Mutation of His 834 in human anion exchanger 1 affects substrate binding

Biochimica Et Biophysica Acta
Shinya TakazakiN Hamasaki

Abstract

Anion exchanger 1 (AE1 or band 3) is responsible for Cl(-)-HCO3(-) exchange on erythrocyte membrane. Previously, we showed that band 3 is fixed in an inward-facing conformation by specific modification of His 834 with DEPC, resulting in a strong inhibition of its anion transport activity. To clarify the physiological role of His 834, we evaluated the sulfate transport activities of various band 3 mutants: different mutants at His 834 and alanine mutants of peripheral residues around 834 (Lys 829-Phe 836) in yeast cell membranes. The K(m) values of the His 834 mutants were 4-10 times higher than that of the wild type, while their V(max) values were barely lower than that of wild type. Meanwhile, the K(m) values of the peripheral alanine mutants were only slightly increased. These data suggest that His 834 is critically important for the efficient binding of sulfate anion, but not for the conformational change induced by substrate binding.

References

Dec 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·S E LuxH F Lodish
Jan 13, 2001·Vox Sanguinis·N Hamasaki, M Yamamoto
Nov 26, 2002·The Journal of Biological Chemistry·Quansheng ZhuJoseph R Casey
Jul 23, 2004·Journal of Biochemistry·Yoshito AbeNaotaka Hamasaki
Jun 6, 2006·Journal of Biochemistry·Shinya TakazakiNaotaka Hamasaki

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Citations

Apr 16, 2013·Journal of Molecular Biology·Pamela BonarJoseph R Casey
Dec 14, 2011·Biochimica Et Biophysica Acta·Shinya TakazakiNaotaka Hamasaki

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