122364-83-4Relevant academic research and scientific papers
Luciferin and derivatives as a DYRK selective scaffold for the design of protein kinase inhibitors
Rothweiler, Ulli,Eriksson, Jonas,Stensen, Wenche,Leeson, Frederick,Engh, Richard A.,Svendsen, John S.
, p. 140 - 148 (2015)
D-Luciferin is widely used as a substrate in luciferase catalysed bioluminescence assays for in vitro studies. However, little is known about cross reactivity and potential interference of D-luciferin with other enzymes. We serendipitously found that firefly luciferin inhibited the CDK2/Cyclin A protein kinase. Inhibition profiling of D-luciferin over a 103-protein kinase panel showed significant inhibition of a small set of protein kinases, in particular the DYRK-family, but also other members of the CMGC-group, including ERK8 and CK2. Inhibition profiling on a 16-member focused library derived from D-luciferin confirms that D-luciferin represents a DYRK-selective chemotype of fragment-like molecular weight. Thus, observation of its inhibitory activity and the initial SAR information reported here promise to be useful for further design of protein kinase inhibitors with related scaffolds.
Sensitive luciferin derived probes for selective carboxypeptidase activity
Chang, Yu-Cheng,Chao, Pei-Wen,Tung, Ching-Hsuan
body text, p. 3931 - 3934 (2011/08/06)
Highly selective luminescent probes, QLUC-TYR and LUC-GLU, for detection of carboxypeptidase activity were synthesized. Caged substrates were first cleaved by corresponding carboxypeptidases, and then they were activated by luciferase to emit light. Enzym
