The A26G replacement in the consensus sequence A-X-X-X-X-G-K-[T,S] of the guanine nucleotide binding site activates the intrinsic GTPase of the elongation factor 2 from the archaeon Sulfolobus solfataricus.
De Vendittis E, Adinolfi BS, Amatruda MR, Raimo G, Masullo M, Bocchini V.
De Vendittis E, et al. Among authors: masullo m.
Eur J Biochem. 1999 Jun;262(2):600-5. doi: 10.1046/j.1432-1327.1999.00428.x.
Eur J Biochem. 1999.
PMID: 10336648
Free article.
In contrast, the A26G substitution enhanced the catalytic efficiency of the intrinsic SsEF-2 GTPase triggered by ethylene glycol [Raimo, G., Masullo, M., Scarano, G., & Bocchini, V. (1997) Biochimie 78, 832-837]. Surprisingly, A26GSsEF-2 was able to hydrolyse GT …
In contrast, the A26G substitution enhanced the catalytic efficiency of the intrinsic SsEF-2 GTPase triggered by ethylene glycol [Raimo, G., …