Membrane-associated ATPase from Zymomonas mobilis; purification and characterization.
The major ATPase (adenosinetriphosphatase, EC 3.6.1.3) activity present in the membrane of Zymomonas mobilis has been isolated, using a novel combination of multifunctional hydrophobic adsorbents. On subjecting the preparation to gel filtration, activity was lost, but could be restored by reconstituting fractions from the column. Subunit composition of the fractions indicated that the Zymomonas mobilis ATPase is of the F0F1 type, and so is probably involved in proton pumping. The contribution of this ATPase to the overall ATP turnover in the cells has been calculated to be approximately 20% and so it may be partly responsible for the phenomenon of 'uncoupled growth' observed with Zymomonas mobilis.
Reyes
L
L
Centre for Protein and Enzyme Technology, La Trobe University, Bundoora, Vic., Australia.
Scopes
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RK
D000251:Adenosine Triphosphatases / Q000302:isolation & purification*; D001421:Bacteria, Anaerobic / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics
D000251:Adenosine Triphosphatases