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Literature summary extracted from

  • Lencina, A.M.; Ding, Z.; Schurig-Briccio, L.A.; Gennis, R.B.
    Characterization of the type III sulfide:quinone oxidoreductase from Caldivirga maquilingensis and its membrane binding (2013), Biochim. Biophys. Acta, 1827, 266-275.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Localization

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
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.5.4 45000
-
 x * 45000, SDS-PAGE Caldivirga maquilingensis

Organism

EC Number Organism UniProt Comment Textmining
1.8.5.4 Caldivirga maquilingensis
-
-
-
1.8.5.4 Caldivirga maquilingensis IC-167
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.5.4
-
 Caldivirga maquilingensis

Substrates and Products (Substrate)

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
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.5.4 ? x * 45000, SDS-PAGE Caldivirga maquilingensis

Synonyms

EC Number Synonyms Comment Organism
1.8.5.4 SQR
-
 Caldivirga maquilingensis
1.8.5.4 sulfide:decylubiquinone oxidoreductase
-
 Caldivirga maquilingensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.5.4 60
-
 assay at Caldivirga maquilingensis

Turnover Number [1/s]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.5.4 7.5
-
 assay at Caldivirga maquilingensis

Cofactor

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

General Information

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