BRENDA - Enzyme Database show
show all sequences of 1.97.1.9

Purification of selenate reductase from Alcaligenes sp. CKCr-6A with the ability to biosynthesis of selenium nanoparticle Enzymatic behavior study in imidazolium based ionic liquids and organic solvent

Mesbahi-Nowrouzi, M.; Mollania, N.; J. Mol. Liq. 249, 1254-1262 (2018)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Ag+
70% inhibition at 1 mM
Alcaligenes sp.
Ca2+
about 20% inhibition at 1 mM
Alcaligenes sp.
EDTA
inhibits the enzymatic reducing activity slightly, addition of Mo2+ and Zn2+ to the reaction mixture eliminates the EDTA inhibitory effect
Alcaligenes sp.
Hg2+
complete inhibition at 1 mM
Alcaligenes sp.
Mn2+
35% inhibition at 1 mM
Alcaligenes sp.
N-ethyl maleimide
complete inhibition
Alcaligenes sp.
NaN3
60% inhibition at 1 mM
Alcaligenes sp.
Pb2+
45% inhibition at 1 mM
Alcaligenes sp.
Zn2+
30% inhibition at 1 mM
Alcaligenes sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.8
-
selenate
pH 6.0, 35°C
Alcaligenes sp.
5.47
-
Selenite
pH 6.0, 35°C
Alcaligenes sp.
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Alcaligenes sp.
5829
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mo2+
role of Mo2+ in selenate reductase
Alcaligenes sp.
additional information
Na+ and Mg2+ have no effect on the activity at 1 mM
Alcaligenes sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
197000
-
gel filtration
Alcaligenes sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
selenate + NADH + H+
Alcaligenes sp.
-
selenite + H2O + NAD+
-
-
?
selenate + NADH + H+
Alcaligenes sp. CKCr-6A
-
selenite + H2O + NAD+
-
-
?
selenite + NADH + H+
Alcaligenes sp.
-
selenium + H2O + NAD+
-
-
?
selenite + NADH + H+
Alcaligenes sp. CKCr-6A
-
selenium + H2O + NAD+
-
-
?
Organic Solvent Stability
Organic Solvent
Commentary
Organism
Methanol
decreases enzyme activity but increases thermal inactivation of the enzyme
Alcaligenes sp.
n-propanol
decreases enzyme activity but increases thermal inactivation of the enzyme
Alcaligenes sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Alcaligenes sp.
-
isolated from Sabzevar of Iran
-
Alcaligenes sp. CKCr-6A
-
isolated from Sabzevar of Iran
-
Purification (Commentary)
Commentary
Organism
native enzyme 21.29fold by ammonium sulfate fractionation, anion exchange and hydrophonic interaction chromatography, followed by ultrafiltration
Alcaligenes sp.
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
15.36
-
purified enzyme, pH 6.0, 35°C
Alcaligenes sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
selenate + NADH + H+
-
745578
Alcaligenes sp.
selenite + H2O + NAD+
-
-
-
?
selenate + NADH + H+
-
745578
Alcaligenes sp. CKCr-6A
selenite + H2O + NAD+
-
-
-
?
selenite + NADH + H+
-
745578
Alcaligenes sp.
selenium + H2O + NAD+
-
-
-
?
selenite + NADH + H+
-
745578
Alcaligenes sp. CKCr-6A
selenium + H2O + NAD+
-
-
-
?
Subunits
Subunits
Commentary
Organism
heterotetramer
1 * 70000 + 1 * 45000 + 1 * 35000 + 1 *27000, SDS-PAGE
Alcaligenes sp.
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
-
Alcaligenes sp.
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
70
activity range, profile overview, 70% and 35% of maximum activity at 50°C and 60°C
Alcaligenes sp.
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
thermal stability analysis by differential scanning calorim
Alcaligenes sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Alcaligenes sp.
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5
9
activity range, profile overview
Alcaligenes sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ag+
70% inhibition at 1 mM
Alcaligenes sp.
Ca2+
about 20% inhibition at 1 mM
Alcaligenes sp.
EDTA
inhibits the enzymatic reducing activity slightly, addition of Mo2+ and Zn2+ to the reaction mixture eliminates the EDTA inhibitory effect
Alcaligenes sp.
Hg2+
complete inhibition at 1 mM
Alcaligenes sp.
Mn2+
35% inhibition at 1 mM
Alcaligenes sp.
N-ethyl maleimide
complete inhibition
Alcaligenes sp.
NaN3
60% inhibition at 1 mM
Alcaligenes sp.
Pb2+
45% inhibition at 1 mM
Alcaligenes sp.
Zn2+
30% inhibition at 1 mM
Alcaligenes sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.8
-
selenate
pH 6.0, 35°C
Alcaligenes sp.
5.47
-
Selenite
pH 6.0, 35°C
Alcaligenes sp.
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Alcaligenes sp.
5829
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mo2+
role of Mo2+ in selenate reductase
Alcaligenes sp.
additional information
Na+ and Mg2+ have no effect on the activity at 1 mM
Alcaligenes sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
197000
-
gel filtration
Alcaligenes sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
selenate + NADH + H+
Alcaligenes sp.
-
selenite + H2O + NAD+
-
-
?
selenate + NADH + H+
Alcaligenes sp. CKCr-6A
-
selenite + H2O + NAD+
-
-
?
selenite + NADH + H+
Alcaligenes sp.
-
selenium + H2O + NAD+
-
-
?
selenite + NADH + H+
Alcaligenes sp. CKCr-6A
-
selenium + H2O + NAD+
-
-
?
