Related Experiment Video
Updated: Jun 21, 2026

13:16
Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles
Published on: December 31, 2019
Backbone assignments of the 34 kDa ketopantoate reductase from E. coli
Stephen J Headey1, Amelia Vom, Jamie S Simpson
1Medicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences, Monash University (Parkville Campus), 381 Royal Parade, Parkville, VIC 3052, Australia.
Biomolecular NMR Assignments
|July 29, 2009
Abstract:
Ketopantoate reductase is an essential enzyme for pantothenate (vitamin B5) synthesis and a potential antibiotic target. Here we report the 15N and 1HN, 13C', 13C(alpha) and 13C(beta) chemical shift assignments of the 34 kDa ketopantoate reductase in its apo state.

