Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Tafreshi, N.K.h.; Sadeghizadeh, M.; Emamzadeh, R.; Ranjbar, B.; Naderi-Manesh, H.; Hosseinkhani, S.
    Site-directed mutagenesis of firefly luciferase: implication of conserved residue(s) in bioluminescence emission spectra among firefly luciferases (2008), Biochem. J., 412, 27-33.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.13.12.7 biotechnology imaging technology Lampyris turkestanicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.7 expression in Escherichia coli BL21 Lampyris turkestanicus

Protein Variants

EC Number Protein Variants Comment Organism
1.13.12.7 H245N red- and green-emitting luciferase, increase in thermostability, about 25% decrease in relative activity Lampyris turkestanicus
1.13.12.7 H431Y red- and green-emitting luciferase, about 85% decrease in relative acitivity Lampyris turkestanicus
1.13.12.7 S284T red-emitting luciferase, about 75% decrease in relative activity Lampyris turkestanicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.12.7 0.01612
-
 D-luciferin wild-type luciferase Lampyris turkestanicus
1.13.12.7 0.023
-
 D-luciferin mutant H245N Lampyris turkestanicus
1.13.12.7 0.026
-
 D-luciferin mutant H431Y Lampyris turkestanicus
1.13.12.7 0.03
-
 D-luciferin mutant S284T Lampyris turkestanicus
1.13.12.7 0.135
-
 ATP wild-type luciferase Lampyris turkestanicus
1.13.12.7 0.168
-
 ATP mutant H245N Lampyris turkestanicus
1.13.12.7 0.1872
-
 ATP mutant H431Y Lampyris turkestanicus
1.13.12.7 0.2484
-
 ATP mutant S284T Lampyris turkestanicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.12.7 Mg2+ required Lampyris turkestanicus

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.7 Lampyris turkestanicus Q5UFR2 wild-type emits green light
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.12.7 Ni-NTA Sepharose Lampyris turkestanicus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.13.12.7 additional information
-
 11500000000000 relative light units/mg, mutant H245N Lampyris turkestanicus
1.13.12.7 additional information
-
 15000000000000 relative light units/mg, wild-type luciferase Lampyris turkestanicus
1.13.12.7 additional information
-
 2500000000000 relative light units/mg, mutant H431Y Lampyris turkestanicus
1.13.12.7 additional information
-
 3600000000000 relative light units/mg, mutant S284T Lampyris turkestanicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.7 D-luciferin + ATP + O2 assay at 25°C, pH 7.8 Lampyris turkestanicus oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.12.7 firefly luciferase
-
 Lampyris turkestanicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.12.7 24
-
 wild-type luciferase, mutant H245N and H431Y Lampyris turkestanicus
1.13.12.7 25
-
 assay at Lampyris turkestanicus
1.13.12.7 30
-
 mutant S284T Lampyris turkestanicus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.13.12.7 15 40 at 35°C native luciferase completely inactive, mutant H245N still 80% residual activity, mutant S284T and H431Y about 20% residual activity Lampyris turkestanicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.12.7 7.8
-
 assay at Lampyris turkestanicus
1.13.12.7 8
-
 wild-type luciferase, mutant S284T Lampyris turkestanicus
1.13.12.7 8.5
-
 mutant H245N and H431Y Lampyris turkestanicus