Information on EC 1.8.5.4 - sulfide:quinone reductase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.8.5.4
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RECOMMENDED NAME
GeneOntology No.
sulfide:quinone reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
n HS- + n quinone = polysulfide + n quinol
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfide oxidation I (sulfide-quinone reductase)
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Sulfur metabolism
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SYSTEMATIC NAME
IUBMB Comments
sulfide:quinone oxidoreductase
Contains FAD. Ubiquinone, plastoquinone or menaquinone can act as acceptor in different species. This enzyme catalyses the formation of sulfur globules. It is also an important step in anoxygenic bacterial photosynthesis.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 sulfide + ubiquinone-1
hydrogen disulfide + ubiquinol-1
show the reaction diagram
-
-
-
?
sulfide + 2,3-dimethyl-1,4-naphthoquinone
sulfur + 2,3-dimethyl-1,4-naphthoquinol
show the reaction diagram
-
-
-
-
?
sulfide + 2-methyl-3-methylthio-1,4-naphthoquinone
sulfur + 2-methyl-3-methylthio-1,4-naphthoquinol
show the reaction diagram
-
lowest activity
-
-
?
sulfide + caldariellaquinone
sulfur + caldariellaquinol
show the reaction diagram
-
-
-
-
?
sulfide + cyanide + ubiquinone-1
thiocyanate + ubiquinol-1
show the reaction diagram
-
-
-
?
sulfide + decylubiquinone
polysulfide + decylubiquinol
show the reaction diagram
sulfide + decylubiquinone
sulfur + decylubiquinol
show the reaction diagram
sulfide + decylubiquinone + cyanide
sulfur + decylubiquinol + thiocyanate
show the reaction diagram
-
-
-
-
?
sulfide + decylubiquinone + Escherichia coli thioredoxin
sulfur + decylubiquinol + ?
show the reaction diagram
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with Escherichia coli thioredoxin, SQR exhibits one-tenth of the cyanide-dependent activity
-
-
?
sulfide + decylubiquinone + sulfite
sulfur + decylubiquinol + ?
show the reaction diagram
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with sulfite, SQR exhibits one-tenth of the cyanide-dependent activity
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-
?
sulfide + duroquinone
sulfur + duroquinol
show the reaction diagram
sulfide + duroquinone 23
sulfur + duroquinol
show the reaction diagram
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% compared to the activity with decylubiquinone
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-
?
sulfide + menadione
polysulfide + menadiol
show the reaction diagram
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25% compared to the activity with decylubiquinone
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-
?
sulfide + menadione
sulfur + menadiol
show the reaction diagram
sulfide + plastoquinone-1
sulfur + plastoquinol-1
show the reaction diagram
sulfide + plastoquinone-2
sulfur + plastoquinol-2
show the reaction diagram
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highest activity
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-
?
sulfide + quinone
elemental sulfur + quinol
show the reaction diagram
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-
-
-
?
sulfide + quinone
sulfur + quinol
show the reaction diagram
sulfide + sulfite + ubiquinone-1
thiosulfate + ubiquinol-1
show the reaction diagram
-
-
-
?
sulfide + ubiquinone
? + ubiquinol
show the reaction diagram
sulfide + ubiquinone-1
sulfur + ubiquinol-1
show the reaction diagram
sulfide + ubiquinone-2
sulfur + ubiquinol-2
show the reaction diagram
sulfide + ubiquinone-4
sulfur + ubiquinol-4
show the reaction diagram
sulfide + ubiquinone-9
sulfur + ubiquinol-9
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sulfide + quinone
elemental sulfur + quinol
show the reaction diagram
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-
-
-
?
sulfide + ubiquinone-1
sulfur + ubiquinol-1
show the reaction diagram
Q9Y6N5
-
-
-
?
additional information
?
