Cover Feature: Probing the Substrate Promiscuity of Isopentenyl Phosphate Kinase as a Platform for Hemiterpene Analogue Production (ChemBioChem 17/2019). (21st August 2019)

• Record Type: Journal Article
• Authors: Lund, Sean; Courtney, Taylor; Williams, Gavin J.
• Is Part Of: Chembiochem. Volume 20:Number 17(2019)
• Page Start: 2162
• Page End: 2162
• Publication Date: 2019-08-21
• Subjects: hemiterpenes -- kinases -- phosphorylation -- synthetic biology -- terpenoids; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201900494
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract : The cover feature picture shows the substrate promiscuity of isopentenyl monophosphate kinase—a key enzyme in a recently described artificial metabolic pathway for hemiterpene biosynthesis. The remarkable broad substrate tolerance of this enzyme sets the stage to produce unnatural isoprenoids by coupling the activity of the kinase to downstream isoprenoid biosynthesis. More information can be found in the communication by G. J. Williams et al. on page 2217 in Issue 17, 2019 (DOI: 10.1002/cbic.201900135 ).