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7.2.2.1: Na+-transporting two-sector ATPase

This is an abbreviated version!
For detailed information about Na+-transporting two-sector ATPase, go to the full flat file.

Word Map on EC 7.2.2.1

Reaction

ATP
+
H2O
 + n Na+[side 1] =
ADP
 +
phosphate
 + n Na+[side 2]

Synonyms

A1AO ATP synthase, ATP phosphohydrolase (Na+-transporting), ATP synthase, EC 3.6.3.15, F-type ATP synthase, F1FO-ATPase, KPA1, Lipid-binding protein, Na+ pump, Na+ V-ATPase, Na+(Li+, K+)/H+ antiporter, Na+-ATPase, Na+-translocating ATPase, Na+-translocating F1FO-ATPase, Na+-translocating V-ATPase, Na+-transporting FoF1 ATP synthase, Na+-transporting P-type ATPase, Na+-transporting two-sector ATPase, Na+-transporting V-ATPase, Ntp, sodium ion-pumping adenosine triphosphatase, UmpAB, V-ATPase, V-type Na+-ATPase, vacuolar Na+-translocating ATPase, vacuolar-type Na+-ATPase, vacuolar-type Na+-translocating ATPase, vacuole-type ATPase

ECTree

     7 Translocases
         7.2 Catalysing the translocation of inorganic cations
             7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
                7.2.2.1 Na+-transporting two-sector ATPase

Engineering

Engineering on EC 7.2.2.1 - Na+-transporting two-sector ATPase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A236C
R573E
-
inactive mutant
R573K
-
mutant can grow in alcaline medium
R573L
-
inactive mutant
R573Q
-
inactive mutant
A214C
-
N-ethylmaleimide significantly inhibits ATP synthesis (18%) and hydrolysis as well as proton pumping activities of the enzyme
A218C
-
N-ethylmaleimide significantly inhibits ATP synthesis (19%) and hydrolysis as well as proton pumping activities of the enzyme
E216C
-
the mutant is not inhibited by N-ethylmaleimide
F217C
-
the mutant shows wild type activity also in the presence of N-ethylmaleimide
G215C
-
N-ethylmaleimide significantly inhibits ATP synthesis (42%) and hydrolysis as well as proton pumping activities of the enzyme
I223C
-
N-ethylmaleimide significantly inhibits ATP synthesis (45%) and hydrolysis as well as proton pumping activities of the enzyme
K219C
-
N-ethylmaleimide significantly inhibits ATP synthesis activity (43%) of the enzyme
N222C
-
N-ethylmaleimide significantly inhibits ATP synthesis and hydrolysis as well as proton pumping activities of the enzyme
N230C
-
N-ethylmaleimide significantly inhibits ATP synthesis (38%) and hydrolysis as well as proton pumping activities of the enzyme
P220C
-
the mutant shows about wild type activity also in the presence of N-ethylmaleimide
T221C
-
N-ethylmaleimide significantly inhibits ATP synthesis and hydrolysis as well as proton pumping activities of the enzyme
additional information
-
mutant with a lesion in membrane Na+-translocation is neither inhibited by dicyclohexylcarbodiimide nor stimulated by Na+