Membrane-reversible H+-ATPase from Micrococcus lysodeikticus.
Treatment of phosphorylating fragments of bacterial membrane from Micrococcus lysodeikticus with trypsin leads to increase ATPase activity. As a result of this treatment, the membrane fragments acquire the ability to transform the ATP energy into transmembrane difference in potential. Dithiothreitol has a similar effect to that of trypsin on the membrane fragments from M. lysodeikticus. Dicyclohexylcarbodimide inhibits ATPase of the membrane fragments of M. lysodeikticus, and also the ATPase-reaction-coupled generation of membrane potential. It has been suggested that the increased ATPase activity of membranes from M. lysodeikticus during treatment with trypsin and dithiothreitol is connected with the effect of these agents on the protein inhibitor of ATPase.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology / Q000502:physiology; D003486:Cyanides / Q000494:pharmacology; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008293:Malates / Q000378:metabolism; D008564:Membrane Potentials; D008837:Micrococcus / Q000187:drug effects / Q000201:enzymology* / Q000502:physiology; D010085:Oxidative Phosphorylation; D010101:Oxygen Consumption
D003486:Cyanides; D008293:Malates; D004024:Dicyclohexylcarbodiimide; D000251:Adenosine Triphosphatases