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
Methanol
decreases enzyme activity but increases thermal inactivation of the enzyme
Alcaligenes sp.
n-propanol
decreases enzyme activity but increases thermal inactivation of the enzyme
Alcaligenes sp.
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme 21.29fold by ammonium sulfate fractionation, anion exchange and hydrophonic interaction chromatography, followed by ultrafiltration
Alcaligenes sp.
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
15.36
-
purified enzyme, pH 6.0, 35°C
Alcaligenes sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
selenate + NADH + H+
-
745578
Alcaligenes sp.
selenite + H2O + NAD+
-
-
-
?
selenate + NADH + H+
-
745578
Alcaligenes sp. CKCr-6A
selenite + H2O + NAD+
-
-
-
?
selenite + NADH + H+
-
745578
Alcaligenes sp.
selenium + H2O + NAD+
-
-
-
?
selenite + NADH + H+
-
745578
Alcaligenes sp. CKCr-6A
selenium + H2O + NAD+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
heterotetramer
1 * 70000 + 1 * 45000 + 1 * 35000 + 1 *27000, SDS-PAGE
Alcaligenes sp.
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
-
Alcaligenes sp.
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
70
activity range, profile overview, 70% and 35% of maximum activity at 50°C and 60°C
Alcaligenes sp.
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
thermal stability analysis by differential scanning calorim
Alcaligenes sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Alcaligenes sp.
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5
9
activity range, profile overview
Alcaligenes sp.
General Information
General Information
Commentary
Organism
physiological function
cell-free extracts of Alcaligenes sp. CKCr-6A catalyzes the NADH-dependent reduction of selenate and selenite to elemental selenium
Alcaligenes sp.
General Information (protein specific)
General Information
Commentary
Organism
physiological function
cell-free extracts of Alcaligenes sp. CKCr-6A catalyzes the NADH-dependent reduction of selenate and selenite to elemental selenium
Alcaligenes sp.
Other publictions for EC 1.97.1.9
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)
745578
Mesbahi-Nowrouzi
-
Purification of selenate redu ...
Alcaligenes sp., Alcaligenes sp. CKCr-6A
J. Mol. Liq.
249
1254-1262
2018
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2
1
2
1
4
2
2
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1
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1
1
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1
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1
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744727
Subedi
Simultaneous selenate reducti ...
Clostridium sp., Clostridium ultunense, Exiguobacterium sp., Gottschalkia acidurici, Gottschalkia acidurici ATCC 7906, Lysinibacillus sp., Pseudomonas sp., Thauera sp. MZ1T, Tissierella sp.
Chemosphere
183
536-545
2017
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8
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8
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18
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17
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18
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744808
Wen
Quantitative detection of sel ...
Pseudomonas stutzeri, Thauera selenatis, Thauera selenatis ATCC 55363, Thauera sp.
Enzyme Microb. Technol.
85
19-24
2016
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3
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3
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4
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7
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4
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745727
Connelly
Biosynthesis of selenate redu ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2a
Microbiology
162
2136-2146
2016
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1
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5
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1
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2
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6
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2
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5
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1
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2
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2
2
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1
1
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744931
Yee
Selenate reductase activity i ...
Escherichia coli
FEMS Microbiol. Lett.
361
138-143
2014
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2
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2
1
1
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1
1
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727752
Kuroda
Molecular cloning and characte ...
Bacillus selenatarsenatis, Bacillus selenatarsenatis SF-1
J. Bacteriol.
193
2141-2148
2011
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1
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14
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1
3
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714365
Dridge
Thermostable properties of the ...
Thauera selenatis
Biochimie
92
1268-1273
2010
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1
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715508
Lowe
Quinol-cytochrome c oxidoreduc ...
Thauera selenatis
J. Biol. Chem.
285
18433-18442
2010
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1
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1
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697509
Hunter
Reduction of selenite to eleme ...
Pseudomonas sp., Pseudomonas sp. CA5
Curr. Microbiol.
58
493-498
2009
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697647
Ma
Role of menaquinone biosynthes ...
Enterobacter cloacae, Enterobacter cloacae SLD1a-1 / ATCC 700258, Escherichia coli K-12
Environ. Microbiol.
11
149-158
2009
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699361
Leaver
Enterobacter cloacae SLD1a-1 g ...
Enterobacter cloacae, Enterobacter cloacae SLD1a-1 / ATCC 700258
J. Ind. Microbiol. Biotechnol.
35
867-873
2008
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1
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684986
Dridge
Investigation of the redox cen ...
Thauera selenatis
Biochem. J.
408
19-28
2007
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671304
Ridley
Development of a viologen-base ...
Enterobacter cloacae, Enterobacter cloacae SLD1a-1 / ATCC 700258
Anal. Biochem.
358
289-294
2006
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2
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1
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7
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671468
Ridley
Resolution of distinct membran ...
Enterobacter cloacae, Enterobacter cloacae SLD1a-1 / ATCC 700258
Appl. Environ. Microbiol.
72
5173-5180
2006
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3
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1
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657903
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Microbial reduction of selenat ...
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X-ray absorption spectroscopy ...
Thauera selenatis
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644816
Watts
Selenate reduction by Enteroba ...
Enterobacter cloacae, Enterobacter cloacae SLD1a-1 / ATCC 700258
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2003
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644814
Maher
Crystallization and preliminar ...
Thauera selenatis
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2002
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644815
Bebien
Involvement of a putative moly ...
Escherichia coli
Microbiology
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2002
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644813
Krafft
Cloning and sequencing of the ...
Thauera selenatis
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10
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2000
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644812
Stolz
Bacterial respiration of arsen ...
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Schroder
Purification and characterizat ...
Thauera selenatis
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644810
Rech
The terminal reductases for se ...
Thauera selenatis
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1992
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