Possible Involvement of Cysteine and Histidine Residues in the (NH4
+ + Na+)-Activated ATPase of an Anaerobic Alkaliphile, Amphibacillus xylanus |
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Authors: | Yoshikane Okano Takahiro Maeki Noriyuki Koyama |
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Institution: | (1) Department of Chemistry, Faculty of Science, Chiba University, Yayoi, Chiba 263, Japan , JP |
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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.
Received: 2 June 1997 / Accepted: 7 July 1997 |
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