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Literature summary extracted from

  • Motomura, K.; Hirota, R.; Okada, M.; Ikeda, T.; Ishida, T.; Kuroda, A.
    A new subfamily of polyphosphate kinase 2 (class III PPK2) catalyzes both nucleoside monophosphate phosphorylation and nucleoside diphosphate phosphorylation (2014), Appl. Environ. Microbiol., 80, 2602-2608.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.4.33 additional information the enzyme is not activated in the presence of ammonium sulfate Meiothermus ruber

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.33 gene Mrub_2488, cloned from chromosomal DNA, sequence comparisons, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3)pLysS Meiothermus ruber

Protein Variants

EC Number Protein Variants Comment Organism
2.7.4.33 E126G site-directed mutagenesis, ATP synthesis activity from AMP by the mutants is reduced to 17.5% and ATP synthesis activity from ADP to 23.3% of the wild-type enzyme Meiothermus ruber
2.7.4.33 E126N site-directed mutagenesis, ATP synthesis activity from AMP by the mutants is reduced to 5.0% of the wild-type enzyme Meiothermus ruber

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.33 Mg2+ less effective than Mn2+ Meiothermus ruber
2.7.4.33 Mn2+ Meiothermus ruber PPK2 requires Mn2+ rather than Mg2+ for its activity Meiothermus ruber

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.4.33 31600
-
-
 Meiothermus ruber
2.7.4.33 32000
-
-
 Meiothermus ruber

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.33 ADP + (phosphate)n Meiothermus ruber cf. EC 2.7.4.1 ATP + (phosphate)n-1
-
 ?
2.7.4.33 ADP + (phosphate)n Meiothermus ruber NBRC 106122 cf. EC 2.7.4.1 ATP + (phosphate)n-1
-
 ?
2.7.4.33 AMP + (phosphate)n Meiothermus ruber
-
 ADP + (phosphate)n-1
-
 ?
2.7.4.33 AMP + (phosphate)n Meiothermus ruber NBRC 106122
-
 ADP + (phosphate)n-1
-
 ?
2.7.4.33 additional information Meiothermus ruber class III PPK2 shows broad substrate specificity over purine and pyrimidine bases. This class III PPK2 possesses both class I and II activities ?
-
 ?
2.7.4.33 additional information Meiothermus ruber NBRC 106122 class III PPK2 shows broad substrate specificity over purine and pyrimidine bases. This class III PPK2 possesses both class I and II activities ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.33 Meiothermus ruber A0A806DL21 gene Mrub_2488
-
2.7.4.33 Meiothermus ruber NBRC 106122 A0A806DL21 gene Mrub_2488
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.33 recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3)pLysS by affinity chromatography Meiothermus ruber

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.4.33 0.08
-
 AMP to ATP activity of the mutant E126N, pH 7.0, 70°C Meiothermus ruber
2.7.4.33 0.28
-
 AMP to ATP activity of the mutant E126G, pH 7.0, 70°C Meiothermus ruber
2.7.4.33 0.37
-
 ADP to ATP activity of the mutant E126N, pH 7.0, 70°C Meiothermus ruber
2.7.4.33 0.63
-
 ADP to ATP activity of the mutant E126G, pH 7.0, 70°C Meiothermus ruber
2.7.4.33 1.6
-
 AMP to ATP activity of the wild-type enzyme, pH 7.0, 70°C Meiothermus ruber
2.7.4.33 2.7
-
 ADP to ATP activity of the wild-type enzyme, pH 7.0, 70°C Meiothermus ruber

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.33 ADP + (phosphate)n cf. EC 2.7.4.1 Meiothermus ruber ATP + (phosphate)n-1
-
 ?
2.7.4.33 ADP + (phosphate)n cf. EC 2.7.4.1 Meiothermus ruber ATP + (phosphate)n-1
-
 r
2.7.4.33 ADP + (phosphate)n cf. EC 2.7.4.1 Meiothermus ruber NBRC 106122 ATP + (phosphate)n-1
-
 ?
2.7.4.33 ADP + (phosphate)n cf. EC 2.7.4.1 Meiothermus ruber NBRC 106122 ATP + (phosphate)n-1
-
 r
2.7.4.33 AMP + (phosphate)n
-
 Meiothermus ruber ADP + (phosphate)n-1
-
 ?
2.7.4.33 AMP + (phosphate)n
-
 Meiothermus ruber ADP + (phosphate)n-1
-
 r
2.7.4.33 AMP + (phosphate)n
-
 Meiothermus ruber NBRC 106122 ADP + (phosphate)n-1
-
 ?
2.7.4.33 additional information class III PPK2 shows broad substrate specificity over purine and pyrimidine bases. This class III PPK2 possesses both class I and II activities Meiothermus ruber ?
-
 ?
2.7.4.33 additional information class III PPK2 shows broad substrate specificity, the enzyme prefers polyphosphate of 25 to 50 in chain length. PPK2 also possesses PAP activity Meiothermus ruber ?
-
 ?
2.7.4.33 additional information class III PPK2 shows broad substrate specificity over purine and pyrimidine bases. This class III PPK2 possesses both class I and II activities Meiothermus ruber NBRC 106122 ?
-
 ?
2.7.4.33 additional information class III PPK2 shows broad substrate specificity, the enzyme prefers polyphosphate of 25 to 50 in chain length. PPK2 also possesses PAP activity Meiothermus ruber NBRC 106122 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.4.33 monomer 1 * 32000, recombinant His-tagged enzyme, SDS-PAGE, 1 * 31600, about, sequence calculation Meiothermus ruber

Synonyms

EC Number Synonyms Comment Organism
2.7.4.33 class III PPK2
-
 Meiothermus ruber

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.4.33 60 70
-
 Meiothermus ruber

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.7.4.33 40.8
-
 activity range, profile overview Meiothermus ruber

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.4.33 70
-
 recombinant enzyme PPK2 is stable at 70°C in the presence of both Mn2+ and polyphosphate but immediately loses its activity in the absence of either Mn2+ or polyphosphate, in the presence of Mg2+ and polyphosphate, PPK2 loses its activity within 15 min Meiothermus ruber

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.4.33 7
-
 assay at Meiothermus ruber

General Information

EC Number General Information Comment Organism
2.7.4.33 evolution polyphosphate kinases, responsible for the synthesis and utilization of polyphosphate, are divided into two families (PPK1 and PPK2) due to differences in amino acid sequence and kinetic properties. Phylogenetic analysis suggests that the PPK2 family is divided into three subfamilies (classes I, II, and III). Class I and II PPK2s catalyze nucleoside diphosphate and nucleoside monophosphate phosphorylation, respectively. Class III PPK2 catalyzes both nucleoside monophosphate and nucleoside diphosphate phosphorylation synthesizing ATP from AMP. Class III PPK2 shows broad substrate specificity over purine and pyrimidine bases. Class III PPK2 possesses both class I and II activities. The class III subfamily is closest to a PPK2 ancestor, overview Meiothermus ruber
2.7.4.33 additional information residue E126 is important for class III PPK2 activity. Structure homology modeling using the Arthrobacter aurescens PPK2 enzyme (PDB ID 3RHF) sequence as template Meiothermus ruber
2.7.4.33 physiological function enzyme PPK2 catalyzes preferentially polyphosphate-driven nucleotide phosphorylation (utilization of polyphosphate), which is important for the survival of microbial cells under conditions of stress or pathogenesis. Class III PPK2 catalyzes both nucleoside monophosphate and nucleoside diphosphate phosphorylation, synthesizing ATP from AMP by a single enzyme Meiothermus ruber