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Q9Y6N5
cyanide, sulfite, or sulfide can act as the sulfane sulfur acceptor in reactions that exhibit pH optima at 8.5, 7.5, or 7.0, respectively, and produce thiocyanate, thiosulfate, or a putative sulfur analogue of hydrogen peroxide, i.e. H2S2, respectively. Sulfite is the physiological acceptor of the sulfur and the reaction is the predominant source of the thiosulfate produced during H2S oxidation by mammalian tissues
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-heptylquinolin-4-ol 1-oxide
2-n-heptyl-4-hydroxy-quinone-N-oxide
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2-n-nonyl-4-hydroxyquinoline-N-oxide
2n-nonyl-4-hydroxyquinoline-N-oxide
Antimycin
antimycin A
aurachin C
cyanide
HQNO
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a quinone competitive inhibitor
iodoacetamide
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0.3 mM, complete inhibition
Myxothiazol
myxothiazole
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n-nonyl-4-hydroxyquinoline-N-oxide
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Stigmatellin
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyanide
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SQR isolated from yeast mitochondria reduces decyl-ubiquinone after the addition of sulfide only in the presence of cyanide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65 - 2.6
cyanide
0.002 - 0.036
decylubiquinone
0.031 - 0.04
plastoquinone-1
0.002 - 0.4
Sulfide
0.174
sulfite
cosubstrates sulfide, ubiquinone-1, pH 7.5, 25C
0.0054 - 0.0199
ubiquinone-1
0.014
ubiquinone-2
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apparent value, at pH 7.0, temperature not specified in the publication
0.0016
ubiquinone-4
0.00643
ubiquinone-9
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
2,3-dimethyl-1,4-naphthoquinone
Acidianus ambivalens
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at 50C, pH 6.5
0.43
caldariella quinone
Acidianus ambivalens
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at 50C, pH 6.5
330
cyanide
Homo sapiens
Q9Y6N5
cosubstrates sulfide, ubiquinone-1, pH 8.5, 25C
0.38 - 1.2
decylubiquinone
0.15
menadione
Acidianus ambivalens
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at 50C, pH 6.5
0.6 - 379
Sulfide
368
sulfite
Homo sapiens
Q9Y6N5
cosubstrates sulfide, ubiquinone-1, pH 7.5, 25C
360 - 364
ubiquinone-1
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5100
cyanide
Homo sapiens
Q9Y6N5
cosubstrates sulfide, ubiquinone-1, pH 8.5, 25C
118
2100 - 31000
Sulfide
318
19000 - 27000
ubiquinone-1
1150
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
cyanide
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20 mM Tris-HCl, pH 8.0, at 22C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005 - 0.012
2-heptylquinolin-4-ol 1-oxide
0.05
2-n-heptyl-4-hydroxy-quinone-N-oxide
Acidithiobacillus ferrooxidans
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at pH 7.0, temperature not specified in the publication
0.00076 - 0.006
2-n-nonyl-4-hydroxyquinoline-N-oxide
0.015
Antimycin
Aquifex aeolicus
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in 50 mM Tris-HCl, pH 7.4, 40C
0.00096 - 0.22
antimycin A
0.000012 - 0.028
aurachin C
0.000038
aurachin D
Chlorobaculum thiosulfatiphilum
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in 20 mM Tris-HCl, pH 7.8, at 24C
0.01 - 0.54
cyanide
0.004 - 0.039
Myxothiazol
0.043
myxothiazole
Aquifex aeolicus
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in 50 mM Bis-Tris (pH 7.0), at 20C
0.00014
n-nonyl-4-hydroxyquinoline-N-oxide
Oscillatoria limnetica
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in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22C
0.000005 - 0.02
Stigmatellin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.018
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enzyme from washed membrane, in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22C
0.1
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crude extract, in 10 mM bis-Tris-HCl, pH 6.5, temperature not specified in the publication
0.11
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cell-free extract, at pH 7.0, temperature not specified in the publication
0.127
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using 2,3-dimethyl-1,4-naphthoquinone as cosubstrate, at 50C, pH 6.5
0.194
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using menadione as cosubstrate, at 50C, pH 6.5
0.47
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using decylubiquinone as cosubstrate, at 50C, pH 6.5
0.531
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using caldariella quinone as cosubstrate, at 50C, pH 6.5
1.88
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after 105fold purification, in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22C
20.55
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after 186.8fold purification, at pH 7.0, temperature not specified in the publication
55.4
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in 50 mM Tris-HCl (pH 7.5), temperature not specified in the publication
71.4
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at 40C, pH 7.4
581
pH 7.5, 25C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
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with 0.015 mM decylubqiuinone reduced/mg protein/min, the activity at 70C is 5fold higher than the activity at 20C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
estimated from amino acid sequence
6.5
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deduced from amino acid sequence
7.7
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estimated from amino acid sequence
9.7
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calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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enzyme mRNA expression during sulfide exposure in the body wall and hindgut increases in a time- and concentration-dependent manner that increases significantly at 12 h and continuously increases with time. At the protein level, enzyme expression in the two tissues increases significantly at 12 h after application of 50 microM sulfide and 6 h after 150 microM, and then continues to increase
