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Literature summary extracted from

  • Perez-Castineira, J.; Lopez-Marques, R.; Losada, M.; Serrano, A.
    A thermostable K+-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima (2001), FEBS Lett., 496, 6-11 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.1 heterologous expression in Saccharomyces cerevisiae Thermotoga maritima

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.1 membrane membrane-embedded polypeptide Thermotoga maritima 16020
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Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.1 K+ activity increases more than 6fold in the presence of KCl and NH4Cl in comparison with the activity measured in the absence of any monovalent cation Thermotoga maritima
3.6.1.1 Mg2+ the enzyme shows maximal activity with magnesium pyrophosphate, the physiological substrate of the protein. The enzyme strongly binds magnesium ions to acquire the right conformation and that it is isolated in a stable magnesium-containing form, unless cations are removed by a harsh treatment with a potent chelator Thermotoga maritima
3.6.1.1 NaCl NaCl produces a slight increase in activity Thermotoga maritima
3.6.1.1 NH4+ activity increases more than 6fold in the presence of KCl and NH4Cl in comparison with the activity measured in the absence of any monovalent cation Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.1 Thermotoga maritima Q9S5X0
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3.6.1.1 Thermotoga maritima DSM 3109 Q9S5X0
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.1 diphosphate + H2O no significant proton-translocation activity can be assayed in the total membrane fractions of pTVP-transformed yeast cells. This is probably due to the fact that the activity of the hyperthermophilic enzyme is negligible below 50-55°C. Above 50°C the high passive conductance of yeast membranes to protons makes it impossible to establish a reasonable pH gradient as demonstrated with V-PPases that hydrolyze PPi at these temperatures Thermotoga maritima 2 phosphate
-
 ?
3.6.1.1 diphosphate + H2O no significant proton-translocation activity can be assayed in the total membrane fractions of pTVP-transformed yeast cells. This is probably due to the fact that the activity of the hyperthermophilic enzyme is negligible below 50-55°C. Above 50°C the high passive conductance of yeast membranes to protons makes it impossible to establish a reasonable pH gradient as demonstrated with V-PPases that hydrolyze PPi at these temperatures Thermotoga maritima DSM 3109 2 phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.1.1 V-PPase
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 Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.1 70
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-
 Thermotoga maritima

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.6.1.1 60 85 60°C: about 50% of maximal activity, 85°C: about 65% of maximal activity Thermotoga maritima