Literature summary for 3.6.5.3 extracted from

Granata, V.; Graziano, G.; Ruggiero, A.; Raimo, G.; Masullo, M.; Arcari, P.; Vitagliano, L.; Zagari, A..
Stability against temperature of Sulfolobus solfataricus elongation factor 1alpha, a multi-domain protein (2008), Biochim. Biophys. Acta, 1784, 573-581.

Search for more literature for 3.6.5.3

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Saccharolobus solfataricus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	EF-1alpha shows GTPase activity and GDP-binding ability	Saccharolobus solfataricus	?	-	?

Synonyms

Synonyms	Comment	Organism
EF-1alpha	-	Saccharolobus solfataricus
elongation factor 1alpha	-	Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
20	100	EF-1alpha denaturation profile at pH 4.0, the protonation state of the numerous Asp and Glu residues plays a critical role for the thermally denatured state of the enzyme, reversibility of the inter-conversion between the two denatured forms, overview	Saccharolobus solfataricus

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Release 2023.1 (January 2023)