Manually annotated by BRENDA team
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termination of endogenous H2S signalling in the colonic muscularis externa occurs via catabolism to thiosulfate and sulfate partially via a mechanism involving sulfide:quinone reductase
Manually annotated by BRENDA team
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enzyme mRNA expression during sulfide exposure in the body wall and hindgut increases in a time- and concentration-dependent manner that increases significantly at 12 h and continuously increases with time. At the protein level, enzyme expression in the two tissues increases significantly at 12 h after application of 50 microM sulfide and 6 h after 150 microM, and then continues to increase
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
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sedimentation equilibrium centrifugation
46930
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deduced from amino acid sequence
47000
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calculated from amino acid sequence
52000
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SDS-PAGE
55000
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SDS-PAGE
60000 - 65000
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native enzyme, gel filtration
120000
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gel filtration
160000
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analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
monomer
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1 * 57000, SDS-PAGE
multimer
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x * 47000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 2.2 M NH4H2PO4 and 100 mM Tris-HCl, pH 8.5 (final pH of the solution is 4.5), or 2.2 M NH4H2PO4/K2HPO4 at pH 4.5
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crystal structures of the wild-type enzyme in complex with sodium selenide and gold(I) cyanide. Mechanism for the reduction of sulfides to elemental sulfur may involve nucleophilic attack of Cys356 on C4A atom of FAD or alternatively, an alternative anionic radical mechanism by direct electron transfer from Cys356 to the isoalloxazine ring of FAD
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hanging drop vapor diffusion method, using 30% (w/v) PEG 600, 0.1 M bis-Tris pH 5.5, 0.1 M ammonium sulfate
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native or in complex with decylubiquinone, hanging drop vapor diffusion method, using 30% (w/v) polyethylene glycol 600, 0.1 M 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)propane-1,3-diol (pH 5.5 or pH 6.5), 0.1 M magnesium sulfate, and 0.05% (w/v) n-dodecyl beta-D-maltoside
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crystallization in two crystal forms of hexagonal, prism shape and thin, elongated shape
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hanging drop vapor diffusion method, using 2.0 M ammonium sulfate and 4% (v/v) PEG 400
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
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the reaction with membranes that have been heated for more than 2 h at 95C is negligible
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, protein is stable and monodisperse in 50 mM dodecyl-D-maltoside for weeks, either in the absence of salt or in the presence of N 1 M NaCl
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4C, purified protein in 3% (w/v) dodecyl-beta-D-maltoside either in the absence of salt or in the presence of N 1 M NaCl, six weeks, no loss of activity
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80C, purified protein in 3% (w/v) dodecyl-beta-D-maltoside either in the absence of salt or in the presence of N 1 M NaCl, one day, 50% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Hi-Trap column chromatography, and Superdex 200 gel filtration
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ammonium sulfate precipitation, phenyl-Toyopearl column chromatography, and TSKgel G3000 gel filtration
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ammonium sulfate precipitation, phenyl-TSK column chromatography, T SK-gel filtration and analytical gel filtration
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DEAE-cellulose column chromatography and Mono Q column chromatography
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MonoQ column chromatography and TSK 4000 gel filtration
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MonoQ column chromatography, TSK-1 gel filtration, and TSK-2 gel filtration
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Ni-NTA column chromatography
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Ni-NTA column chromatography, gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) or Rosetta-gami(DE3) cells as a thioredoxin-fusion protein in inclusion bodies in an inactive form
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expressed in Escherichia coli; expression in Escherichia coli
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expressed in Saccharomyces cerevisiae
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expression at low temperature in Escherichia coli by using an optimized synthetic gene and cold-adapted chaperonins
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme mRNA expression during sulfide exposure in the body wall and hindgut increases in a time- and concentration-dependent manner that increases significantly at 12 h and continuously increases with time
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SQR activity is induced for 2 h in the presence of 1.25 mM sulfide and light
the number of Sqrdl transcripts in the brain increases with increasing age
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C128S
-
