EC Number | Cloned (Comment) | Organism |
---|---|---|
1.8.5.4 | expressed in Escherichia coli | Caldivirga maquilingensis |
1.8.5.4 | expression in Escherichia coli | Caldivirga maquilingensis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.8.5.4 | L379D | all of the expressed protein is membrane-bound, the mutant enzyme is inactive | Caldivirga maquilingensis |
1.8.5.4 | L379D | inactive mutant enzyme, all of the expressed protein is membrane-bound | Caldivirga maquilingensis |
1.8.5.4 | L379D/M380N | both the membrane-bound and soluble forms of this protein are inactive | Caldivirga maquilingensis |
1.8.5.4 | L379D/M380N | the mutant protein is found in both the cytoplasmic and membrane fractions in equal proportions after disruption of the Escherichia coli cells, and each fraction has the same FAD content as the membrane bound wild type enzyme (about 50%) | Caldivirga maquilingensis |
1.8.5.4 | L379N | all of the expressed protein is membrane-bound, the mutant enzyme is inactive | Caldivirga maquilingensis |
1.8.5.4 | L379N | the mutant enzyme is inactive due to a perturbation of the decylubiquinone binding site | Caldivirga maquilingensis |
1.8.5.4 | M380N | mutation results in protein that is entirely membrane-bound, but which has the same activity as wild type enzyme | Caldivirga maquilingensis |
1.8.5.4 | M380N | this is one of the two mutations in the L379D/M380N double mutant. The M380N mutation by itself results in protein that is entirely membrane-bound, but which has the same activity as wild type enzyme | Caldivirga maquilingensis |
1.8.5.4 | additional information | in the truncation mutant SQRT1 a stop codon is introduced to eliminate the last 21 amino acids from the C-terminus, removing one putative amphiphilic helix. In construct SQRT2, the last 45 amino acids are removed, thus eliminating both of the amphiphilic helices. Both SQRT1 and SQRT2 when expressed in Escherichia coli result in water-soluble proteins. In each case the yield of protein is nearly 5-fold higher than the wild type construct, in which the recombinant protein is bound to the membrane. The FAD content of each of the truncated proteins, as well as the characteristics of the absorption spectra, is identical to those of the detergent-solubilized, wild type enzyme. No sulfide:decylubiquinone oxidoreductase activity is observed in either case | Caldivirga maquilingensis |
1.8.5.4 | Y383Q/F384K | both the soluble and membrane-bound versions of this double-mutant are catalytically active. The membrane-bound mutant enzyme has a specific activity about 30% higher than the wild type enzyme and the Km for sulfide is about half of the value found for the wild type enzyme. The water-soluble version of this mutant enzyme is twice as active as the wild type enzyme and the Km values for both sulfide and decylubiquinone are about the same as the wild type, membrane-bound form | Caldivirga maquilingensis |
1.8.5.4 | Y383Q/F384K | this mutant protein is expressed in a yield similar to the wild type enzyme and is found equally in the cytoplasmic and membrane fractions after cell disruption. The isolated proteins from each fraction contain FAD to the same extent as the wild type enzyme. Both the soluble and membrane bound versions of this double-mutant are catalytically active. The membrane-bound mutant enzyme has a specific activity about 30% higher than the wild type enzyme and the Km for sulfide is about half of the value found for the wild type (0.046 mM vs.0.077 mM). The water-soluble version of this mutant enzyme is twice as active as the wild type SQR (1.20 vs. 0.60 nmol quinone reduced/s* nM FAD) and the Km values for both sulfide and decylubiquinone are about the same as the wild type, membrane-bound form | Caldivirga maquilingensis |
1.8.5.4 | Y383Q/F384K/L379D/M380N | the mutant protein is found entirely in the cytoplasmic fraction but there is no catalytic activity | Caldivirga maquilingensis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.8.5.4 | aurachin C | 250 nM, complete inhibition | Caldivirga maquilingensis | |
1.8.5.4 | iodoacetamide | 0.3 mM, complete inhibition | Caldivirga maquilingensis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.8.5.4 | 0.03 | - |
decylubiquinone | pH 7.5, 60°C, wild-type enzyme | Caldivirga maquilingensis | |
1.8.5.4 | 0.03 | - |
decylubiquinone | pH 7.5, 60°C, membrane-bound wild-type enzyme | Caldivirga maquilingensis | |
1.8.5.4 | 0.032 | - |
decylubiquinone | pH 7.5, 60°C, membrane-bound mutant enzyme M380N | Caldivirga maquilingensis | |
1.8.5.4 | 0.033 | - |
decylubiquinone | pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K | Caldivirga maquilingensis | |
1.8.5.4 | 0.036 | - |
decylubiquinone | pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K | Caldivirga maquilingensis | |
1.8.5.4 | 0.046 | - |
Sulfide | pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K | Caldivirga maquilingensis | |
