1. Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway
- Author
-
Claudia Clemente, Nicholas Johnson, Xiaodan Ouyang, Rafael V. Popin, Sergio Dall'Angelo, Matti Wahlsten, Jouni Jokela, Alessandro Colombano, Brunello Nardone, David P. Fewer, Wael E. Houssen, Institute of Biotechnology, Department of Food and Nutrition, Department of Microbiology, Faculty of Agriculture and Forestry, Cyanobacteria research, Helsinki Institute of Sustainability Science (HELSUS), and Microbial Natural Products
- Subjects
HETEROCYCLIZATION ,PROTEINS ,Metals and Alloys ,ENABLES ,General Chemistry ,Catalysis ,TRYPTOPHAN ,Surfaces, Coatings and Films ,Electronic, Optical and Magnetic Materials ,DRUG DISCOVERY ,Materials Chemistry ,Ceramics and Composites ,1182 Biochemistry, cell and molecular biology ,MACROCYCLASE ,ENZYMES ,CYCLIC PEPTIDE - Abstract
Cyanobactins are linear and cyclic post-translationally modified peptides. Here we show that the prenyl-D-Arg-containing autum-nalamide A is a member of the cyanobactin family. Biochemical assays demonstrate that the AutF prenyltransferase targets the guanidinium moiety in arginine and homoarginine and is a useful tool for biotechnological applications.
- Published
- 2022