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Literature summary for 1.8.2.2 extracted from

  • Meulenberg, R.; Pronk, J.T.; Hazeu, W.; van Dijken, J.P.; Frank, J.; Bos, P.; Kuenen, J.G.
    Purification and partial characterization of thiosulfate dehydrogenase from Thiobacillus acidophilus (1993), J. Gen. Microbiol., 139, 2033-2039.
No PubMed abstract available
Search for more literature for 1.8.2.2

Inhibitors

Inhibitors Comment Organism Structure
azide 63% inhibition at 0.5 mM Acidiphilium acidophilum
EDTA not inhibitory Acidiphilium acidophilum
N-ethylmaleimide not inhibitory Acidiphilium acidophilum
Na2SeO3 39% inhibition at 0.5 mM Acidiphilium acidophilum
Na2SeO4 51% inhibition at 5 mM Acidiphilium acidophilum
p-chloromercuribenzoate 32% inhibition at 0.1 mM Acidiphilium acidophilum
SO32- 100% inhibition at 0.5 mM Acidiphilium acidophilum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.54
-
 thiosulfate at pH 7 Acidiphilium acidophilum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
20000
-
 2 * 24000 + 2 * 20000, SDS-PAGE, both subunits contain c553-type heme Acidiphilium acidophilum
24000
-
 2 * 24000 + 2 * 20000, SDS-PAGE, both subunits contain c553-type heme Acidiphilium acidophilum
102000
-
 gel filtration Acidiphilium acidophilum

Organism

Organism UniProt Comment Textmining
Acidiphilium acidophilum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using ammonium sulfate precipitation, hydrophobic interaction chromatography, anion-exchange chromatography and gel filtration Acidiphilium acidophilum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4925
-
 purified enzyme Acidiphilium acidophilum

Storage Stability

Storage Stability Organism
frozen, stable for at least 3 months Acidiphilium acidophilum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no activity with: pyrrolo-quinoline quinone, methyl- or benzyl viologen, methylthiazol tetrazolium bromide Acidiphilium acidophilum ?
-
 ?
additional information NAD+, methylene blue, 2,6-dichlorophenol indophenol Acidiphilium acidophilum ?
-
 ?
additional information no activity with: NADP+, O2 Acidiphilium acidophilum ?
-
 ?
thiosulfate + oxidized acceptor phenazine methosulfate and phenazine ethosulfate assayed in the presence of dichlorophenolindophenol and Thialhalivibrio versutus cytochrome c550 support low, but significant enzyme activities Acidiphilium acidophilum tetrathionate + reduced acceptor
-
 ?
thiosulfate + oxidized acceptor mammalian cytochrome c acts as electron acceptor Acidiphilium acidophilum tetrathionate + reduced acceptor
-
 ?
thiosulfate + oxidized acceptor Wurster's blue can also serve as electron acceptor Acidiphilium acidophilum tetrathionate + reduced acceptor
-
 ?
thiosulfate + oxidized acceptor ferricyanide is a good electron acceptor Acidiphilium acidophilum tetrathionate + reduced acceptor
-
 ?
thiosulfate + oxidized acceptor ferricyanide acts as electron acceptor Acidiphilium acidophilum tetrathionate + reduced acceptor
-
 ?

Subunits

Subunits Comment Organism
heterotetramer 2 * 24000 + 2 * 20000, SDS-PAGE, both subunits contain c553-type heme Acidiphilium acidophilum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-
-
 20% decrease of activity in 2 h and 60% decrease of activity in 7 h Acidiphilium acidophilum
30
-
 50% decrease of activity in 2 h Acidiphilium acidophilum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
8500
-
 thiosulfate at pH 7 Acidiphilium acidophilum
250000
-
 thiosulfate at least, at pH 3 Acidiphilium acidophilum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3
-
 purified enzyme Acidiphilium acidophilum

pH Stability

pH Stability pH Stability Maximum Comment Organism
2
-
 unstable below Acidiphilium acidophilum

Cofactor

Cofactor Comment Organism Structure
heme c 5.3 mole per mol of native enzyme, made up of two different c-553 hemes, present in both subunit types Acidiphilium acidophilum