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Literature summary for 1.8.1.18 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
Search for more literature for 1.8.1.18

Cloned(Commentary)

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

KM Value [mM]

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

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment 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)

Purification (Comment) Organism
more than 140fold Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
polysulfide(n) + NADPH + H+
-
 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 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) 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) Pyrococcus furiosus hydrogen sulfide + NADP+
-
 ?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment 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

Expression

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