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Literature summary for 3.6.1.11 extracted from

  • Lindner, S.N.; Knebel, S:; Wesseling,H.; Schoberth, S.M.; Wendisch, V.F.
    Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum[down-pointing small open triangle] (2009), Appl. Environ. Microbiol., 75, 3161-3170.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.1.11

Activating Compound

Activating Compound Comment Organism Structure
additional information CaCl2, BaCl2, CuSO4, and SnCl2 do not show any activating effect on PPX2 Corynebacterium glutamicum

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, overexpression of ppx2 gene in Corynebacterium glutamicum results in higher exopolyphosphatase activities in crude extracts and deletion of the gene with lower activities than those of the wild-type strain Corynebacterium glutamicum
overexpression of ppx1 gene in Corynebacterium glutamicum results in higher exopolyphosphatase activities in crude extracts and deletion of the gene with lower activities than those of the wild-type strain Corynebacterium glutamicum

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
 Corynebacterium glutamicum
ATP
-
 Corynebacterium glutamicum
Ca2+ PPX2 is inhibited by millimolar concentrations Corynebacterium glutamicum
CaCl2 3.8 mM CaCl2 leads to half-maximal inhibition of His-tagged PPX2 Corynebacterium glutamicum
dATP
-
 Corynebacterium glutamicum
dGTP
-
 Corynebacterium glutamicum
GTP
-
 Corynebacterium glutamicum
ITP
-
 Corynebacterium glutamicum
Mg2+ PPX2 is inhibited by millimolar concentrations, activity is reduced 2fold at 10 mM MnCl2 Corynebacterium glutamicum
Mn2+ PPX2 is inhibited by millimolar concentrations, activity is reduced 2fold at 3.5 mM MnCl2 Corynebacterium glutamicum
Pyrophosphate 8.2 mM pyrophosphate leads to half-maximal inhibition of His-tagged PPX2 Corynebacterium glutamicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
 Triphosphate in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2 Corynebacterium glutamicum
0.11
-
 Tetraphosphate in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2 Corynebacterium glutamicum

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ enzyme is stimulated 0.26fold at a concentration of 2 mM Corynebacterium glutamicum
K+ PPX2 activity is increased, 25 mM KCl resulting in a 3fold increase in the specific activity Corynebacterium glutamicum
Mg2+ enzyme requires Mg2+ cations but is inhibited by higher concentrations, Mg2+ shows the highest stimulation at 2 mM Corynebacterium glutamicum
Mn2+ enzyme is stimulated 0.86fold at a concentration of 2 mM Corynebacterium glutamicum
Zn2+ enzyme is stimulated 0.11fold at a concentration of 2 mM Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(phosphate)n + H2O Corynebacterium glutamicum degradation of polyphosphate (phosphate)n-1 + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q8NRR8
-
-
Corynebacterium glutamicum Q8NT99
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant ppx2 enzyme is purified by Ni-nitrilotriacetic acid chromatography Corynebacterium glutamicum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 when various short- to medium-chain PolyPs are tested, His-tagged PPX2 is most active with polyphosphates of 3-20 phosphate residues Corynebacterium glutamicum
0.04
-
 analysis of the constructed deletion mutant ppx2 reveal reduced exopolyphosphatase activity, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2 Corynebacterium glutamicum
0.08
-
 analysis of the constructed deletion mutant ppx1 reveal reduced exopolyphosphatase activity, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2 Corynebacterium glutamicum
0.12
-
 wild type, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2 Corynebacterium glutamicum
0.43
-
 overexpression of ppx1 increase the specific activity of exopolyphosphatase by 4fold compared to that of the empty vector control Corynebacterium glutamicum
0.8
-
 crude cell extracts of wild type strain pVWEx1-ppx2 show 6fold higher exopolyphosphatase activity than those of wild type pVWEx1 Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(phosphate)n + H2O degradation of polyphosphate Corynebacterium glutamicum (phosphate)n-1 + phosphate
-
 ?
additional information PPX2 is active with short-chain polyphosphates, even accepting diphosphate Corynebacterium glutamicum ?
-
 ?
tetraphosphate + H2O
-
 Corynebacterium glutamicum triphosphate + phosphate
-
 ?
triphosphate + H2O
-
 Corynebacterium glutamicum diphosphate + phosphate
-
 ?

Subunits

Subunits Comment Organism
monomer determined by gel filtration Corynebacterium glutamicum

Synonyms

Synonyms Comment Organism
exopolyphosphatase
-
 Corynebacterium glutamicum
PPX1
-
 Corynebacterium glutamicum
PPX2
-
 Corynebacterium glutamicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Corynebacterium glutamicum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25 40 at pH 6.8, 2 mM MgCl2 and 25 mM KCl, no significant loss of activity is observed after 60 min Corynebacterium glutamicum
45
-
 after preheating at 45°C for 30 and 60 min, 70% and 40% of the PPX2 activity remains Corynebacterium glutamicum
50
-
 after preheating at 50°C, His-tagged PPX2 loses its activity quickly, after incubation for 60 min, no activity remains Corynebacterium glutamicum
60
-
 complete inactivation of His-tagged PPX2 within 5 min Corynebacterium glutamicum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.6
-
 Triphosphate in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2 Corynebacterium glutamicum
0.9
-
 Tetraphosphate in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2 Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
 highest activity of recombinant His-tagged PPX2 is reached in 50 mM PIPES buffer Corynebacterium glutamicum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.4
-
 dGTP
-
 Corynebacterium glutamicum
0.6
-
 ADP
-
 Corynebacterium glutamicum
0.6
-
 dATP
-
 Corynebacterium glutamicum
0.8
-
 GTP
-
 Corynebacterium glutamicum
0.8
-
 ITP
-
 Corynebacterium glutamicum
2.6
-
 ATP
-
 Corynebacterium glutamicum