Abstract
An appropriate mixture of ethylene glycol and BaCl2 enhanced the otherwise very low intrinsic GTPase activity of the elongation factor 2 isolated from the archaeon Sulfolobus solfataricus (SsEF-2). The enzymatic activity became up to 300-fold higher than that of the SsEF-2 GTPase measured in the absence of any stimulator, but remained 20-fold lower than that stimulated by ribosome. The stimulatory effect of ethylene glycol/Ba2+ was attributed to the increased affinity for GTP, probably related to a conformational change occurring in a hydrophobic region near the catalytic site.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adenosine Diphosphate Ribose
-
Alcohols / pharmacology*
-
Barium Compounds / pharmacology
-
Binding Sites
-
Cations, Divalent / pharmacology
-
Chlorides / pharmacology
-
Ethylene Glycol
-
Ethylene Glycols / pharmacology
-
GTP Phosphohydrolase-Linked Elongation Factors / metabolism
-
GTP-Binding Proteins / metabolism
-
Guanosine Diphosphate / pharmacology
-
Guanosine Triphosphate / metabolism*
-
Guanosine Triphosphate / pharmacology
-
Guanylyl Imidodiphosphate / metabolism
-
Guanylyl Imidodiphosphate / pharmacology
-
Hydrogen-Ion Concentration
-
Hydrolysis
-
Peptide Elongation Factor 2
-
Peptide Elongation Factors / drug effects
-
Peptide Elongation Factors / metabolism*
-
Sulfolobus / enzymology*
-
Temperature
Substances
-
Alcohols
-
Barium Compounds
-
Cations, Divalent
-
Chlorides
-
Ethylene Glycols
-
Peptide Elongation Factor 2
-
Peptide Elongation Factors
-
barium chloride
-
Guanosine Diphosphate
-
Adenosine Diphosphate Ribose
-
Guanylyl Imidodiphosphate
-
Guanosine Triphosphate
-
GTP Phosphohydrolase-Linked Elongation Factors
-
GTP-Binding Proteins
-
Ethylene Glycol