Catalytic rate (kcat) of luciferase for the oxidation of luciferin

Value 1.6 sec^-1
Organism Unspecified
Reference Rangaraju V, Calloway N, Ryan TA. Activity-driven local ATP synthesis is required for synaptic function. Cell. 2014 Feb 13 156(4):825-35. doi: 10.1016/j.cell.2013.12.042. p.825 right column bottom paragraphPubMed ID24529383
Primary Source Branchini, B.R., Magyar, R.A., Murtiashaw, M.H., Anderson, S.M., and Zimmer, M. (1998). Site-directed mutagenesis of histidine 245 in firefly luciferase: a proposed model of the active site. Biochemistry 37, 15311–15319.PubMed ID9799491
Comments "Firefly luciferase catalyzes the oxidation of luciferin, a cell-permeant substrate, using ATP and Mg2+ to give light with a quantum yield of 0.41 (Fraga, 2008). This enzymatic process specifically requires ATP and other nucleotides do not impact this protein’s function (Moyer and Henderson, 1983), thereby making luciferase an efficient optical reporter of ATP. However, two major limitations hamper its use for quantitative subcellular imaging: its slow catalytic rate (kcat = 1.6sec^-1) (primary source) and lack of a suitable calibration for specific activity in situ."
Entered by Uri M
ID 111084