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A Tryptophan Prenyltransferase with Broad Substrate Tolerance from Bacillus subtilis subsp. natto
Author(s) -
Sugita Tomotoshi,
Okada Masahiro,
Nakashima Yu,
Tian Tian,
Abe Ikuro
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800174
Subject(s) - bacillus subtilis , tryptophan , biochemistry , prenyltransferase , residue (chemistry) , quorum sensing , biology , chemistry , enzyme , prenylation , bacteria , amino acid , genetics , virulence , gene
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.