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Effect of divalent cations on the ATPase activity of Escherichia coli SecA
Author(s) -
Kim Joon-Sik,
Ahn Taeho,
Ko Junsang,
Park Chankyu,
Kim Hyoungman
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02265-7
Subject(s) - divalent , chemistry , atpase , enzyme , escherichia coli , biochemistry , cofactor , naphthalene , enzyme assay , biophysics , biology , organic chemistry , gene
It was found that Ca 2+ stimulates the intrinsic SecA ATPase activity in the absence as well as in the presence of liposome. On the other hand, Mg 2+ , the general cofactor for ATPase, did not affect the intrinsic SecA ATPase but reduced the portion of ATPase activity enhanced by Ca 2+ . The enhancement of SecA ATPase activity correlated well with the increase in 8‐anilino‐1‐naphthalene‐sulfonic acid binding of SecA, suggesting that increased exposure of hydrophobic residues stimulates the enzyme activity.