| 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 |