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Literature summary 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

Activating Compound

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.18 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
1.13.11.18 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

EC Number Protein Variants Comment Organism
1.13.11.18 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

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

Metals/Ions

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

Organism

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.13.11.18 1484
-
 purified recombinant enzyme, pH 6.5, 35°C Acidithiobacillus ferrooxidans
1.13.11.18 2336
-
 purified recombinant enzyme, pH 8.0, 45°C Acidithiobacillus caldus

Subunits

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.18 35
-
-
 Acidithiobacillus ferrooxidans
1.13.11.18 45 55
-
 Acidithiobacillus caldus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.13.11.18 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.18 7.6
-
-
 Acidithiobacillus ferrooxidans
1.13.11.18 8
-
-
 Acidithiobacillus caldus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.13.11.18 6.5 9.6 activity range, recombinant enzyme Acidithiobacillus ferrooxidans
1.13.11.18 7.6 8.6 activity range, recombinant enzyme Acidithiobacillus caldus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.13.11.18 Acidithiobacillus ferrooxidans sequence calculation
-
 5.43

General Information

EC Number General Information Comment Organism
1.13.11.18 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