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Literature summary for 1.14.12.8 extracted from

  • Locher, H.H.; Leisinger, T.; Cook, A.M.
    4-Sulphobenzoate 3,4-dioxygenase. Purification and properties of a desulphonative two-component enzyme system from Comamonas testosteroni T-2 (1991), Biochem. J., 274, 833-842.
    View publication on PubMedView publication on EuropePMC

General Stability

General Stability Organism
ammonium sulfate precipitation leads to excessive loss of activity Comamonas testosteroni
chloride-buffers result in diminished yields during purification Comamonas testosteroni
glycerol, 30% v/v, stabilizes Comamonas testosteroni
repeated freezing and thawing inactivates Comamonas testosteroni

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.025 0.032 4-Sulfobenzoate
-
Comamonas testosteroni

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Comamonas testosteroni 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ requirement, iron-sulfur protein, 1 mol (2Fe-2S) per mol reductase B, one 2Fe-2S center (Rieske-type) per oxygenase A subunit, atomic absorption spectroscopy Comamonas testosteroni

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
simple multi-component dioxygenase of two, perhaps three components: reductase B coupled to dimeric oxygenase, reductase C exhibits only 15% of total activity Comamonas testosteroni
36000
-
1 * 36000, reductase B, SDS-PAGE Comamonas testosteroni
39000
-
reductase B, contains 1 mol of FMN and about 2 mol each of iron and inorganic sulfur per mol, Superose gel filtration Comamonas testosteroni
47000
-
reductase B, Sephadex G-2000 gel filtration Comamonas testosteroni
50000
-
2 * 50000, oxygenase A, SDS-PAGE Comamonas testosteroni
85000
-
oxygenase A, native dioxygenase: the enzyme is presumed to be homodimeric, Superose gel filtration Comamonas testosteroni
105000
-
oxygenase A, native dioxygenase: the enzyme is presumed to be homodimeric, Sephadex G-2000 gel filtration Comamonas testosteroni

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-sulfobenzoate + NADH + O2 Comamonas testosteroni reaction in toluene-p-sulfonate degradation pathway, simple multi-component dioxygenase of 2, perhaps 3 components: reductase B coupled to dimeric oxygenase, the third component, reductase C, represents only 15% of total activity 3,4-dihydroxybenzoate + sulfite + NAD+
-
?
4-sulfobenzoate + NADH + O2 Comamonas testosteroni T-2 reaction in toluene-p-sulfonate degradation pathway, simple multi-component dioxygenase of 2, perhaps 3 components: reductase B coupled to dimeric oxygenase, the third component, reductase C, represents only 15% of total activity 3,4-dihydroxybenzoate + sulfite + NAD+
-
?

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni
-
T-2
-
Comamonas testosteroni T-2
-
T-2
-

Purification (Commentary)

Purification (Comment) Organism
-
Comamonas testosteroni

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.11
-
reductase B Comamonas testosteroni
0.8
-
oxygenase A Comamonas testosteroni
84
-
reductase B, dichlorophenolindophenol Comamonas testosteroni
138
-
reductase B, cytochrome c Comamonas testosteroni
318
-
reductase B, ferricyanide Comamonas testosteroni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-sulfobenzoate + NADH + O2
-
Comamonas testosteroni 3,4-dihydroxybenzoate + sulfite + NAD+
-
?
4-sulfobenzoate + NADH + O2 reaction in toluene-p-sulfonate degradation pathway, simple multi-component dioxygenase of 2, perhaps 3 components: reductase B coupled to dimeric oxygenase, the third component, reductase C, represents only 15% of total activity Comamonas testosteroni 3,4-dihydroxybenzoate + sulfite + NAD+
-
?
4-sulfobenzoate + NADH + O2
-
Comamonas testosteroni T-2 3,4-dihydroxybenzoate + sulfite + NAD+
-
?
4-sulfobenzoate + NADH + O2 reaction in toluene-p-sulfonate degradation pathway, simple multi-component dioxygenase of 2, perhaps 3 components: reductase B coupled to dimeric oxygenase, the third component, reductase C, represents only 15% of total activity Comamonas testosteroni T-2 3,4-dihydroxybenzoate + sulfite + NAD+
-
?
additional information poor substrates: 2-sulfobenzoate, 3-sulfobenzoate, benzenesulfonate, 4-methylbenzenesulfonate, 4-hydroxybenzenesulfonate, 4-aminobenzenesulfonate, 4-nitrobenzenesulfonate, 4-chloro-benzenesulfonate, 4-sulfophenylacetate, 4-sulfophenylpropionate, 4-sulfophenylbutyrate, no substrates are: benzoate, 4-methylbenzoate, 4-hydroxybenzoate, 4-aminobenzoate, 4-nitrobenzoate, 4-chlorobenzoate Comamonas testosteroni ?
-
?
additional information poor substrates: 2-sulfobenzoate, 3-sulfobenzoate, benzenesulfonate, 4-methylbenzenesulfonate, 4-hydroxybenzenesulfonate, 4-aminobenzenesulfonate, 4-nitrobenzenesulfonate, 4-chloro-benzenesulfonate, 4-sulfophenylacetate, 4-sulfophenylpropionate, 4-sulfophenylbutyrate, no substrates are: benzoate, 4-methylbenzoate, 4-hydroxybenzoate, 4-aminobenzoate, 4-nitrobenzoate, 4-chlorobenzoate Comamonas testosteroni T-2 ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 50000, oxygenase A, SDS-PAGE Comamonas testosteroni
monomer 1 * 36000, reductase B, SDS-PAGE Comamonas testosteroni

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at, reductase B Comamonas testosteroni
30
-
assay at Comamonas testosteroni

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Comamonas testosteroni

Cofactor

Cofactor Comment Organism Structure
FMN flavoprotein, 1 mol FMN/mol reductase B Comamonas testosteroni
additional information no independent ferredoxin Comamonas testosteroni
NADH
-
Comamonas testosteroni