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Literature summary for 7.1.2.1 extracted from

  • Petrov, V.V.
    Point mutations in Pma1 H+-ATPase of Saccharomyces cerevisiae: influence on its expression and activity (2010), Biochemistry, 75, 1055-1063.
    View publication on PubMed
Search for more literature for 7.1.2.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Saccharomyces cerevisiae NY13 cells Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E803A 15% ATPase and 13% H+ transport activity compared to the wild type enzyme. The mutation has no significant influence on the ATPase and cell sensitivity to heat shock. However, it causes a shift in the equilibrium between E1 and E2 conformations of the enzyme towards E1 Saccharomyces cerevisiae
F796A 4% ATPase and no H+ transport activity compared to the wild type enzyme. The mutation causes enzyme and cell sensitivity to heat shock when expressed in secretory vesicles Saccharomyces cerevisiae
I794A 4% ATPase and no H+ transport activity compared to the wild type enzyme. The mutation increases temperature sensitivity of cells when the enzyme is expressed either in secretory vesicles or, to a lesser extent, in plasma membrane Saccharomyces cerevisiae
I799A 2% ATPase and no H+ transport activity compared to the wild type enzyme. The mutation is lethal for cells regardless of expression of the enzyme in secretory vesicles or plasma membrane Saccharomyces cerevisiae
I807A 11% ATPase and no H+ transport activity compared to the wild type enzyme Saccharomyces cerevisiae
L797A 20% ATPase and 17% H+ transport activity compared to the wild type enzyme Saccharomyces cerevisiae
L801A 7% ATPase and no H+ transport activity compared to the wild type enzyme Saccharomyces cerevisiae
Q798A 1% ATPase and no H+ transport activity compared to the wild type enzyme. The mutation is lethal for cells regardless of expression of the enzyme in secretory vesicles or plasma membrane Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
orthovanadate
-
 Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.7
-
 ATP mutant enzyme E803A, at pH 5.7 and 30°C Saccharomyces cerevisiae
0.7
-
 ATP mutant enzyme L797A, at pH 5.7 and 30°C Saccharomyces cerevisiae
1.4
-
 ATP wild type enzyme, at pH 5.7 and 30°C Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane
-
 Saccharomyces cerevisiae 5886
-
secretory vesicle
-
 Saccharomyces cerevisiae 99503
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae SY4
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Saccharomyces cerevisiae ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in
-
 Saccharomyces cerevisiae SY4 ADP + phosphate + H+/out
-
 ?

Synonyms

Synonyms Comment Organism
H+-ATPase
-
 Saccharomyces cerevisiae
PMA1
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function H+-ATPase is a key enzyme of cell metabolism generating electrochemical proton gradient across the plasma membrane, thus playing an important role in the maintenance of ion homeostasis in the cell Saccharomyces cerevisiae