Literature summary for 1.13.12.5 extracted from

Liyaghatdar, Z.; Emamzadeh, R.; Rasa, S.M.M.; Nazari, M.
Trehalose radial networks protect Renilla luciferase helical layers against thermal inactivation (2017), Int. J. Biol. Macromol., 105, 66-73 .

Search for more literature for 1.13.12.5

Application

Application	Comment	Organism
molecular biology	Renilla luciferase (Rluc) from Renilla reniformis is an appropriate protein reporter for the detection of specific molecular targets due to its bioluminescent feature, although its relatively low stability limits the application	Renilla reniformis

Cloned(Commentary)

Cloned (Comment)	Organism
gene luc, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)	Renilla reniformis

General Stability

General Stability	Organism
trehalose a thermostabilizing effect, a wide radial like network of trehalose molecules supports alpha-helix structures that are located in the N-terminus and C-terminus of the protein. In the water simulation box, these helices alter to instable structures at high temperatures. Reduction of the fluctuation of these helices in the presence of trehalose molecules, may prevent the protein from unfolding and increase its shelf-life	Renilla reniformis

Organism

trehalose a thermostabilizing effect, a wide radial like network of trehalose molecules supports alpha-helix structures that are located in the N-terminus and C-terminus of the protein. In the water simulation box, these helices alter to instable structures at high temperatures. Reduction of the fluctuation of these helices in the presence of trehalose molecules, may prevent the protein from unfolding and increase its shelf-life

Renilla reniformis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	effects of trehalose and sucrose as chemical chaperones on the kinetic stability of Rluc, activity of the enzyme in presence of these additives at high temperatures, mechanism of stability, molecular dynamic simulation, modeliing, overview	Renilla reniformis

Organism

Organism	UniProt	Comment	Textmining
Renilla reniformis	P27652	-	-

Subunits

Subunits	Comment	Organism
More	Rluc has an alpha/beta-hydrolase fold that consists of 6 helices sur-rounding the catalytic triad in the center of the enzyme. Structure analysis at 30-40°C in absence or presence of sugars, structure comparison, overview	Renilla reniformis

Synonyms

Synonyms	Comment	Organism
Renilla luciferase	-	Renilla reniformis
RLuc	-	Renilla reniformis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
32	-	-	Renilla reniformis

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
20	50	activity range, purified enzyme in absence of trehalose or sucrose	Renilla reniformis
20	60	activity range, purified enzyme in presence of 1.2 M trehalose or sucrose	Renilla reniformis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
30	-	Rluc remaining activity in the absence and presence of 0.6 M and 1.2 M of trehalose, and 1.2 M of sucrose at 30°C is 15%, about 50%, around 100%, and almost 60%, respectively, after 60 min	Renilla reniformis
40	-	in the absence and presence of 0.6 M of trehalose, the remaining activity is only about 2% and 6%, respectively, although it increases about 70fold upon incubation of the enzyme solution in a buffer containing 1.2 M of trehalose. It also seems that the remaining activity in the presence of 1.2 M of sucrose in the first 10 min is slightly better than in its absence, and a little activity is seen even after 60 min	Renilla reniformis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Renilla reniformis