| Title: | A Tryptophan Prenyltransferase with Broad Substrate Tolerance from Bacillus subtilis subsp. natto |
| Author(s): | Sugita T; Okada M; Nakashima Y; Tian T; Abe I; |
| Address: | "Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan. Present address: Department of Material and Life Chemistry, Kanagawa University, Yokohama, 221-8686, Japan" |
| ISSN/ISBN: | 1439-7633 (Electronic) 1439-4227 (Linking) |
| Abstract: | "Bacillus subtilis subsp. natto secretes the ComX(natto) pheromone as a quorum-sensing pheromone to produce poly-gamma-glutamate for biofilm formation. The amino-acid sequence of the pheromone is Lys-Trp-Pro-Pro-Ile-Glu, and the tryptophan residue is post-translationally modified with a farnesyl group to form a tricyclic scaffold. Unlike other Bacillus ComX pheromones, the tryptophan residue is distant from the C-terminal end of the precursor peptide ComX(natto) . Here, we report the functional analysis of ComQ(natto) , which catalyzes a unique farnesyl-transfer reaction. ComQ(natto) recognizes not only full-length ComX(natto) but also N- and/or C-terminal truncated ComX(natto) analogues and even a single tryptophan for modification with a farnesyl group in vitro. These results, together with the calculated kinetic parameters, suggest that ComQ(natto) does not require a leader sequence for substrate recognition and is a promising enzyme with broad substrate tolerance for the synthesis of various prenylated tryptophan derivatives" |
| Keywords: | Alkyl and Aryl Transferases/chemistry/*metabolism Amino Acid Sequence Bacillus subtilis/*enzymology Bacterial Proteins/chemistry/*metabolism Catalysis Kinetics Oligopeptides/*biosynthesis/chemistry Pheromones/*biosynthesis/chemistry Prenylation Protein Pr; |
| Notes: | "MedlineSugita, Tomotoshi Okada, Masahiro Nakashima, Yu Tian, Tian Abe, Ikuro eng Research Support, Non-U.S. Gov't Germany 2018/04/18 Chembiochem. 2018 Jul 4; 19(13):1396-1399. doi: 10.1002/cbic.201800174. Epub 2018 Jun 1" |
