Abstract.
Effect of various inhibitors on the (NH4 + + Na+)-activated ATPase of an anaerobic alkaliphile, Ep01(a strain of Amphibacillus xylanus), was examined. Among the chemicals tested, the enzyme was drastically inactivated by p-chloromercuribenzoic acid and diethyl pyrocarbonate. The ATPase activity of the enzyme, which was inactivated by p-chloromercuribenzoic acid and diethyl pyrocarbonate, was remarkably restored by β-mercaptoethanol and hydroxylamine, respectively, suggesting the involvement of cysteine and histidine residues in the enzyme activity. Analysis of the inhibition kinetics by diethyl pyrocarbonate indicated that modification of a single histidine residue per ATPase molecule was sufficient to inactivate the enzyme.
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Received: 2 June 1997 / Accepted: 7 July 1997
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Okano, Y., Maeki, T. & Koyama, N. Possible Involvement of Cysteine and Histidine Residues in the (NH4 + + Na+)-Activated ATPase of an Anaerobic Alkaliphile, Amphibacillus xylanus . Curr Microbiol 36, 9–12 (1998). https://doi.org/10.1007/s002849900271
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DOI: https://doi.org/10.1007/s002849900271