The authors thank Professor Horst Schulz, Wenfeng Yu, and Lina Nie (City University of New York) for assistance with rat homogenates and supplying the rMCAD enzyme; Professor Jung-Ja Kim (Medical College of Wisconsin) for supplying the pSCAD, pMCAD, and hLCAD enzymes; and Dominic Yee for intellectual contributions. This work was generously supported by The G. Harold & Leila Y. Mathers Charitable Foundation. M.K.F. is the recipient of a NSF Predoctoral Fellowship.
Fluoromorphic Substrates for Fatty Acid Metabolism: Highly Sensitive Probes for Mammalian Medium-Chain Acyl-CoA Dehydrogenase†
Article first published online: 19 DEC 2005
Copyright © 2006 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 45, Issue 4, pages 637–642, January 16, 2006
How to Cite
Froemming, M. K. and Sames, D. (2006), Fluoromorphic Substrates for Fatty Acid Metabolism: Highly Sensitive Probes for Mammalian Medium-Chain Acyl-CoA Dehydrogenase. Angew. Chem. Int. Ed., 45: 637–642. doi: 10.1002/anie.200502675
- Issue published online: 11 JAN 2006
- Article first published online: 19 DEC 2005
- Manuscript Received: 29 JUL 2005
- enzyme promiscuity;
- fluorescent probe;
- medium-chain acyl-CoA dehydrogenase;
Not fussy: A systematic study revealed considerable substrate tolerance of medium-chain acyl-CoA dehydrogenase (MCAD), a member of the β-oxidation pathway for the degradation of fatty acids. Three fluorogenic reporter substrates were developed, which in turn allowed for selective, sensitive, and continuous monitoring of MCAD activity in tissue homogenates.