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

BRENDA support

Literature summary extracted from

  • Ayabe, K.; Zako, T.; Ueda, H.
    The role of firefly luciferase C-terminal domain in efficient coupling of adenylation and oxidative steps (2005), FEBS Lett., 579, 4389-4394.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.7 expressed in Escherichia coli XL10-Gold cells Photinus pyralis

Protein Variants

EC Number Protein Variants Comment Organism
1.13.12.7 H245D longest rise time known among single point mutants Photinus pyralis
1.13.12.7 K529A similar rise time compared to wild type enzyme Photinus pyralis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.12.7 Mg2+ enzyme activity without 10 mM MgSO4 decreases to about 50% of that of wild type enzyme in the presence of Mg2+ Photinus pyralis

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.7 Photinus pyralis
-
-
-

Storage Stability

EC Number Storage Stability Organism
1.13.12.7 4°C, in 50 mM Tris-HCl, 1 mM EDTA, 150 mM NaCl, 1 mM DTT and 0.8 M ammonium sulfate pH 8.0 Photinus pyralis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.7 D-luciferin + O2 + ATP
-
Photinus pyralis oxyluciferin + CO2 + H2O + AMP + diphosphate + hv
-
r

Synonyms

EC Number Synonyms Comment Organism
1.13.12.7 firefly luciferase
-
Photinus pyralis
1.13.12.7 Luc
-
Photinus pyralis
1.13.12.7 Ppy
-
Photinus pyralis