Literature summary for 7.2.2.19 extracted from

Duerr, K.L.; Tavraz, N.N.; Zimmermann, D.; Bamberg, E.; Friedrich, T.
Characterization of Na,K-ATPase and H,K-ATPase enzymes with glycosylation-deficient beta-subunit variants by voltage-clamp fluorometry in Xenopus oocytes (2008), Biochemistry, 47, 4288-4297.

Search for more literature for 7.2.2.19

Cloned(Commentary)

Cloned (Comment)	Organism
expression of the wild-type H,K-ATPase, alpha- and beta-subunits, and glycosylation-deficient Asn-to-Gln beta-mutants in Xenopus laevis oocytes	Rattus norvegicus

Protein Variants

Protein Variants	Comment	Organism
additional information	the absence of the huge N-linked oligosaccharide moiety on the beta-subunit in the glycosylation-deficient Asn-to-Gln beta-mutants does not affect alpha/beta co-assembly, plasma membrane delivery or functional activity of the holoenzyme, differences in neither the voltage-dependent E1P/E2P ratio nor the kinetics of the E1P/E2P transition between holoenzymes comprising glycosylated and glycosylation-deficient beta-subunits, overview	Rattus norvegicus
N103Q	site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme	Rattus norvegicus
N130Q	site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme	Rattus norvegicus
N146Q	site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme	Rattus norvegicus
N161Q	site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme	Rattus norvegicus
N193Q	site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme	Rattus norvegicus
N225Q	site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme	Rattus norvegicus
N99Q	site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme	Rattus norvegicus

Inhibitors

Inhibitors	Comment	Organism	Structure
Omeprazole	-	Rattus norvegicus
SCH 28080	-	Rattus norvegicus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics, wild-type and mutant enzymes, overview	Rattus norvegicus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
plasma membrane	-	Rattus norvegicus	5886	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	N-linked glycosylation of beta-subunit, the absence of the huge N-linked oligosaccharide moiety on the beta-subunit in the glycosylation-deficient Asn-to-Gln beta-mutants does not affect alpha/beta co-assembly, plasma membrane delivery or functional activity of the holoenzyme, differences in neither the voltage-dependent E1P/E2P ratio nor the kinetics of the E1P/E2P transition between holoenzymes comprising glycosylated and glycosylation-deficient beta-subunits, overview	Rattus norvegicus

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant enzymes partially from Xenopus laevis oocytes by plasma membrane preparation	Rattus norvegicus

Source Tissue

Source Tissue	Comment	Organism	Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	activity measurement by voltage-clamp fluorometry	Rattus norvegicus

Subunits

Subunits	Comment	Organism
oligomer	-	Rattus norvegicus

Synonyms

Synonyms	Comment	Organism
H,K-ATPase	-	Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
22	-	assay at room temperature	Rattus norvegicus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Rattus norvegicus

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Release 2023.1 (January 2023)