in activity is observed, both at pH 7.0 and at pH 9.0, when polysulfide (11 mM) is used as the substrate compared to when elemental sulfur (6.4 g/liter) is used. Polysulfide is stable at pH 8 and readily dissociates to colloidal sulfur and sulfide at neutral pH. A much greater stimulation of activity would be observed if polysulfide is the preferred substrate, particularly at the higher pH
722519
Pyrococcus furiosus
hydrogen sulfide + NAD(P)+
-
-
-
?
sulfur + NADH + H+
colloidal sulfur generated from polysulfide is a better substrate than the elemental sulfur. The sulfur reductase activity requires anaerobic conditions (the product sulfide is oxidized by oxygen)
722519
Pyrococcus furiosus
hydrogen sulfide + NAD+
-
-
-
?
sulfur + NADPH + H+
colloidal sulfur generated from polysulfide is a better substrate than the elemental sulfur. The sulfur reductase activity requires anaerobic conditions (the product sulfide is oxidized by oxygen)
722519
Pyrococcus furiosus
hydrogen sulfide + NADP+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 48720, mass spectrometry; 2 * 50000, SDS-PAGE
Pyrococcus furiosus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
85
-
assay at
Pyrococcus furiosus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
sulfide production
Pyrococcus furiosus
7
-
assay at
Pyrococcus furiosus
Expression
Organism
Commentary
Expression
Pyrococcus furiosus
up-regulated within 10 min after the addition of elemental sulfur
up
Expression (protein specific)
Organism
Commentary
Expression
Pyrococcus furiosus
up-regulated within 10 min after the addition of elemental sulfur
up
Other publictions for EC 1.8.1.18
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)
727447
Harnvoravongchai
Characterization and gene dele ...
Thermococcus kodakarensis
Extremophiles
18
603-616
2014
1
-
1
-
-
-
-
-
-
-
3
1
-
4
-
-
1
-
-
-
2
-
3
2
1
-
-
-
1
-
-
3
-
-
-
2
-
2
5
-
-
-
-
-
-
-
-
-
3
1
-
-
-
2
-
-
2
-
3
2
2
-
-
-
2
-
-
-
-
-
-
-
-
-
722535
Bridger
Deletion strains reveal metabo ...
Pyrococcus furiosus
J. Bacteriol.
193
6498-6504
2011
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
723210
Lipscomb
SurR: a transcriptional activa ...
Pyrococcus furiosus
Mol. Microbiol.
71
332-349
2009
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
727547
Toth
A novel NADPH-dependent oxidor ...
Thermococcus litoralis, Thermococcus litoralis DSM 5473
FEMS Microbiol. Lett.
282
8-14
2008
-
-
1
-
-
-
-
2
-
-
-
-
-
2
-
-
1
-
-
-
1
-
2
-
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
1
-
-
1
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
722519
Schut
Insights into the metabolism o ...
Pyrococcus furiosus
J. Bacteriol.
189
4431-4441
2007
-
-
1
-
-
-
-
2
1
-
3
1
-
6
1
-
1
-
-
-
-
-
5
1
1
-
-
-
2
-
-
4
-
-
-
-
-
1
4
-
-
-
-
-
-
2
1
-
3
1
-
1
-
1
-
-
-
-
5
1
1
-
-
-
2
-
-
-
1
-
-
1
-
-