Literature summary for 1.13.12.7 extracted from

Viviani, V.R.; Pelentir, G.F.; Oliveira, G.; Tomazini, A.; Bevilaqua, V.R.
Role of E270 in pH- and metal-sensitivities of firefly luciferases (2020), Photochem. Photobiol. Sci., 19, 1548-1558 .

Search for more literature for 1.13.12.7

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli BL21-DE3 cells	Amydetes vivianii

Protein Variants

Protein Variants	Comment	Organism
E270A	the mutation drastically decreases the spectral pH-sensitivity, and extends the activity profile above pH 9.0. These mutations also decrease the sensitivity to metals such as zinc, mercury and cadmium. The mutation may unwind a turn of the alpha-helix-10, indirectly increasing the interaction of the pH-sensor and other residues at the bottom of the luciferin binding site, stabilizing the green light emitting conformation	Amydetes vivianii
E270G	the mutation drastically decreases the spectral pH-sensitivity, and extends the activity profile above pH 9.0. These mutations also decrease the sensitivity to metals such as zinc, mercury and cadmium. The mutation may unwind a turn of the alpha-helix-10, indirectly increasing the interaction of the pH-sensor and other residues at the bottom of the luciferin binding site, stabilizing the green light emitting conformation	Amydetes vivianii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0025	-	D-firefly luciferin	pH 8.0, 22°C, mutant enzyme E270A	Amydetes vivianii
0.004	-	D-firefly luciferin	pH 8.0, 22°C, mutant enzyme E270G	Amydetes vivianii
0.005	-	ATP	pH 8.0, 22°C, mutant enzyme E270A	Amydetes vivianii
0.009	-	ATP	pH 8.0, 22°C, wild-type enzyme	Amydetes vivianii
0.009	-	D-firefly luciferin	pH 8.0, 22°C, wild-type enzyme	Amydetes vivianii
0.017	-	ATP	pH 8.0, 22°C, mutant enzyme E270G	Amydetes vivianii

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-firefly luciferin + O2 + ATP	Amydetes vivianii	-	firefly oxyluciferin + CO2 + AMP + diphosphate + hv	-	?

Organism

Organism	UniProt	Comment	Textmining
Amydetes vivianii	A0A3F2YLV6	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-firefly luciferin + O2 + ATP	-	Amydetes vivianii	firefly oxyluciferin + CO2 + AMP + diphosphate + hv	-	?
D-firefly luciferin + O2 + ATP	the enzyme display a typical change in bioluminescence color to red at acidic pH, high temperatures and in the presence of heavy metals	Amydetes vivianii	firefly oxyluciferin + CO2 + AMP + diphosphate + hv	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
22	-	assay at	Amydetes vivianii

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	ATP	kinetic properties of luciferase and E270 mutants	Amydetes vivianii
additional information	-	D-firefly luciferin	kinetic properties of luciferase and E270 mutants	Amydetes vivianii

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Amydetes vivianii

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
additional information	-	ATP	kinetic properties of luciferase and E270 mutants	Amydetes vivianii
additional information	-	D-firefly luciferin	kinetic properties of luciferase and E270 mutants	Amydetes vivianii

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Release 2023.1 (January 2023)