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Literature summary for 1.13.11.18 extracted from

  • Wang, H.; Liu, S.; Liu, X.; Li, X.; Wen, Q.; Lin, J.
    Identification and characterization of an ETHE1-like sulfur dioxygenase in extremely acidophilic Acidithiobacillus spp (2014), Appl. Microbiol. Biotechnol., 98, 7511-7522 .
    View publication on PubMed
Search for more literature for 1.13.11.18

Activating Compound

Activating Compound Comment Organism Structure
DTT 9% activation at 1 mM Acidithiobacillus ferrooxidans

Cloned(Commentary)

Cloned (Comment) Organism
gene sdo, DNA and amino acid sequence determination and analysis, quantitative RT-PCR expression analysis, recombinant overexpression in Escherichia coli strain BL21(DE3) Acidithiobacillus ferrooxidans
gene sdo, DNA and amino acid sequence determination and analysis, quantitative RT-PCR expression analysis, recombinant overexpression in Escherichia coli strain BL21(DE3) Acidithiobacillus caldus

Protein Variants

Protein Variants Comment Organism
additional information construction of an sdo knockout mutant and an sdo overexpression strain from Acidithiobacillus ferrooxidans strain ATCC 23270. By overexpressing sdo in strain ATCC 23270, a 91fold increased sdo transcriptional level and a 2.5fold increase in SDO activity are observed when sulfur S0 is used as sole energy source. The sdo knockout mutant of displays a slightly reduced growth capacity in S0-medium compared with the wild type but still maintains high S0-oxidizing activity, suggesting that there is at least one other S0-oxidizing enzyme besides SDO in Acidithiobacillus ferrooxidans ATCC 23270 cells Acidithiobacillus ferrooxidans

Inhibitors

Inhibitors Comment Organism Structure
Co2+ complete inhibition at 1 mM Acidithiobacillus caldus
Co2+ complete inhibition at 1 mM Acidithiobacillus ferrooxidans
Cu2+ complete inhibition at 1 mM Acidithiobacillus caldus
Cu2+ almost complete inhibition at 1 mM Acidithiobacillus ferrooxidans
DTT 23% inhibition at 1 mM Acidithiobacillus caldus
EDTA 96.6% inhibition at 1 mM Acidithiobacillus caldus
EDTA 84.5% inhibition at 1.0 mM Acidithiobacillus ferrooxidans
Fe2+ 84% inhibition at 1 mM Acidithiobacillus caldus
Fe2+ 84% inhibition at 1 mM Acidithiobacillus ferrooxidans
Fe3+ 79% inhibition at 1 mM Acidithiobacillus caldus
Fe3+ 65% inhibition at 1 mM Acidithiobacillus ferrooxidans
Hg2+ complete inhibition at 1 mM Acidithiobacillus caldus
Hg2+ complete inhibition at 1 mM Acidithiobacillus ferrooxidans
Mg2+ 4% inhibition at 1 mM Acidithiobacillus caldus
Mg2+ 23% inhibition at 1 mM Acidithiobacillus ferrooxidans
Mn2+ 55% inhibition at 1 mM Acidithiobacillus caldus
Mn2+ 61% inhibition at 1 mM Acidithiobacillus ferrooxidans
NEM almost complete inhibition at 1 mM Acidithiobacillus caldus
NEM almost complete inhibition at 1 mM Acidithiobacillus ferrooxidans
Ni2+ complete inhibition at 1 mM Acidithiobacillus caldus
Ni2+ almost complete inhibition at 1 mM Acidithiobacillus ferrooxidans
Zn2+ complete inhibition at 1 mM Acidithiobacillus caldus
Zn2+ almost complete inhibition at 1 mM Acidithiobacillus ferrooxidans

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the eukaryotic mitochondrial sulfur dioxygenases metal II binding site is conserved but no metal binding is observed Acidithiobacillus ferrooxidans
additional information the eukaryotic mitochondrial sulfur dioxygenases metal II binding site is conserved but no metal binding is observed Acidithiobacillus caldus

Organism

Organism UniProt Comment Textmining
Acidithiobacillus caldus A0A1E7YQH3
-
-
Acidithiobacillus caldus MTH-04 A0A1E7YQH3
-
-
Acidithiobacillus ferrooxidans B7J413
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1484
-
 purified recombinant enzyme, pH 6.5, 35°C Acidithiobacillus ferrooxidans
2336
-
 purified recombinant enzyme, pH 8.0, 45°C Acidithiobacillus caldus

Subunits

Subunits Comment Organism
? x * 25120, sequence calculation Acidithiobacillus ferrooxidans

Synonyms

Synonyms Comment Organism
AFE_0269
-
 Acidithiobacillus ferrooxidans
BAE27_01805
-
 Acidithiobacillus caldus
ETHE1-like sulfur dioxygenase
-
 Acidithiobacillus ferrooxidans
ETHE1-like sulfur dioxygenase
-
 Acidithiobacillus caldus
SDO
-
 Acidithiobacillus ferrooxidans
SDO
-
 Acidithiobacillus caldus
sulfur dioxygenase
-
 Acidithiobacillus ferrooxidans
sulfur dioxygenase
-
 Acidithiobacillus caldus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
 Acidithiobacillus ferrooxidans
45 55
-
 Acidithiobacillus caldus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 37 optimal activity at 35°C, more than 88%of its maximum activity between 20°C and 37°C. Very limited SDO activity is detected at 50°C or above Acidithiobacillus ferrooxidans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
-
 Acidithiobacillus ferrooxidans
8
-
-
 Acidithiobacillus caldus

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9.6 activity range, recombinant enzyme Acidithiobacillus ferrooxidans
7.6 8.6 activity range, recombinant enzyme Acidithiobacillus caldus

pI Value

Organism Comment pI Value Maximum pI Value
Acidithiobacillus ferrooxidans sequence calculation
-
 5.43

General Information

General Information Comment Organism
malfunction by overexpressing sdo in strain ATCC 23270, a 91fold increased sdo transcriptional level and a 2.5fold increase in SDO activity are observed when sulfur S0 is used as sole energy source. The sdo knockout mutant displays a slightly reduced growth capacity in S0-medium compared with the wild type but still maintains high S0-oxidizing activity, suggesting that there is at least one other S0-oxidizing enzyme besides SDO in Acidithiobacillus ferrooxidans ATCC 23270 cells Acidithiobacillus ferrooxidans