Relaxed specificity in aromatic prenyltransferases
- 1 July 2005
- journal article
- Published by Springer Nature in Nature Chemical Biology
- Vol. 1 (2) , 71-72
- https://doi.org/10.1038/nchembio0705-71
Abstract
Prenylation represent a critical step in the biosynthesis of many natural products, A new study reveals how aromatic prenyltransferase enzymes tolerate diverse aromatic polyketides while still controlling the length of prenyl side chains.Keywords
This publication has 7 references indexed in Scilit:
- Structural basis for the promiscuous biosynthetic prenylation of aromatic natural productsNature, 2005
- Natural products and combinatorial chemistry: back to the futureCurrent Opinion in Chemical Biology, 2004
- CloQ, a prenyltransferase involved in clorobiocin biosynthesisProceedings of the National Academy of Sciences, 2003
- Structure, mechanism and function of prenyltransferasesEuropean Journal of Biochemistry, 2002
- The TIM‐barrel fold: a versatile framework for efficient enzymesFEBS Letters, 2001
- Barrel structures in proteins: Automatic identification and classification including a sequence analysis of TIM barrelsProtein Science, 1999
- Biosynthetic studies of naphterpin, a terpenoid metabolite of streptomycesTetrahedron Letters, 1990