Requires Na+ and K+. This enzyme, found in some bacteria and archaea, couples the energy from diphosphate hydrolysis to active sodium translocation across the membrane. The enzyme is electrogenic, as the Na+ transport results in generation of a positive potential in the inner side of the membrane.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
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SYSTEMATIC NAME
IUBMB Comments
diphosphate phosphohydrolase (Na+-transporting)
Requires Na+ and K+. This enzyme, found in some bacteria and archaea, couples the energy from diphosphate hydrolysis to active sodium translocation across the membrane. The enzyme is electrogenic, as the Na+ transport results in generation of a positive potential in the inner side of the membrane.
enzyme does not catalyze oxygen exchange between phosphate and water. Solubilized HppA exhibits low but measurable PPi-synthesizing activity, which also requires Na+ but is inhibited by K+
enzyme exhibits an absolute requirement for Na+ but displays the highest activity in the presence of millimolar levels of both Na+ and K+. Two Na+ binding sites and one K+ binding site are involved in enzyme activation. In the absence of K+, Li+ may substitute for Na+
enzyme does not catalyze oxygen exchange between phosphate and water. Solubilized HppA exhibits low but measurable PPi-synthesizing activity, which also requires Na+ but is inhibited by K+
enzyme exhibits an absolute requirement for Na+ but displays the highest activity in the presence of millimolar levels of both Na+ and K+. Two Na+ binding sites and one K+ binding site are involved in enzyme activation. In the absence of K+, Li+ may substitute for Na+
enzyme exhibits an absolute requirement for Na+ but displays the highest activity in the presence of millimolar levels of both Na+ and K+. Two Na+ binding sites and one K+ binding site are involved in enzyme activation
enzyme catalyzes Na+ rather than H+ transport into Escherichia coli inner membrane vesicles. When assayed in uncoupled inner membrane vesicles, enzyme exhibits an absolute requirement for Na+ but displays the highest hydrolyzing activity in the presence of both Na+ and K+. Two Na+ binding sites are present in the protein. One of these sites can also bind K+, resulting in a 10fold increase in the affinity of the other site for Na+ and a 2fold increase in maximal velocity. The Na+ transport is accompanied by the generation of a positive inside membrane potential
enzyme catalyzes Na+ rather than H+ transport into Escherichia coli inner membrane vesicles. When assayed in uncoupled inner membrane vesicles, enzyme exhibits an absolute requirement for Na+ but displays the highest hydrolyzing activity in the presence of both Na+ and K+. Two Na+ binding sites are present in the protein. One of these sites can also bind K+, resulting in a 10fold increase in the affinity of the other site for Na+ and a 2fold increase in maximal velocity. The Na+ transport is accompanied by the generation of a positive inside membrane potential
enzyme catalyzes Na+ rather than H+ transport into Escherichia coli inner membrane vesicles. When assayed in uncoupled inner membrane vesicles, enzyme exhibits an absolute requirement for Na+ but displays the highest hydrolyzing activity in the presence of both Na+ and K+. Two Na+ binding sites are present in the protein. One of these sites can also bind K+, resulting in a 10fold increase in the affinity of the other site for Na+ and a 2fold increase in maximal velocity. The Na+ transport is accompanied by the generation of a positive inside membrane potential
enzyme catalyzes Na+ rather than H+ transport into Escherichia coli inner membrane vesicles. When assayed in uncoupled inner membrane vesicles, enzyme exhibits an absolute requirement for Na+ but displays the highest hydrolyzing activity in the presence of both Na+ and K+. Two Na+ binding sites are present in the protein. One of these sites can also bind K+, resulting in a 10fold increase in the affinity of the other site for Na+ and a 2fold increase in maximal velocity. The Na+ transport is accompanied by the generation of a positive inside membrane potential
enzyme catalyzes Na+ rather than H+ transport into Escherichia coli inner membrane vesicles. When assayed in uncoupled inner membrane vesicles, enzyme exhibits an absolute requirement for Na+ but displays the highest hydrolyzing activity in the presence of both Na+ and K+. Two Na+ binding sites are present in the protein. One of these sites can also bind K+, resulting in a 10fold increase in the affinity of the other site for Na+ and a 2fold increase in maximal velocity. The Na+ transport is accompanied by the generation of a positive inside membrane potential
enzyme belongs to a monophyletic clade comprising Na+-transporting PPases within the K+-dependent subfamily. A specific Glu residue located in the cytoplasm-membrane interface of transmembrane helix 6 appears to be central in the transport mechanism
enzyme belongs to a monophyletic clade comprising Na+-transporting PPases within the K+-dependent subfamily. A specific Glu residue located in the cytoplasm-membrane interface of transmembrane helix 6 appears to be central in the transport mechanism
enzyme belongs to a monophyletic clade comprising Na+-transporting PPases within the K+-dependent subfamily. A specific Glu residue located in the cytoplasm-membrane interface of transmembrane helix 6 appears to be central in the transport mechanism
enzyme belongs to a monophyletic clade comprising Na+-transporting PPases within the K+-dependent subfamily. A specific Glu residue located in the cytoplasm-membrane interface of transmembrane helix 6 appears to be central in the transport mechanism
enzyme is able to complement a yeast mutant lacking cytosolic soluble diphosphatase IPP1 and acts also under salt stress. When yeast cells expressing HppA1 are grown in the presence of NaCl only a marginal increase in their internal PPi levels is observed with respect to control cells
inverted membrane vesicles of Acetobacter woodii have a membrane-bound diphosphatase that catalyzes diphosphate hydrolysis. Hydrolysis of diphosphate is accompanied by Na+ transport into the lumen of the inverted membrane vesicles. Na+ transport is primary and electrogenic
enzyme is able to complement a yeast mutant lacking cytosolic soluble diphosphatase IPP1 and acts also under salt stress. When yeast cells expressing HppA1 are grown in the presence of NaCl only a marginal increase in their internal PPi levels is observed with respect to control cells
The H+-translocating inorganic pyrophosphatase from Arabidopsis thaliana is more sensitive to sodium than its Na+-translocating counterpart from Methanosarcina mazei