Structural Basis of Substrate Promiscuity and Catalysis by the Reverse Prenyltransferase

Autor:	Samuel A, Eaton, Trey A, Ronnebaum, Benjamin W, Roose, David W, Christianson
Rok vydání:	2023
Předmět:	Neoprene Prenylation Biological Products Hemiterpenes Indoles Organophosphorus Compounds Fusarium Nitrogen Tryptophan Tryptophan Synthase Dimethylallyltranstransferase Catalysis Substrate Specificity
Zdroj:	Biochemistry. 61(18)
ISSN:	1520-4995
Popis:	The regiospecific prenylation of an aromatic amino acid catalyzed by a dimethylallyl-l-tryptophan synthase (DMATS) is a key step in the biosynthesis of many fungal and bacterial natural products. DMATS enzymes share a common "ABBA" fold with divergent active site contours that direct alternative C-C, C-N, and C-O bond-forming trajectories. DMATS1 from
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::434209d989875d088aa5eff80ae535e9 https://pubmed.ncbi.nlm.nih.gov/36084241 Zobrazit plný text záznamu