Literature summary for 7.1.2.2 extracted from

Chaban, Y.L.; Coskun, U.; Keegstra, W.; Oostergetel, G.T.; Boekema, E.J.; Grueber, G.
Structural characterization of an ATPase active F1-/V1 -ATPase (alpha3beta3EG) hybrid complex (2004), J. Biol. Chem., 279, 47866-47870.

Search for more literature for 7.1.2.2

Application

Application	Comment	Organism
additional information	formation of an active alpha3beta3EG hybrid complex by co-reconstitution of subunits alpha and beta of the F1-ATPase and of subunits E and G of Saccharomyces cerevisiae V-ATPase, the coupling subunit gamma inside the alpha3beta3 oligomer of F1 can be effectively replaced by subunit E of the V-ATPase, the E and gamma subunit are structurally similiar, but their genes do not show homology	Bacillus sp. (in: Bacteria)

Organism

Organism	UniProt	Comment	Textmining
Bacillus sp. (in: Bacteria)	-	-	-
Bacillus sp. (in: Bacteria) PS3	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
alpha and beta subunits of F1-ATPase	Bacillus sp. (in: Bacteria)

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
11	-	subunits alpha and beta of the F1-ATPase	Bacillus sp. (in: Bacteria)
29	-	alpha3beta3EG hybrid complex, shows 53% of the complete F1-ATPase activity	Bacillus sp. (in: Bacteria)
31	-	alpha3beta3EG hybrid complex	Bacillus sp. (in: Bacteria)
54	-	complete F1-ATPase	Bacillus sp. (in: Bacteria)

Synonyms

Synonyms	Comment	Organism
F1-ATPase	-	Bacillus sp. (in: Bacteria)

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Release 2023.1 (January 2023)