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.

The site for GTP hydrolysis on the archaeal elongation factor 2 is unmasked by aliphatic alcohols

RAIMO, Gennaro;
1996

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.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11695/9401
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