Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 7.1.2.1 extracted from

  • Serrano, R.; Portillo, F.
    Catalytic and regulatory sites of yeast plasma membrane H+-ATPase studied by directed mutagenesis (1990), Biochim. Biophys. Acta, 1018, 195-199.
    View publication on PubMed
Search for more literature for 7.1.2.1

Protein Variants

Protein Variants Comment Organism
C376L mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 65% of the activity of the wild type enzyme, 5fold increase in Ki for vanadate Saccharomyces cerevisiae
D226N decreased turnover and level of phosphorylated enzyme-intermediate Saccharomyces cerevisiae
D226N 5% decrease in ATPase activity, 35% decrease in H+ transport Saccharomyces cerevisiae
D378E 5fold lower Ki for vanadate than in wild type Saccharomyces cerevisiae
D378E no decrease in ATPase activity, 65% decrease in H+ transport Saccharomyces cerevisiae
D378N 5fold lower Ki for vanadate than in wild type Saccharomyces cerevisiae
D378T about 3fold lower Ki for vanadate than in wild type Saccharomyces cerevisiae
D378T 20% decrease in ATPase activity, 85% decrease in H+ transport Saccharomyces cerevisiae
D534N mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 10% of the activity of the wild type enzyme Saccharomyces cerevisiae
D560N mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 5% of the activity of the wild type enzyme Saccharomyces cerevisiae
D634N slow turnover, increased level of phosphorylated enzyme-intermediate, 10fold increase in Ki for vanadate Saccharomyces cerevisiae
D638N mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 5% of the activity of the wild type enzyme Saccharomyces cerevisiae
D730N increased level of phosphorylated enzyme-intermediate Saccharomyces cerevisiae
E233Q no turnover, increased level of phosphorylated enzyme-intermediate Saccharomyces cerevisiae
E233Q 70% decrease in ATPase activity, 85% decrease in H+ transport Saccharomyces cerevisiae
K379Q mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 70% of the activity of the wild type enzyme Saccharomyces cerevisiae
K379Q abour 3fold lower Ki for vanadate than in wild type Saccharomyces cerevisiae
K474H mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 10% of the activity of the wild type enzyme Saccharomyces cerevisiae
K474Q mutation decreases activity and phosphorylation to a similar extent, ATPase activity is less than 5% of the activity of the wild type enzyme Saccharomyces cerevisiae
K474R mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 30% of the activity of the wild type enzyme Saccharomyces cerevisiae
P335A 30% decrease in ATPase activity, 60% decrease in H+ transport Saccharomyces cerevisiae
S234A 3.5fold increase in ATPase activity, 20% decrease in H+ transport Saccharomyces cerevisiae
T231G greatly increased level of phosphorylated enzyme-intermediate, 30fold higher Ki for vanadate Saccharomyces cerevisiae

Localization

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

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