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The E 1 /E 2 ‐Preference of Gastric H,K‐ATPase Mutants
Author(s) -
PONT JAN JOEP H. H. M.,
SWARTS HERMAN G. P.,
WILLEMS PETER H. G. M.,
KOENDERINK JAN B.
Publication year - 2003
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2003.tb07157.x
Subject(s) - preference , mutant , mutagenesis , atpase , chemistry , mutation , stereochemistry , biophysics , biochemistry , enzyme , biology , mathematics , gene , statistics
A bstract : Gastric H,K‐ATPase has, in the absence of ATP and added ions, a preference for the E 2 conformation. Mutations in the cation‐binding pocket often result in a preference for the E 1 ‐conformation. This can be paralleled by the occurrence of K + ‐ independent ATPase activity. These two phenomena could be separated by combined mutagenesis of several residues in and around the cation‐binding pocket. Models of the three‐dimensional structure of H,K‐ATPase visualize the relationship between the E 1 /E 2 preference and the structure.