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Literature summary for 2.7.9.3 extracted from

  • Preobrazhenskaya, Y.V.; Stenko, A.I.; Shvarts, M.V.; Lugovtsev, V.Y.
    Binding stoichiometry of a recombinant selenophosphate synthetase with one synonymic substitution E197D to a fluorescent nucleotide analog of ATP, TNP-ATP (2013), J. Amino Acids, 2013, 983565.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.9.3

Cloned(Commentary)

Cloned (Comment) Organism
gene selD, DNA and amino acid sequence determination and analysis of enzymes from Escherichia coli strains DH5alpha-T1 AND BL21-Gold (DE3), that differ in position 14 and 197, and compared to the DNA sequence from Escherichia coli strain K-12, recombinant overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21-Gold (DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
E197D site-directed mutagenesis Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37500
-
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + selenide + H2O Escherichia coli
-
 AMP + selenophosphate + phosphate
-
 ?
ATP + selenide + H2O Escherichia coli DH5alpha-T1 and BL21-Gold(DE3)
-
 AMP + selenophosphate + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 gene selD
-
Escherichia coli DH5alpha-T1 and BL21-Gold(DE3)
-
 gene selD
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21-Gold (DE3) by ammonium sulfate fractionation, dialysis, and anion exchange chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-triphosphate + selenide + H2O the compound is used as a synthetic analogue of the substrate ATP for the monitoring and quantitative analysis of the functional activity of SPS Escherichia coli 2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-monophosphate + selenophosphate + phosphate
-
 ?
2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-triphosphate + selenide + H2O the compound is used as a synthetic analogue of the substrate ATP for the monitoring and quantitative analysis of the functional activity of SPS Escherichia coli DH5alpha-T1 and BL21-Gold(DE3) 2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-monophosphate + selenophosphate + phosphate
-
 ?
ATP + selenide + H2O
-
 Escherichia coli AMP + selenophosphate + phosphate
-
 ?
ATP + selenide + H2O
-
 Escherichia coli DH5alpha-T1 and BL21-Gold(DE3) AMP + selenophosphate + phosphate
-
 ?

Subunits

Subunits Comment Organism
dimer 4 * 37500, SDS-PAGE, in solution, the recombinant SPS exists as a dimer with two active sites capable of ATP binding in each subunit Escherichia coli
tetramer 4 * 37500, SDS-PAGE, the enzyme SPS seems to exist in a form of tetramer in given reaction conditions, in accordance with the concentration stoichiometry of 4 mol of TNP-ATP to 1 mole of recombinant protein, molecular structure modelling Escherichia coli

Synonyms

Synonyms Comment Organism
SelD
-
 Escherichia coli
selenophosphate synthetase
-
 Escherichia coli
SPS
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-triphosphate i.e. TNP-ATP, binding analysis of recombinant wild-type and mutant E197D to TNP-ATP, a synthetic fluorescent nucleotide analogue of ATP. The compound is used as a synthetic analogue of the substrate ATP for the monitoring and quantitative analysis of the functional activity of SPS. A non-linear regression analysis of the saturation curve of TNP-ATP binding to D197 SPS fitting to a model with 2 distinct binding sites with KDs different in order. Kinetics, overview Escherichia coli
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
additional information the non-linear regression analysis of the saturation curve of TNP-ATP binding to D197 SPS fits to a model with 2 distinct binding sites with KDs different in order. Enzyme SPS exists in a form of tetramer in given reaction conditions, in accordance with the concentration stoichiometry of 4 mol of 2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-triphosphate to 1 mole of recombinant protein Escherichia coli