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Literature summary extracted from

  • Schut, G.J.; Bridger, S.L.; Adams, M.W.
    Insights into the metabolism of elemental sulfur by the hyperthermophilic archaeon Pyrococcus furiosus: characterization of a coenzyme A-dependent NAD(P)H sulfur oxidoreductase (2007), J. Bacteriol., 189, 4431-4441.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.18 expression in Escherichia coli with an N-terminal His-tag Pyrococcus furiosus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.18 0.01
-
 NADH pH 7.0, 85°C Pyrococcus furiosus
1.8.1.18 0.018
-
 NADPH pH 7.0, 85°C Pyrococcus furiosus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.1.18 cytosol
-
 Pyrococcus furiosus 5829
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.1.18 48720
-
 2 * 48720, mass spectrometry Pyrococcus furiosus
1.8.1.18 50000
-
 2 * 50000, SDS-PAGE Pyrococcus furiosus
1.8.1.18 100000
-
 gel filtration Pyrococcus furiosus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.1.18 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

EC Number Organism UniProt Comment Textmining
1.8.1.18 Pyrococcus furiosus Q8U1M0
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.8.1.18 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)

EC Number Purification (Comment) Organism
1.8.1.18 more than 140fold Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.18 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 Pyrococcus furiosus ?
-
 ?
1.8.1.18 polysulfide(n) + NADPH + H+
-
 Pyrococcus furiosus hydrogen sulfide + polysulfide(n-1) + NADP+
-
 ?
1.8.1.18 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 Pyrococcus furiosus hydrogen sulfide + NAD(P)+
-
 ?
1.8.1.18 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) Pyrococcus furiosus hydrogen sulfide + NAD+
-
 ?
1.8.1.18 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) Pyrococcus furiosus hydrogen sulfide + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.1.18 homodimer 2 * 50000, SDS-PAGE Pyrococcus furiosus
1.8.1.18 homodimer 2 * 48720, mass spectrometry Pyrococcus furiosus

Synonyms

EC Number Synonyms Comment Organism
1.8.1.18 NADPH NSR
-
 Pyrococcus furiosus
1.8.1.18 PF1186
-
 Pyrococcus furiosus
1.8.1.18 S(0) reductase
-
 Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.1.18 85
-
 assay at Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.18 6.5
-
 sulfide production Pyrococcus furiosus
1.8.1.18 7
-
 assay at Pyrococcus furiosus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.18 CoA the activity is dependent on CoA, Km: 8.5 mM Pyrococcus furiosus
1.8.1.18 FAD PF1186 is a member of a large family of flavin adenine dinucleotide (FAD)-dependent pyridine nucleotide-disulfide oxidoreductase genes Pyrococcus furiosus
1.8.1.18 NADH activity with NADH is 50% compared to the activity with NADPH Pyrococcus furiosus
1.8.1.18 NADPH activity with NADH is 50% compared to the activity with NADPH Pyrococcus furiosus

Expression

EC Number Organism Comment Expression
1.8.1.18 Pyrococcus furiosus up-regulated within 10 min after the addition of elemental sulfur up