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

BRENDA support

Literature summary for 1.13.12.7 extracted from

  • DeLuca M.; McElroy, W.D.
    Two kinetically distinguishable ATP sites in firefly luciferase (1984), Biochem. Biophys. Res. Commun., 123, 764-770.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
ATP mechanism Photinus pyralis
Procion blue MX-R irreversible inhibitor, enzyme protected by luciferin, ATP and MgATP2-; time dependent Photinus pyralis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.11
-
ATP two catalytically active sites: first site with a Km for ATP of 0.11 mM is responsible for initial flash, a second site with a Km for ATP of 0.02 mM catalyses the continuous low production of light Photinus pyralis

Organism

Organism UniProt Comment Textmining
Photinus pyralis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Photinus luciferin + O2 + ATP
-
Photinus pyralis oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
?

Subunits

Subunits Comment Organism
dimer only one subunit is enzymatically active Photinus pyralis