EC Number | Cloned (Comment) | Organism |
---|---|---|
1.8.1.18 | expression in Escherichia coli with an N-terminal His-tag | Pyrococcus furiosus |
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 |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.8.1.18 | cytosol | - |
Pyrococcus furiosus | 5829 | - |
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 |
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)+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.1.18 | Pyrococcus furiosus | Q8U1M0 | - |
- |
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 |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.8.1.18 | more than 140fold | Pyrococcus furiosus |
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+ | - |
? |
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 |
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 |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.8.1.18 | 85 | - |
assay at | Pyrococcus furiosus |
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 |
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 |
EC Number | Organism | Comment | Expression |
---|---|---|---|
1.8.1.18 | Pyrococcus furiosus | up-regulated within 10 min after the addition of elemental sulfur | up |