Open AccessEffect of Atebrin on Bacterial Membrane Adenosine Triphosphatases in Relation to the Divalent Cation Used as Substrate and/or Activator
Author(s) -
J. Carreira,
Emilio Muñoz
Publication year - 1977
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.11.1.38
Subject(s) - divalent , atpase , enzyme , chemistry , biochemistry , activator (genetics) , escherichia coli , adenosine triphosphate , substrate (aquarium) , membrane , adenosine , biophysics , biology , organic chemistry , gene , ecology
The action of atebrin on purified adenosine triphosphatase (ATPase) fromMicrococcus lysodeikticus was studied as well as on the membrane-bound and soluble ATPases fromEscherichia coli andBacillus megaterium . Atebrin inhibited the Ca2+ -dependent activity of all these enzymes, and the inhibition was reversed by an excess of Ca2+ ions. Kinetic studies carried out with the purified enzyme fromM. lysodeikticus showed that the inhibition by atebrin was strongly cooperative, suggesting the complex nature of the process. On the other hand, atebrin stimulated the Mg2+ ATPase activity of theM. lysodeikticus enzyme, displacing its adenosine 5′-triphosphate (ATP)/Mg2+ optimum ratios, but inhibited the Mg2+ -ATPase activity ofE. coli provided that ATP was in excess over Mg2+ , i.e., that the ATP/Mg2+ ratio was higher than its optimum. These results suggest that divalent cations influence the bacterial ATPases in different ways depending on the type of divalent ion and/or enzyme. The effect of atebrin on bacterial ATPases may reflect those differences, and its complex mechanism of action might be related to the existence of more than one site for divalent cations and/or distinct conformational states in these enzymes.