Effect of divalent cations on the ATPase activity of Escherichia coli SecA

Citation
Js. Kim et al., Effect of divalent cations on the ATPase activity of Escherichia coli SecA, FEBS LETTER, 493(1), 2001, pp. 12-16
Citations number
24
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
0014-5793 → ACNP
Volume
493
Issue
1
Year of publication
2001
Pages
12 - 16
Database
ISI
SICI code
0014-5793(20010323)493:1<12:EODCOT>2.0.ZU;2-K
Abstract
It was found that Ca2+ stimulates the intrinsic SecA ATPase activity in the absence as well as in the presence of liposome, On the other hand, Mg2+, t he general cofactor for ATPase. did not affect the intrinsic SecA ATPase bu t reduced the portion of ATPase activity enhanced by. Ca2+. The enhancement of SecA ATPase activity correlated well with the increase in 8-anilino-1-n aphthalene-sulfonic acid binding of SecA, suggesting that increased exposur e of hydrophobic residues stimulates the enzyme activity. (C) 2001 Publishe d by Elsevier Science B.V. on behalf of the Federation of European Biochemi cal Societies.