BRENDA - Enzyme Database show
show all sequences of 1.13.11.55

First characterisation of the active oligomer form of sulfur oxygenase reductase from the bacterium Aquifex aeolicus

Pelletier, N.; Leroy, G.; Guiral, M.; Giudici-Orticoni, M.T.; Aubert, C.; Extremophiles 12, 205-215 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinantly expressed in Escherichia coli
Aquifex aeolicus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
contains iron atoms indispensable for the enzyme activity
Aquifex aeolicus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37674
-
16 * 37674, calculated from nucleotide sequence
Aquifex aeolicus
38000
-
16 * 38000, SDS-PAGE
Aquifex aeolicus
602000
-
nondenaturing native gel electrophoresis
Aquifex aeolicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sulfur + H2O + O2
Aquifex aeolicus
sulfur oxygenase reductase is responsible for the initial oxidation step of elemental sulfur in archaea
?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aquifex aeolicus
-
-
-
Purification (Commentary)
Commentary
Organism
wild-type and recombinant enzyme
Aquifex aeolicus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
5
-
-
Aquifex aeolicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sulfur + H2O + O2
-
686624
Aquifex aeolicus
?
-
-
-
?
sulfur + H2O + O2
sulfur oxygenase reductase is responsible for the initial oxidation step of elemental sulfur in archaea
686624
Aquifex aeolicus
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
hexadecamer
16 * 37674, calculated from nucleotide sequence; 16 * 38000, SDS-PAGE
Aquifex aeolicus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
-
Aquifex aeolicus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
45
-
Tm values are 45°C and 70°C
Aquifex aeolicus
70
-
Tm values are 45°C and 70°C
Aquifex aeolicus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.5
8
the enzyme is active from pH 5.5 to 8
Aquifex aeolicus
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinantly expressed in Escherichia coli
Aquifex aeolicus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
contains iron atoms indispensable for the enzyme activity
Aquifex aeolicus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37674
-
16 * 37674, calculated from nucleotide sequence
Aquifex aeolicus
38000
-
16 * 38000, SDS-PAGE
Aquifex aeolicus
602000
-
nondenaturing native gel electrophoresis
Aquifex aeolicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sulfur + H2O + O2
Aquifex aeolicus
sulfur oxygenase reductase is responsible for the initial oxidation step of elemental sulfur in archaea
?
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
wild-type and recombinant enzyme
Aquifex aeolicus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
5
-
-
Aquifex aeolicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sulfur + H2O + O2
-
686624
Aquifex aeolicus
?
-
-
-
?
sulfur + H2O + O2
sulfur oxygenase reductase is responsible for the initial oxidation step of elemental sulfur in archaea
686624
Aquifex aeolicus
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
hexadecamer
16 * 37674, calculated from nucleotide sequence; 16 * 38000, SDS-PAGE
Aquifex aeolicus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
-
Aquifex aeolicus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
45
-
Tm values are 45°C and 70°C
Aquifex aeolicus
70
-
Tm values are 45°C and 70°C
Aquifex aeolicus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.5
8
the enzyme is active from pH 5.5 to 8
Aquifex aeolicus
Other publictions for EC 1.13.11.55
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
742795
Ruehl
A sulfur oxygenase from the h ...
Aquifex aeolicus, Thioalkalivibrio paradoxus, Thioalkalivibrio paradoxus Arh 1
J. Bacteriol.
199
e00675
2017
-
-
2
-
4
-
3
-
-
2
2
3
-
8
-
-
2
-
-
2
3
1
8
3
2
1
2
-
2
2
-
-
-
-
-
-
-
2
-
-
4
-
-
3
-
-
-
2
2
3
-
-
-
2
-
2
3
1
8
3
2
1
2
-
2
2
-
-
-
2
2
-
-
-
742580
Guo
Sulfur metabolism pathways in ...
Sulfobacillus acidophilus, Sulfobacillus acidophilus TPY
Front. Microbiol.
7
1861
2016
-
-
1
-
-
-
-
-
-
-
-
2
-
7
-
-
-
-
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
743261
Janosch
Sulfur oxygenase reductase (S ...
no activity in Acidithiobacillus caldus, Sulfobacillus thermosulfidooxidans, Sulfobacillus thermosulfidooxidans DSM 9293
Microorganisms
3
707-724
2015
-
-
1
-
-
-
-
-
-
-
-
-
-
12
-
-
-
-
-
1
2
-
4
-
2
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
4
-
4
-
4
-
-
-
2
-
-
-
-
-
-
-
-
-
742198
Yin
Whole-genome sequencing revea ...
Acidithiobacillus thiooxidans, Acidithiobacillus thiooxidans A01
BMC Microbiol.
14
179
2014
-
-
1
-
-
-
-
-
1
-
-
2
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
725890
Zhang
Site-specific mutagenesis and ...
Sulfobacillus acidophilus, Sulfobacillus acidophilus TPY
Microbiol. Res.
168
654-660
2013
1
-
1
-
7
-
-
-
-
-
1
2
-
7
-
-
1
-
1
-
7
-
2
1
1
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
7
-
-
-
-
-
-
-
1
2
-
-
-
1
1
-
7
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
724777
You
-
Structural basis for the therm ...
Acidianus tengchongensis, Acidithiobacillus sp. SM-1, Sulfurisphaera tokodaii
Chin. J. Chem. Engin.
20
52-61
2012
-
-
3
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
3
-
3
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
3
-
-
-
-
-
-
-
-
-
-
-
725278
Veith
The sulfur oxygenase reductase ...
