A Tryptophan Prenyltransferase with Broad Substrate Tolerance from Bacillus subtilis subsp natto

作者：Sugita Tomotoshi; Okada Masahiro; Nakashima Yu; Tian Tian; Abe Ikuro^*

来源：ChemBioChem, 2018, 19(13): 1396-1399.

DOI：10.1002/cbic.201800174

• nitrogen heterocycles
• pheromones
• polycycles
• post-translational modification
• prenyltransferase
• tryptophan

Bacillus subtilis subsp. natto secretes the ComX(natto) pheromone as a quorum-sensing pheromone to produce poly--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.

• 出版日期2018-7-4