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Literature summary for 1.13.12.7 extracted from

  • Noori, A.R.; Hosseinkhani, S.; Ghiasi, P.; Akbari, J.; Heydari, A.
    Magnetic nanoparticles supported ionic liquids improve firefly luciferase properties (2014), Appl. Biochem. Biotechnol., 172, 3116-3127 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information enzyme activity and structural stability increases in presence of magnetic magnetite (lambda-Fe2O3) nanoparticles supported ionic liquids. The effect of ingredients which are used is not considerable on Km value of luciferase for ATP and also Km value for luciferin, synthesis and evaluation, overview. The use of ionic liquids supported on magnetic nanoparticles improves kinetic and structural properties of firefly luciferase using bioluminescence assay, fluorescence spectroscopy, and circular dichroism Photinus pyralis

Inhibitors

Inhibitors Comment Organism Structure
additional information irreversible aggregation because of the exposure of its hydrophobic sites followed by structural changes leads to its further inactivation Photinus pyralis

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Photinus pyralis P08659
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-firefly luciferin + O2 + ATP
-
Photinus pyralis firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
?

Synonyms

Synonyms Comment Organism
firefly luciferase
-
Photinus pyralis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
free wild-type enzyme Photinus pyralis
30
-
enzyme in presence of magnetic magnetite nanoparticles supported ionic liquids Photinus pyralis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
thermal stability and activity at 35°C of the enzyme in presence of magnetic magnetite nanoparticles supported ionic liquids is increased compared to the free enzyme, overview Photinus pyralis
35 45 free enzyme shows 65% remaning activity after 10 min at 35°C, inactivation after 4 min at 35°C, inactivation at 45°C Photinus pyralis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
-
Photinus pyralis

Cofactor

Cofactor Comment Organism Structure
ATP
-
Photinus pyralis

General Information

General Information Comment Organism
physiological function firefly luciferase from North American Photinus pyralis is a monooxygenase that performs ATP-dependent conversion of luciferin into a luciferyl-adenylate, which is oxidized in a multistep reaction to electronically excited oxyluciferin Photinus pyralis