title: Significance of the glutamate-139 residue of the V-type Na+-ATPase NtpK subunit in catalytic turnover linked with salt tolerance of Enterococcus hirae.
abstract: A Glu139Asp mutant of the NtpK subunit (kE139D) of Enterococcus hirae vacuolar-type ATPase (V-ATPase) lost tolerance to sodium but not to lithium at pH 10. Purified kE139D V-ATPase retained relatively high specific activity and affinity for the lithium ion compared to the sodium ion. The kE139 residue of V-ATPase is indispensable for its enzymatic activity that is linked with the salt tolerance of enterococci.
authors: Integrated Center for Sciences, Ehime University, Matsuyama, Japan1; Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, Japan.
authors: Miyuki
authors: M
authors: Kawano-Kawada
authors: Hiroko
authors: H
authors: Takahashi
authors: Kazuei
authors: K
authors: Igarashi
authors: Takeshi
authors: T
authors: Murata
authors: Ichiro
authors: I
authors: Yamato
authors: Michio
authors: M
authors: Homma
authors: Yoshimi
authors: Y
authors: Kakinuma
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