PMID:11277996
| Citation |
Kim, J, Ahn, T, Ko, J, Park, C and Kim, H (2001) Effect of divalent cations on the ATPase activity of Escherichia coli SecA. FEBS Lett. 493:12-6 |
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| Abstract |
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. |
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| Keywords |
Adenosine Triphosphatases/metabolism; Anilino Naphthalenesulfonates/pharmacology; Bacterial Proteins; Calcium/metabolism; Calcium Chloride/pharmacology; Carrier Proteins/metabolism; Cations; Cell Membrane/metabolism; Chelating Agents/pharmacology; Dose-Response Relationship, Drug; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins; Fluorescent Dyes/pharmacology; Kinetics; Ligands; Liposomes/metabolism; Magnesium/metabolism; Membrane Transport Proteins; Protein Binding; Temperature |
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