Literature summary for 3.6.5.3 extracted from

Masullo, M.; Cantiello, P.; de Paola, B.; Catanzano, F.; Arcari, P.; Bocchini, V.
G13A substitution affects the biochemical and physical properties of the elongation factor 1 alpha. A reduced intrinsic GTPase activity is partially restored by kirromycin (2002), Biochemistry, 41, 628-633.

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Activating Compound

Activating Compound	Comment	Organism	Structure
kirromycin	enhances activity of mutant enzyme G13A (maximal stimulation at 0.04 mM), does not stimulate intrinsic GTPase of SsEF-1alpha triggered by 3.6 M NaCl	Saccharolobus solfataricus

Protein Variants

Protein Variants	Comment	Organism
G13A	compared to wild-type enzyme the mutant shows a reduced rate of Phe polymerization and a reduced intrinsic GTPase activity that is stimulated by high concentrations of NaCl. Mutant enzyme shows an increased affinity for GTP and GDP. The temperature inducing a 50% denaturation of the mutant enzyme is 5°C lower than that of the wild-type enzyme	Saccharolobus solfataricus

Inhibitors

Inhibitors	Comment	Organism	Structure
GDP	-	Saccharolobus solfataricus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0027	-	GTP	60°C, wild-type enzyme	Saccharolobus solfataricus
0.0046	-	GTP	60°C, mutant enzyme G13A	Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GTP + H2O	-	Saccharolobus solfataricus	GDP + phosphate	-	?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
80	-	mutant G13A	Saccharolobus solfataricus
90	-	wild-type enzyme	Saccharolobus solfataricus

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
70	95	70°C: about 60% of maximal activity, 95°C: about 90% of maximal activity, wild-type enzyme	Saccharolobus solfataricus
70	86	about 60% of maximal activity at 70°C and at 86°C, mutant enzyme G13A	Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
87	-	half-denaturation of mutant enzyme G13A	Saccharolobus solfataricus
91	-	10 min, 50% inactivation of GDP binding ability, mutant enzyme G13A	Saccharolobus solfataricus
92	-	half-denaturation of wild-type enzyme	Saccharolobus solfataricus
94	-	10 min, 50% inactivation of GDP binding ability, wild-type enzyme	Saccharolobus solfataricus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.00167	-	GTP	60°C, mutant enzyme G13A	Saccharolobus solfataricus
0.013	-	GTP	60°C, wild-type enzyme	Saccharolobus solfataricus

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.0008	-	GDP	60°C, wild-type enzyme	Saccharolobus solfataricus
0.0042	-	GDP	60°C, mutant enzyme G13A	Saccharolobus solfataricus

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Release 2023.1 (January 2023)