loss of activity in assay with decylubiquinone
C356S
-
loss of activity in assay with decylubiquinone, loss of activity for reduction of FAD fluorescence by Na2S
H132A
-
about 40% of wild-type activity in assay with decylubiquinone
H198A
-
about 60% of wild-type activity in assay with decylubiquinone
S126A
-
about 35% of wild-type activity in assay with decylubiquinone
C128A
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about 35% of wild-type activity in assay with decylubiquinone
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C160A
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loss of activity in assay with decylubiquinone, about 35% of wild-type activity for reduction of FAD fluorescence by Na2S
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H132A
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about 40% of wild-type activity in assay with decylubiquinone
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H198A
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about 60% of wild-type activity in assay with decylubiquinone
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S126A
-
about 35% of wild-type activity in assay with decylubiquinone
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L379D
-
all of the expressed protein is membrane-bound, the mutant enzyme is inactive; inactive mutant enzyme, all of the expressed protein is membrane-bound
L379D/M380N
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both the membrane-bound and soluble forms of this protein are inactive; the mutant protein is found in both the cytoplasmic and membrane fractions in equal proportions after disruption of the Escherichia coli cells, and each fraction has the same FAD content as the membrane bound wild type enzyme (about 50%)
L379N
-
all of the expressed protein is membrane-bound, the mutant enzyme is inactive; the mutant enzyme is inactive due to a perturbation of the decylubiquinone binding site
M380N
-
mutation results in protein that is entirely membrane-bound, but which has the same activity as wild type enzyme; this is one of the two mutations in the L379D/M380N double mutant. The M380N mutation by itself results in protein that is entirely membrane-bound, but which has the same activity as wild type enzyme
Y383Q/F384K
-
both the soluble and membrane-bound versions of this double-mutant are catalytically active. The membrane-bound mutant enzyme has a specific activity about 30% higher than the wild type enzyme and the Km for sulfide is about half of the value found for the wild type enzyme. The water-soluble version of this mutant enzyme is twice as active as the wild type enzyme and the Km values for both sulfide and decylubiquinone are about the same as the wild type, membrane-bound form; this mutant protein is expressed in a yield similar to the wild type enzyme and is found equally in the cytoplasmic and membrane fractions after cell disruption. The isolated proteins from each fraction contain FAD to the same extent as the wild type enzyme. Both the soluble and membrane bound versions of this double-mutant are catalytically active. The membrane-bound mutant enzyme has a specific activity about 30% higher than the wild type enzyme and the Km for sulfide is about half of the value found for the wild type (0.046 mM vs.0.077 mM). The water-soluble version of this mutant enzyme is twice as active as the wild type SQR (1.20 vs. 0.60 nmol quinone reduced/s* nM FAD) and the Km values for both sulfide and decylubiquinone are about the same as the wild type, membrane-bound form
Y383Q/F384K/L379D/M380N
-
the mutant protein is found entirely in the cytoplasmic fraction but there is no catalytic activity
L379D/M380N
-
both the membrane-bound and soluble forms of this protein are inactive
-
Y383Q/F384K
-
both the soluble and membrane-bound versions of this double-mutant are catalytically active. The membrane-bound mutant enzyme has a specific activity about 30% higher than the wild type enzyme and the Km for sulfide is about half of the value found for the wild type enzyme. The water-soluble version of this mutant enzyme is twice as active as the wild type enzyme and the Km values for both sulfide and decylubiquinone are about the same as the wild type, membrane-bound form; this mutant protein is expressed in a yield similar to the wild type enzyme and is found equally in the cytoplasmic and membrane fractions after cell disruption. The isolated proteins from each fraction contain FAD to the same extent as the wild type enzyme. Both the soluble and membrane bound versions of this double-mutant are catalytically active. The membrane-bound mutant enzyme has a specific activity about 30% higher than the wild type enzyme and the Km for sulfide is about half of the value found for the wild type (0.046 mM vs.0.077 mM). The water-soluble version of this mutant enzyme is twice as active as the wild type SQR (1.20 vs. 0.60 nmol quinone reduced/s* nM FAD) and the Km values for both sulfide and decylubiquinone are about the same as the wild type, membrane-bound form
-
Y383Q/F384K/L379D/M380N
-
the mutant protein is found entirely in the cytoplasmic fraction but there is no catalytic activity
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C127S
-
1.3% activity compared to the wild type enzyme
C159S
-
0.5% activity compared to the wild type enzyme
C353S
-
0.4% activity compared to the wild type enzyme
H131A
-
20% activity at pH 6.5 and 27% activity at (optimum) pH 4.5 compared to the wild type enzyme
H196A
-
38% activity at pH 6.5 and 40% activity at (optimum) pH 6.2 compared to the wild type enzyme
V300D
-
11% activity compared to the wild type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
termination of endogenous H2S signalling in the colonic muscularis externa occurs via catabolism to thiosulfate and sulfate partially via a mechanism involving sulfide:quinone reductase. In the brain, H2S signal termination occurs partially through protein sequestration and partially through catabolism not involving sulfide:quinone reductase