A Tryptophan Prenyltransferase with Broad Substrate Tolerance from Bacillus subtilis subsp. natto
2018; Wiley; Volume: 19; Issue: 13 Linguagem: Inglês
10.1002/cbic.201800174
ISSN1439-7633
AutoresTomotoshi Sugita, Masahiro Okada, Yu Nakashima, Tian Tian, Ikuro Abe,
Tópico(s)Antimicrobial Peptides and Activities
ResumoAbstract Bacillus subtilis subsp. natto secretes the ComX natto pheromone as a quorum‐sensing pheromone to produce poly‐γ‐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.
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