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Literature summary for 7.1.3.1 extracted from

  • Hedrich, R.; Kurkdjian, A.; Guern, J.; Fluegge, U.I.
    Comparative studies on the electrical properties of the H+ translocating ATPase and pyrophosphatase of the vacuolar-lysosomal compartment (1989), EMBO J., 8, 2835-2841 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.1.3.1

Inhibitors

Inhibitors Comment Organism Structure
diphosphate progressive inhibition above 0.15 mM Beta vulgaris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.015 0.02 diphosphate at pH 8.0 and 20°C Beta vulgaris

Localization

Localization Comment Organism GeneOntology No. Textmining
vacuole
-
 Beta vulgaris 5773
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the enzyme is activated by MgATP or inorganic Mg diphosphate Beta vulgaris

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diphosphate + H2O + H+[side 1] Beta vulgaris
-
 2 phosphate + H+[side 2]
-
 ?

Organism

Organism UniProt Comment Textmining
Beta vulgaris
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
root
-
 Beta vulgaris
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + H2O + H+[side 1]
-
 Beta vulgaris 2 phosphate + H+[side 2]
-
 ?

Synonyms

Synonyms Comment Organism
H+ translocating pyrophosphatase
-
 Beta vulgaris

General Information

General Information Comment Organism
physiological function the enzyme transports protons into the vacuole and polarizes the membrane potential (positive inside the vacuole). The electrochemical gradient provided by the enzyme stimulates effectively the uptake of various metabolites such as malate, citrate and sucrose Beta vulgaris