Possible involvement of a single histidine residue in the P-type Na+-ATPase of a facultatively anaerobic alkaliphile, Exiguobacterium aurantiacum.
Effect of various inhibitors on the P-type Na+-ATPase of a facultatively anaerobic alkaliphile, Exiguobacterium aurantiacum, was examined. The ATPase was extremely sensitive to p-chloromercuriphenylsulfonic acid, a modifier of SH-group. The enzyme was also sensitive to diethylpyrocarbonate, and analysis of the inhibition kinetics by the drug indicated that modification of a single histidine residue per ATPase molecule was sufficient to inactivate the enzyme.
Hirano
A
A
Department of Chemistry, Faculty of Science, Chiba University, Yayoi, Inage-ku, Chiba 263-8522, Japan.
Koyama
N
N
D002731:4-Chloromercuribenzenesulfonate / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D001421:Bacteria, Anaerobic / Q000201:enzymology*; D027682:Cation Transport Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D004047:Diethyl Pyrocarbonate / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006639:Histidine / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration
D027682:Cation Transport Proteins; D004791:Enzyme Inhibitors; D006639:Histidine; D002731:4-Chloromercuribenzenesulfonate; D000251:Adenosine Triphosphatases; C021838:sodium-translocating ATPase; D004047:Diethyl Pyrocarbonate