BRENDA - Enzyme Database
show all sequences of 1.8.5.4

Role of human sulfide quinone oxidoreductase in H2S metabolism

Jackson, M.R.; Melideo, S.L.; Jorns, M.S.; Methods Enzymol. 554, 255-270 (2015)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
cyanide
4.5fold increase in the rate of H2S oxidation in the presence of 1 mM cyanide
Homo sapiens
sulfite
13.6fold increase in the rate of H2S oxidation in the presence of 0.6 mM sulfite
Homo sapiens
Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0109
-
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
0.013
-
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
0.014
-
coenzyme Q
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
0.019
-
coenzyme Q
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
0.174
-
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
0.315
-
Sulfide
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
Homo sapiens
0.65
-
cyanide
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrial membrane
-
Homo sapiens
31966
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sulfide + coenzyme Q
Homo sapiens
-
sulfane sulfur + reduced coenzyme Q
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
Q9Y6N5
-
-
Purification (Commentary)
Commentary
Organism
HiTrap IMAC column chromatography and Q Sepharose column chromatography
Homo sapiens
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.17
-
unpurified enzyme, at pH 8.0 and 25°C
Homo sapiens
580.8
-
purified enzyme, at pH 8.0 and 25°C
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sulfide + coenzyme Q
-
743229
Homo sapiens
sulfane sulfur + reduced coenzyme Q
-
-
-
?
sulfide + cyanide + coenzyme Q
-
743229
Homo sapiens
thiocyanate + reduced coenzyme Q
-
-
-
?
sulfide + sulfide + coenzyme Q
-
743229
Homo sapiens
hydrogen disulfide + reduced coenzyme Q
-
-
-
?
sulfide + sulfite + coenzyme Q
-
743229
Homo sapiens
thiosulfate + reduced coenzyme Q
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 47000, SDS-PAGE
Homo sapiens
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
18.5
-
Sulfide
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
Homo sapiens
65
-
Sulfide
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
Homo sapiens
330
-
cyanide
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
343
-
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
360
-
coenzyme Q
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
364
-
coenzyme Q
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
368
-
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
379
-
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
the enzyme contains 0.82 mol FAD per mol protein
Homo sapiens
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
cyanide
4.5fold increase in the rate of H2S oxidation in the presence of 1 mM cyanide
Homo sapiens
sulfite
13.6fold increase in the rate of H2S oxidation in the presence of 0.6 mM sulfite
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
the enzyme contains 0.82 mol FAD per mol protein
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0109
-
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
0.013
-
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
0.014
-
coenzyme Q
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
0.019
-
coenzyme Q
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
0.174
-
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
0.315
-
Sulfide
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
Homo sapiens
0.65
-
cyanide
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrial membrane
-
Homo sapiens
31966
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sulfide + coenzyme Q
Homo sapiens
-
sulfane sulfur + reduced coenzyme Q
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
HiTrap IMAC column chromatography and Q Sepharose column chromatography
Homo sapiens
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.17
-
unpurified enzyme, at pH 8.0 and 25°C
Homo sapiens
580.8
-
purified enzyme, at pH 8.0 and 25°C
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sulfide + coenzyme Q
-
743229
Homo sapiens
sulfane sulfur + reduced coenzyme Q
-
-
-
?
sulfide + cyanide + coenzyme Q
-
743229
Homo sapiens
thiocyanate + reduced coenzyme Q
-
-
-
?
sulfide + sulfide + coenzyme Q
-
743229
Homo sapiens
hydrogen disulfide + reduced coenzyme Q
-
-
-
?
sulfide + sulfite + coenzyme Q
-
743229
Homo sapiens
thiosulfate + reduced coenzyme Q
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 47000, SDS-PAGE
Homo sapiens
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
18.5
-
Sulfide
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
Homo sapiens
65
-
Sulfide
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
Homo sapiens
330
-
cyanide
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
343
-
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
360
-
coenzyme Q
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
364
-
coenzyme Q
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
368
-
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
379
-
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
210
-
Sulfide
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
Homo sapiens
510
-
cyanide
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
2100
-
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
19000
-
coenzyme Q
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
27000
-
coenzyme Q
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
29000
-
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
31000
-
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
210
-
Sulfide
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
Homo sapiens
510
-
cyanide
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
2100
-
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
19000
-
coenzyme Q
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
27000
-
coenzyme Q
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
29000
-
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
31000
-
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
Homo sapiens
Other publictions for EC 1.8.5.4
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)
742905
Landry
H2S oxidation by nanodisc-emb ...
