Prenyltransferases as key enzymes in primary and secondary metabolism

• Published in: Applied Microbiology and Biotechnology Vol. 99; no. 18; pp. 7379 - 7397
• Main Authors: Winkelblech, Julia, Fan, Aili, Li, Shu-Ming
• Format: Journal Article Book Review
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 01-09-2015; Springer; Springer Nature B.V
• Subjects: Analysis; Biodiversity; Biomedical and Life Sciences; Biosynthesis; Biotechnology; Butadienes - metabolism; crystal structure; Dimethylallyltranstransferase - chemistry; Dimethylallyltranstransferase - metabolism; Enzymes; Flavonoids; Hemiterpenes - metabolism; isoprene; Life Sciences; Metabolism; Metabolites; Microbial Genetics and Genomics; Microbiology; Mini-Review; Natural products; Nitrogen; Pentanes - metabolism; Peptides; Physiological aspects; Plant metabolites; post-translational modification; Post-translational modifications; Prenylation; Protein Conformation; Protein Processing, Post-Translational; Proteins; Proteins - metabolism; Ribonucleic acid; RNA; Secondary Metabolism; Secondary metabolites; Studies; Transfer RNA; tryptophan; tyrosine; Tyrosine - metabolism; Benin; Phylogenetic relationships; tRNA prenyltransferase; Dimethylallyltryptophan synthase; Aromatic prenyltransferase; Peptide prenyltransferase; Protein prenyltransferase; Prenyl diphosphate synthase
• ISSN: 0175-7598; 1432-0614
• DOI: 10.1007/s00253-015-6811-y

Attachment of isoprene units to various acceptors by prenylation plays an important role in primary and secondary metabolism of living organisms. Protein prenylation belongs to posttranslational modification and is involved in cellular regulation process. Prenylated secondary metabolites usually demonstrate promising biological and pharmacological activities. Prenyl transfer reactions catalyzed by prenyltransferases represent the key steps in the biosynthesis and contribute significantly to the structural and biological diversity of these compounds. In the last decade, remarkable progress has been achieved in the biochemical, molecular, and structural biological investigations of prenyltransferases, especially on those of the members of the dimethylallyltryptophan synthase (DMATS) superfamily. Until now, more than 40 of such soluble enzymes are identified and characterized biochemically. They catalyze usually regioselective and stereoselective prenylations of a series of aromatic substances including tryptophan, tryptophan-containing peptides, and other indole derivatives as well as tyrosine or even nitrogen-free substrates. Crystal structures of a number of prenyltransferases have been solved in the past 10 years and provide a solid basis for understanding the mechanism of prenyl transfer reactions.