Significance of the Glutamate-139 Residue of the V-Type Na+-ATPase NtpK Subunit in Catalytic Turnover Linked with Salt Tolerance of Enterococcus hirae | Zendy

Miyuki KawanoKawada | Zendy; Hiroko Takahashi | Zendy; Kazuei Igarashi | Zendy; Takeshi Murata | Zendy; Ichiro Yamato | Zendy; Michio Homma | Zendy; Yoshihiko Kakinuma | Zendy

Open Access

Significance of the Glutamate-139 Residue of the V-Type Na+-ATPase NtpK Subunit in Catalytic Turnover Linked with Salt Tolerance of Enterococcus hirae

Author(s) -

Miyuki KawanoKawada,

Hiroko Takahashi,

Kazuei Igarashi,

Takeshi Murata,

Ichiro Yamato,

Michio Homma,

Yoshihiko Kakinuma

Publication year - 2011

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.01537-10

Subject(s) - enterococcus hirae , biology , protein subunit , atpase , biochemistry , sodium , residue (chemistry) , enzyme , mutant , enterococcus , chemistry , organic chemistry , gene , antibiotics

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.

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