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Literature summary for 7.2.2.19 extracted from

  • Duerr, K.L.; Seuffert, I.; Friedrich, T.
    Deceleration of the E1P-E2P transition and ion transport by mutation of potentially salt bridge-forming residues Lys-791 and Glu-820 in gastric H+/K+-ATPase (2010), J. Biol. Chem., 285, 39366-39379.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.2.2.19

Cloned(Commentary)

Cloned (Comment) Organism
expression of the beta-subunit and a modified form of the alpha-subunit with a single cysteine replacement in the TM5/TM6 extracellular loop, i.e. S806C, in Xenopus laevis oocytes Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
E820A site-directed mutagenesis, shows altered pH dependence compared to the wild-type enzyme Rattus norvegicus
E820D site-directed mutagenesis, charge-conserving mutation, slight preference of the mutants for the E2P state, shows no altered pH dependence compared to the wild-type enzyme Rattus norvegicus
E820K site-directed mutagenesis, charge-inverting mutation, no shift in the conformational distribution toward E1P Rattus norvegicus
E820Q site-directed mutagenesis, shows altered pH dependence compared to the wild-type enzyme Rattus norvegicus
K791A site-directed mutagenesis, charge-neutralizing amino acid replacement, insertion of the Lys791 mutations into the backbone of H,KATPase mutant S806C, which carries a reporter cysteine for site-specific fluorescence labeling. The mutation causes a conformational shift toward the E1P-state and a shift to more positive potentials compared with the wild-type Rattus norvegicus
K791E site-directed mutagenesis, charge-inverting mutation, insertion of the Lys791 mutations into the backbone of H,KATPase mutant S806C, which carries a reporter cysteine for site-specific fluorescence labeling. The mutation causes a conformational shift toward the E1P-state and a shift to more positive potentials compared with the wild-type Rattus norvegicus
K791R site-directed mutagenesis, charge-inverting mutation, insertion of the Lys791 mutations into the backbone of H,KATPase mutant S806C, which carries a reporter cysteine for site-specific fluorescence labeling. The mutation causes a conformational shift toward the E1P-state and a shift to more positive potentials compared with the wild-type Rattus norvegicus
K791S site-directed mutagenesis, charge-neutralizing amino acid replacement, insertion of the Lys791 mutations into the backbone of H,KATPase mutant S806C, which carries a reporter cysteine for site-specific fluorescence labeling. The mutation causes a conformational shift toward the E1P-state and a shift to more positive potentials compared with the wild-type Rattus norvegicus
additional information inversion of the salt bridge polarity does not rescue function does not necessarily exclude that Lys791 and Glu820 in the wild-type proton pump interact in an E2P-stabilizing manner Rattus norvegicus
S806C a single cysteine replacement in the TM5/TM6 extracellular loop of the alpha-subunit. The S806C mutation enables site-specific labeling of H,K-ATPase with the environmentally sensitive fluorophore TMRM, the S806C mutation does not affect the transport properties of gastric H,K-ATPase Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
SCH28080 a K+-competitive inhibitor, SCH28080 is specific for both E2 and E2P conformations Rattus norvegicus
vanadate interacts specifically with the E2 conformational state Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane transmembrane enzyme Rattus norvegicus 5886
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in + K+/out Rattus norvegicus
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 ADP + phosphate + H+/out + K+/in
-
 ir

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P09626
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein reversible phosphorylation of a highly conserved Asp residue, a hallmark of all P-type ATPases, is coupled to the transition between two principal conformational states and the corresponding phosphointermediates Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
gastrointestinal tract
-
 Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in + K+/out
-
 Rattus norvegicus ADP + phosphate + H+/out + K+/in
-
 ir
ATP + H2O + H+/in + K+/out cation binding sites in the transmembrane domains TM42 to TM6, E2-conformation-specific salt bridge between the side chains of Lys791 in TM5 and Glu820 in TM6 of the cation binding pocket Rattus norvegicus ADP + phosphate + H+/out + K+/in
-
 ir
additional information activity tests of the recombinantly expressed enzyme by Rb+ uptake measurements, and voltage clamp fluorometry for site-specific labeling of H,KATPase-expressing TMRM-labeled oocytes Rattus norvegicus ?
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 ?

Subunits

Subunits Comment Organism
More homology model of the gastric H,K-ATPase in the E2 state Rattus norvegicus

Synonyms

Synonyms Comment Organism
H+/K+-ATPase
-
 Rattus norvegicus
H,K-ATPase
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 Rattus norvegicus

General Information

General Information Comment Organism
evolution the ubiquitous Na,K-ATPase and the gastric H,K-ATPase belong to the PIIC subgroup of the extensive class of P-type ATPases, which use ATP hydrolysis for active transport of cations. A lysine residue within the highly conserved center of the fifth transmembrane segment in PIIC-type ATPase alpha-subunits is uniquely found in H,K-ATPases instead of a serine in all Na,K-ATPase, EC 3.6.3.9, isoforms Rattus norvegicus