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Literature summary extracted from

  • Alekseeva, M.; Mavletova, D.; Kolchina, N.; Nezametdinova, V.; Danilenko, V.
    Isolation and purification of recombinant serine/threonine protein kinases of the strain Bifidobacterium longum B379M and investigation of their activity (2015), Biochemistry, 80, 1303-1311 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.1 gene pkb1, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged isozyme in Escherichia coli strain BL21(DE3)pLysS in inclusion bodies Bifidobacterium longum
2.7.11.1 gene pkb2, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged isozyme in Escherichia coli strain BL21(DE3)pLysS in inclusion bodies Bifidobacterium longum
2.7.11.1 gene pkb3, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21(DE3)pLysS Bifidobacterium longum
2.7.11.1 gene pkb4, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21(DE3)pLysS Bifidobacterium longum
2.7.11.1 gene pkb5, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged isozyme in Escherichia coli strain BL21(DE3)pLysS in inclusion bodies Bifidobacterium longum
2.7.11.1 gene pkb6, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged isozyme in Escherichia coli strain BL21(DE3)pLysS in inclusion bodies Bifidobacterium longum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.11.1 34592
-
mass spectrometry Bifidobacterium longum
2.7.11.1 51540
-
mass spectrometry Bifidobacterium longum
2.7.11.1 76989
-
mass spectroemtry Bifidobacterium longum
2.7.11.1 80070
-
mass spectrometry Bifidobacterium longum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.11.1 ATP + a protein Bifidobacterium longum
-
ADP + a phosphoprotein
-
r
2.7.11.1 ATP + a protein Bifidobacterium longum B379M
-
ADP + a phosphoprotein
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.1 Bifidobacterium longum M1QEG4
-
-
2.7.11.1 Bifidobacterium longum M1R338
-
-
2.7.11.1 Bifidobacterium longum M1R344
-
-
2.7.11.1 Bifidobacterium longum M1R969
-
-
2.7.11.1 Bifidobacterium longum M1RFK9
-
-
2.7.11.1 Bifidobacterium longum M1RNN3
-
-
2.7.11.1 Bifidobacterium longum B379M M1QEG4
-
-
2.7.11.1 Bifidobacterium longum B379M M1R338
-
-
2.7.11.1 Bifidobacterium longum B379M M1R344
-
-
2.7.11.1 Bifidobacterium longum B379M M1R969
-
-
2.7.11.1 Bifidobacterium longum B379M M1RFK9
-
-
2.7.11.1 Bifidobacterium longum B379M M1RNN3
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.11.1 additional information the enzyme does not autophosphorylate Bifidobacterium longum
2.7.11.1 phosphoprotein the enzyme performs autophosphorylation Bifidobacterium longum

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.1 recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography Bifidobacterium longum
2.7.11.1 recombinant His-tagged isozyme, solubilized from Escherichia coli strain BL21(DE3)pLysS inclusion bodies, by nickel affinity chromatography Bifidobacterium longum
2.7.11.1 the recombinant His-tagged isozyme Pkb5 catalytic domain is purified and eluted from nickel affinity chromatography by a solution containing 6 M urea, 100 mM Na2HPO4, 10 mM Tris-HCl, 50 mM imidazole, pH 5.3, and 300 mM imidazole, followed by renaturing via dialysis against 1.5 M urea, 50 mM Tris-HCl, 200 mM NaCl, 10% glycerol, pH 8.0 Bifidobacterium longum