1.8.5.4 | 0.073 | - |
Sulfide | pH 7.5, 60°C, membrane-bound mutant enzyme M380N | Caldivirga maquilingensis | |
1.8.5.4 | 0.077 | - |
Sulfide | pH 7.5, 60°C, wild-type enzyme | Caldivirga maquilingensis | |
1.8.5.4 | 0.077 | - |
Sulfide | pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K | Caldivirga maquilingensis | |
1.8.5.4 | 0.077 | - |
Sulfide | pH 7.5, 60°C, membrane-bound wild-type enzyme | Caldivirga maquilingensis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.8.5.4 | membrane | the C-terminal amphiphilic helix is important for membrane binding | Caldivirga maquilingensis | 16020 | - |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.8.5.4 | 45000 | - |
x * 45000, SDS-PAGE | Caldivirga maquilingensis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.5.4 | Caldivirga maquilingensis | - |
- |
- |
1.8.5.4 | Caldivirga maquilingensis IC-167 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.8.5.4 | - |
Caldivirga maquilingensis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.5.4 | sulfide + decylubiquinone | - |
Caldivirga maquilingensis | polysulfide + decylubiquinol | - |
? | |
1.8.5.4 | sulfide + decylubiquinone | - |
Caldivirga maquilingensis IC-167 | polysulfide + decylubiquinol | - |
? | |
1.8.5.4 | sulfide + decylubiquinone | - |
Caldivirga maquilingensis | sulfur + decylubiquinol | - |
? | |
1.8.5.4 | sulfide + decylubiquinone | - |
Caldivirga maquilingensis IC-167 | sulfur + decylubiquinol | - |
? | |
1.8.5.4 | sulfide + duroquinone | 23% compared to the activity with decylubiquinone | Caldivirga maquilingensis | sulfur + duroquinol | - |
? | |
1.8.5.4 | sulfide + duroquinone | 23% compared to the activity with decylubiquinone | Caldivirga maquilingensis IC-167 | sulfur + duroquinol | - |
? | |
1.8.5.4 | sulfide + duroquinone 23 | % compared to the activity with decylubiquinone | Caldivirga maquilingensis | sulfur + duroquinol 23 | - |
? | |
1.8.5.4 | sulfide + menadione | 25% compared to the activity with decylubiquinone | Caldivirga maquilingensis | sulfur + menadiol | - |
? | |
1.8.5.4 | sulfide + menadione | 25% compared to the activity with decylubiquinone | Caldivirga maquilingensis IC-167 | sulfur + menadiol | - |
? | |
1.8.5.4 | sulfide + menadione | 25% compared to the activity with decylubiquinone | Caldivirga maquilingensis | polysulfide + menadiol | - |
? | |
1.8.5.4 | sulfide + ubiquinone-1 | 15% compared to the activity with decylubiquinone | Caldivirga maquilingensis | sulfur + ubiquinol-1 | - |
? | |
1.8.5.4 | sulfide + ubiquinone-1 | 15% compared to the activity with decylubiquinone | Caldivirga maquilingensis IC-167 | sulfur + ubiquinol-1 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.8.5.4 | ? | x * 45000, SDS-PAGE | Caldivirga maquilingensis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.8.5.4 | SQR | - |
Caldivirga maquilingensis |
1.8.5.4 | sulfide:decylubiquinone oxidoreductase | - |
Caldivirga maquilingensis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.8.5.4 | 60 | - |
assay at | Caldivirga maquilingensis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.8.5.4 | 0.6 | - |
Sulfide | pH 7.5, 60°C, membrane-bound wild-type enzyme | Caldivirga maquilingensis | |
1.8.5.4 | 0.6 | - |
decylubiquinone | pH 7.5, 60°C, membrane-bound wild-type enzyme | Caldivirga maquilingensis | |
1.8.5.4 | 0.62 | - |
Sulfide | pH 7.5, 60°C, membrane-bound mutant enzyme M380N | Caldivirga maquilingensis | |
1.8.5.4 | 0.62 | - |
decylubiquinone | pH 7.5, 60°C, membrane-bound mutant enzyme M380N | Caldivirga maquilingensis | |
1.8.5.4 | 0.82 | - |
Sulfide | pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K | Caldivirga maquilingensis | |
1.8.5.4 | 0.82 | - |
decylubiquinone | pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K | Caldivirga maquilingensis | |
1.8.5.4 | 1.2 | - |
Sulfide | pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K | Caldivirga maquilingensis | |
1.8.5.4 | 1.2 | - |
decylubiquinone | pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K | Caldivirga maquilingensis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.8.5.4 | 7.5 | - |
assay at | Caldivirga maquilingensis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.8.5.4 | FAD | FAD is not covalently bound to the protein. Activity is not increased by the addition of FAD (0.020 mM) to the assay buffer | Caldivirga maquilingensis | |
1.8.5.4 | FAD | is not covalently bound to the protein, the cofactor is in an apolar environment, one equivalent of FAD per sulfide:quinone xidoreductase polypeptide | Caldivirga maquilingensis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.8.5.4 | physiological function | sulfide:quinone oxidoreductases are ubiquitous enzymes which have multiple roles: sulfide detoxification, energy generation by providing electrons to respiratory or photosynthetic electron transfer chains, and sulfide homeostasis | Caldivirga maquilingensis |