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Literature summary for 3.6.1.1 extracted from

  • Lee, H.S.; Cho, Y.; Kim, Y.J.; Lho, T.O.; Cha, S.S.; Lee, J.H.; Kang, S.G.
    A novel inorganic pyrophosphatase in Thermococcus onnurineus NA1 (2009), FEMS Microbiol. Lett., 300, 68-74.
    View publication on PubMed
Search for more literature for 3.6.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia Rosetta(DE3)pLysS cells Thermococcus onnurineus

Protein Variants

Protein Variants Comment Organism
G119A the mutant shows less than 50% activity towards diphosphate and increased activity towards ATP compared to the wild type enzyme Thermococcus onnurineus
G119S the mutant shows about 140% activity towards diphosphate and increased activity towards ATP and dATP compared to the wild type enzyme Thermococcus onnurineus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.35
-
 diphosphate wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Mg2+, at 80°C Thermococcus onnurineus
0.48
-
 diphosphate wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Ni2+, at 80°C Thermococcus onnurineus
0.49
-
 diphosphate wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Co2+, at 80°C Thermococcus onnurineus

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ Mg2+ is 72% less effective when compared with Ni2+, maximum activity occurs at 0.5 mM Co2+ Thermococcus onnurineus
Mg2+ Mg2+ is 9% less effective when compared with Ni2+, maximum activity occurs at 2 mM Mg2+ Thermococcus onnurineus
additional information little or no activity is observed in the presence of Cu2+, Zn2+, Ca2+, or Mn2+ Thermococcus onnurineus
additional information PPase has an absolute dependence on divalent metal cations because no measurable activity is observed in their absence Thermococcus onnurineus
Ni2+ dependent on, divalent metal cation with highest efficiency on enzymatic activity, maximum activity occurs at 0.5 mM Ni2+ Thermococcus onnurineus

Organism

Organism UniProt Comment Textmining
Thermococcus onnurineus B6YSF3
-
-

Purification (Commentary)

Purification (Comment) Organism
Talon metal affinity resin column chromatography and Superdex 200 gel filtration Thermococcus onnurineus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O 1% activity compared to diphosphate Thermococcus onnurineus ADP + phosphate
-
 ?
dATP + H2O 7% activity compared to diphosphate Thermococcus onnurineus dADP + phosphate
-
 ?
diphosphate + H2O 100% activity Thermococcus onnurineus phosphate + phosphate
-
 ?
additional information dCTP, ADP, dAMP, phosphoglycolate, phosphoserine, polyphosphate, and 4-nitrophenyl phosphate are no substrates for PPase Thermococcus onnurineus ?
-
 ?

Synonyms

Synonyms Comment Organism
inorganic pyrophosphatase
-
 Thermococcus onnurineus
PPase
-
 Thermococcus onnurineus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.16
-
 diphosphate wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Mg2+, at 80°C Thermococcus onnurineus
0.21
-
 diphosphate wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Ni2+, at 80°C Thermococcus onnurineus
0.22
-
 diphosphate wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Co2+, at 80°C Thermococcus onnurineus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 recombinant enzyme Thermococcus onnurineus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.44
-
 diphosphate wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Ni2+, at 80°C Thermococcus onnurineus
0.45
-
 diphosphate wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Co2+, at 80°C Thermococcus onnurineus
0.46
-
 diphosphate wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Mg2+, at 80°C Thermococcus onnurineus