A Tryptophan Prenyltransferase with Broad Substrate Tolerance from Bacillus subtilis subsp. natto
A Tryptophan Prenyltransferase with Broad Substrate Tolerance from Bacillus subtilis subsp. natto
复制标题
来自枯草芽孢杆菌亚种的具有广泛底物耐受性的色氨酸异戊二烯转移酶。
DOI:
10.1002/cbic.201800174
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发表时间:
2018
期刊:
影响因子:
3.2
通讯作者:
Tian Tian
中科院分区:
文献类型:
--
作者:
Abe Ikuro;Sugita Tomotoshi;Okada Masahiro;Nakashima Yu;Tian Tian
Bacillus subtilissubsp.nattosecretes the ComXnattopheromone 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 otherBacillusComX pheromones, the tryptophan residue is distant from the C‐terminal end of the precursor peptide ComXnatto. Here, we report the functional analysis of ComQnatto, which catalyzes a unique farnesyl‐transfer reaction. ComQnattorecognizes not only full‐length ComXnattobut also N‐ and/or C‐terminal truncated ComXnattoanalogues and even a single tryptophan for modification with a farnesyl group in vitro. These results, together with the calculated kinetic parameters, suggest that ComQnattodoes 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.