Homo sapiens
J. Biol. Chem.
292
11641-11649
2017
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742387
Xin
Recombinant Escherichia coli ...
Cupriavidus pinatubonensis
Environ. Microbiol.
18
5123-5136
2016
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742540
Shuman
A sulfidequinone oxidoreducta ...
Chlorobaculum tepidum
FEMS Microbiol. Lett.
363
1-8
2016
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1
1
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1
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742790
Han
Sulfide consumption in Sulfur ...
Sulfurimonas denitrificans, Sulfurimonas denitrificans DSM-1251
J. Bacteriol.
198
1260-1267
2016
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1
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6
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742453
Harb
Insertion and self-diffusion ...
Aquifex aeolicus
Eur. Phys. J. E Soft Matter
38
110
2015
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742883
Mishanina
Transient kinetic analysis of ...
Homo sapiens
J. Biol. Chem.
290
25072-25080
2015
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743229
Jackson
Role of human sulfide quinone ...
Homo sapiens
Methods Enzymol.
554
255-270
2015
2
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738630
Libiad
Organization of the human mito ...
Homo sapiens
J. Biol. Chem.
289
30901-30910
2014
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741767
Zhang
Characterization of the kinet ...
Acidithiobacillus ferrooxidans
Arch. Biochem. Biophys.
564
110-119
2014
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742246
Ackermann
The vertebrate homologue of s ...
Mus musculus, Rattus norvegicus
Cell Tissue Res.
358
779-792
2014
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727080
Lencina
Characterization of the type I ...
Caldivirga maquilingensis, Caldivirga maquilingensis IC-167
Biochim. Biophys. Acta
1827
266-275
2013
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742250
Bauzai
On the importance of anion-pi ...
Acidithiobacillus ferrooxidans
Chem. Asian J.
8
2708-2713
2013
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724350
Jackson
Human sulfide:Quinone oxidored ...
Homo sapiens
Biochemistry
51
6804-6815
2012
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7
724681
Linden
Sulphide quinone reductase con ...
Mus musculus
Br. J. Pharmacol.
165
2178-2190
2012
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Response of sulfide: quinone o ...
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The vertebrate homolog of sulf ...
Rattus norvegicus
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Cherney
Crystal structure of sulfide:q ...
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2010
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716875
Marcia
A new structure-based classifi ...
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2010
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2
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713676
Zhang
Preliminary X-ray crystallogra ...
Acidithiobacillus ferrooxidans
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839-842
2009
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Brito
Structural and functional insi ...
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716746
Marcia
The structure of Aquifex aeoli ...
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2009
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714950
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Sulfide:quinone oxidoreductase ...
Arenicola marina
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1
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1
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716170
Theissen
Single eubacterial origin of e ...
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714148
Griesbeck
Mechanism of sulfide-quinone r ...
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2002
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713985
Nuebel
Sulfide:quinone oxidoreductase ...
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2000
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1
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1
1
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1
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715343
Bronstein
Cyanobacterial sulfide-quinone ...
Aphanothece halophytica, Pseudanabaena limnetica
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3336-3344
2000
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2
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715339
Schuetz
Sulfide-quinone reductase from ...
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1999
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Schuetz
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1998
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713984
Reinartz
Sulfide oxidation in the photo ...
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1998
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715434
Schuetz
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714994
Shahak
Sulfide quinone reductase (SQR ...
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