Halothiobacillus neapolitanus, Halothiobacillus neapolitanus DSM 15147
J. Bacteriol.
194
677-685
2012
-
-
1
-
-
-
1
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
2
1
1
1
1
-
1
1
-
-
1
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
2
-
-
-
-
-
-
-
-
2
1
1
1
1
-
1
1
-
-
-
2
2
-
-
-
726299
Chen
Acidithiobacillus caldus sulfu ...
Acidithiobacillus caldus, Acidithiobacillus caldus MTH-04
PLoS ONE
7
e39470
2012
-
1
1
-
1
-
-
-
1
-
-
2
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
725074
Veith
Substrate pathways and mechani ...
Acidianus ambivalens
Front. Microbiol.
2
37
2011
1
-
1
1
16
-
3
-
1
1
-
1
-
3
-
-
-
-
-
-
-
-
1
1
1
-
-
-
1
-
-
-
-
-
-
1
-
1
-
1
16
-
-
3
-
-
1
1
-
1
-
-
-
-
-
-
-
-
1
1
1
-
-
-
1
-
-
-
-
2
2
-
-
-
697350
Chen
-
Site-directed mutagenesis reve ...
Acidianus tengchongensis
Chin. Sci. Bull.
54
652-657
2009
-
-
1
-
6
-
3
-
-
1
-
1
-
1
-
-
1
-
-
-
1
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
6
-
-
3
-
-
-
1
-
1
-
-
-
1
-
-
1
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
684915
Li
Crystal structure studies on s ...
Acidianus tengchongensis
Biochem. Biophys. Res. Commun.
369
919-923
2008
-
-
-
1
5
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
686624
Pelletier
First characterisation of the ...
Aquifex aeolicus
Extremophiles
12
205-215
2008
-
-
1
-
-
-
-
-
-
1
3
1
-
4
-
-
1
-
-
-
1
-
2
1
1
-
2
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
3
1
-
-
-
1
-
-
1
-
2
1
1
-
2
-
-
1
-
-
-
-
-
-
-
-
723994
Albers
Production of recombinant and ...
Acidianus ambivalens
Appl. Environ. Microbiol.
72
102-111
2006
-
-
1
-
-
-
-
-
1
-
1
-
-
5
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
726486
Urich
X-ray structure of a self-comp ...
Acidianus ambivalens
Science
311
996-1000
2006
-
-
-
-
-
-
-
-
-
1
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
663712
Chen
Key role of cysteine residues ...
Acidianus tengchongensis, Acidianus tengchongensis S5
Appl. Environ. Microbiol.
71
621-628
2005
4
-
1
-
4
-
13
-
2
-
-
-
-
2
-
-
1
-
-
-
6
1
2
-
-
-
-
-
-
-
-
-
-
-
-
4
-
1
-
-
4
-
-
13
-
-
2
-
-
-
-
-
-
1
-
-
6
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
664199
Urich
The sulfur oxygenase reductase ...
Acidianus ambivalens, Acidianus ambivalens 5737
Biochim. Biophys. Acta
1747
267-270
2005
-
-
1
1
-
-
-
-
-
-
1
-
-
4
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
664994
Urich
Identification of core active ...
Acidianus ambivalens
FEMS Microbiol. Lett.
248
171-176
2005
-
1
1
-
14
-
-
-
-
2
-
1
-
3
-
-
1
-
-
-
16
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
24
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
16
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
724213
Urich
The sulphur oxygenase reductas ...
Acidianus ambivalens, Acidianus ambivalens DSM 3772
Biochem. J.
381
137-146
2004
1
-
1
-
-
-
1
2
-
1
2
2
2
5
-
-
1
-
1
-
-
-
6
1
-
-
-
2
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
2
-
1
2
2
2
-
-
1
1
-
-
-
6
1
-
-
-
2
-
-
-
-
-
1
1
-
-
-
658665
Sun
Purification and properties of ...
Acidianus sp., Acidianus sp. S5
Extremophiles
7
131-134
2003
-
1
1
-
-
-
-
-
-
-
1
-
-
8
-
-
1
-
-
-
1
-
2
-
1
1
-
-
1
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
-
2
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-
439600
He
Cloning and heterologous expre ...
Acidianus sp. S5, Acidianus tengchongensis
FEMS Microbiol. Lett.
193
217-221
2000
-
-
1
-
-
-
-
-
-
-
2
-
-
8
-
-
-
-
-
-
8
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
8
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
666952
Kletzin
-
Sulfur oxidation and reduction ...
Acidianus ambivalens
Syst. Appl. Microbiol.
16
534-543
1994
-
1
1
-
-
-
8
-
1
1
4
-
-
1
-
-
1
-
-
-
3
-
1
2
1
1
-
-
1
1
-
-
-
1
-
-
1
1
-
-
-
-
-
8
-
-
1
1
4
-
-
-
-
1
-
-
3
-
1
2
1
1
-
-
1
1
-
1
-
-
-
-
-
-
665355
Kletzin
Molecular characterization of ...
Acidianus ambivalens
J. Bacteriol.
174
5854-5859
1992
-
1
1
-
-
-
-
-
-
-
1
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
439594
Kletzin
Coupled enzymatic production o ...
Acidianus ambivalens, Acidianus ambivalens DSM 3772
J. Bacteriol.
171
1638-1643
1989
-
-
-
-
-
2
7
-
1
-
2
-
-
5
-
-
1
-
-
1
1
-
2
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
7
-
-
1
-
2
-
-
-
-
1
-
1
1
-
2
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-