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.7.11.1 recombinant His-tagged isozyme Pkb1 from Escherichia coli inclusion bodies by denaturing lysis buffer, containing 6 M urea, 100 mM Na2HPO4, 10 mM Tris-HCl, pH 8.0, and dialysis Bifidobacterium longum
2.7.11.1 recombinant His-tagged isozyme Pkb2 from Escherichia coli inclusion bodies by denaturing lysis buffer, containing 6 M urea, 100 mM Na2HPO4, 10 mM Tris-HCl, pH 8.0, and dialysis Bifidobacterium longum
2.7.11.1 recombinant His-tagged isozyme Pkb5 catalytic domain from Escherichia coli inclusion bodies by denaturing lysis buffer, containing 6 M urea, 100 mM Na2HPO4, 10 mM Tris-HCl, pH 8.0 Bifidobacterium longum
2.7.11.1 recombinant His-tagged isozyme Pkb6 from Escherichia coli inclusion bodies by denaturing lysis buffer, containing 6 M urea, 100 mM Na2HPO4, 10 mM Tris-HCl, pH 8.0, and dialysis Bifidobacterium longum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.1 ATP + a protein
-
Bifidobacterium longum ADP + a phosphoprotein
-
r
2.7.11.1 ATP + a protein
-
Bifidobacterium longum B379M ADP + a phosphoprotein
-
r
2.7.11.1 additional information the enzyme performs autophosphorylation Bifidobacterium longum ?
-
?
2.7.11.1 additional information the enzyme does not perform autophosphorylation Bifidobacterium longum ?
-
?
2.7.11.1 additional information the enzyme's catalytic domain performs autophosphorylation Bifidobacterium longum ?
-
?
2.7.11.1 additional information the enzyme performs autophosphorylation Bifidobacterium longum B379M ?
-
?
2.7.11.1 additional information the enzyme does not perform autophosphorylation Bifidobacterium longum B379M ?
-
?
2.7.11.1 additional information the enzyme's catalytic domain performs autophosphorylation Bifidobacterium longum B379M ?
-
?

Subunits

EC Number Subunits Comment Organism
2.7.11.1 ? 1 * 51540, mass spectrometry, 1 * 45000, recombinant enzyme, SDS-PAGE, 1 * 26766, enzyme catalytic domain, mass spectrometry Bifidobacterium longum
2.7.11.1 ? x * 60439, mass spectrometry, x * 44000, recombinant enzyme, SDS-PAGE, x * 25916, enzyme catalytic domain, mass spectrometry Bifidobacterium longum
2.7.11.1 ? x * 72260, mass spectrometry, x * 47000, recombinant enzyme, SDS-PAGE, x * 29344, enzyme catalytic domain, mass spectrometry Bifidobacterium longum
2.7.11.1 dimer 2 * 44000, recombinant enzyme, SDS-PAGE, 2 * 26334, enzyme catalytic domain, mass spectrometry Bifidobacterium longum
2.7.11.1 dimer 2 * 48000, recombinant enzyme, SDS-PAGE, 2 * 30363, enzyme catalytic domain, mass spectrometry Bifidobacterium longum
2.7.11.1 monomer 1 * 34592, mass spectrometry, 1 * 45000, recombinant enzyme, SDS-PAGE, 1 * 26705, enzyme catalytic domain, mass spectrometry Bifidobacterium longum

Synonyms

EC Number Synonyms Comment Organism
2.7.11.1 Pkb1
-
Bifidobacterium longum
2.7.11.1 Pkb2
-
Bifidobacterium longum
2.7.11.1 Pkb3
-
Bifidobacterium longum
2.7.11.1 Pkb4
-
Bifidobacterium longum
2.7.11.1 Pkb5
-
Bifidobacterium longum
2.7.11.1 Pkb6
-
Bifidobacterium longum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.1 22 37 assay at room temperature or at 37°C Bifidobacterium longum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.1 7.4
-
assay at Bifidobacterium longum

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.1 ADP
-
Bifidobacterium longum
2.7.11.1 ATP
-
Bifidobacterium longum

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.11.1 Bifidobacterium longum isoelectric focusing
-
4.87
2.7.11.1 Bifidobacterium longum isoelectric focusing
-
5.14
2.7.11.1 Bifidobacterium longum isoelectric focusing
-
5.34
2.7.11.1 Bifidobacterium longum isoelectric focusing
-
5.54
2.7.11.1 Bifidobacterium longum isoelectric focusing
-
6.32
2.7.11.1 Bifidobacterium longum isoelectric focusing
-
6.97

General Information

EC Number General Information Comment Organism
2.7.11.1 physiological function serine/threonine protein kinases (STPK) are enzymes that modify other proteins by reversible phosphorylation at serine or threonine residues within consensus sequences, thereby modulating the activity of a broad range of enzymes and controlling specific protein-protein interactions. STPKs of Bifidobacterium can be elements of signal transduction networks and play major regulatory roles in bifidobacterial cells Bifidobacterium longum