Efficient modification of the Pseudomonas aeruginosa toxin 2-heptyl-1-hydroxyquinolin-4-one by three Bacillus glycosyltransferases with broad substrate ranges.
In: Journal of Biotechnology, Jg. 308 (2020-01-20), S. 74-81
Online
academicJournal
Zugriff:
• Identification of glycosyltransferases from Bacillus subtilis converting HQNO. • Kinetic parameters of YjiC, YdhE and Yojk towards HQNO and UDP-glucose. • Identification of glucosylated plant and Pseudomona s derived antimicrobials. • Comparison of NDP-glucose and aglycon promiscuities. Glycosylation of natural and synthetic products can alter the physical, chemical and pharmacological properties of the aglycon. Conversion of 2-heptyl-1-hydroxyquinolin-4-one (HQNO), a potent respiratory inhibitor produced by Pseudomonas aeruginosa , to the less toxic 2-heptyl-1-(β-D-glucopyranosydyl)-quinolin-4-one, was recently demonstrated for Bacillus subtilis strain 168. In this study, we compared the genomes of several Bacillus spp. to identify candidate enzymes for HQNO glucosylation. All three (putative) UDP-glycosyltransferases (GT) of B. subtili s 168 tested, YjiC, YdhE and YojK, were capable of HQNO glucosylation, with YjiC showing the highest turnover rate (k cat) of 4.6 s−1, and YdhE exhibiting the lowest K m value for HQNO of 9.1 μM. All three GT predominantly utilized UDP-glucose, but YdhE was similarly active with TDP-glucose. Among the aglycons tested, HQNO was the preferred substrate of all three GT, but they also showed activities toward the P. aeruginosa exoproducts pyocyanin, 2-heptyl-3-hydroxyquinolin-4(1 H)-one (the Pseudomonas quinolone signal) and 2,4-dihydroxyquinoline, the plant derived antimicrobials vanillin and quercetin, and the macrolide antibiotic tylosin A. Our results underline the promiscuity and substrate flexibility of YjiC, YdhE and YojK, and suggest a physiological role in natural toxin resistance of B. subtilis. Especially YdhE appears to be an attractive biocatalyst for the glycoengineering of natural products. [ABSTRACT FROM AUTHOR]
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Efficient modification of the Pseudomonas aeruginosa toxin 2-heptyl-1-hydroxyquinolin-4-one by three Bacillus glycosyltransferases with broad substrate ranges.
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Autor/in / Beteiligte Person: | Thierbach, Sven ; Sartor, Pascal ; Yücel, Onur ; Fetzner, Susanne |
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Zeitschrift: | Journal of Biotechnology, Jg. 308 (2020-01-20), S. 74-81 |
Veröffentlichung: | 2020 |
Medientyp: | academicJournal |
ISSN: | 0168-1656 (print) |
DOI: | 10.1016/j.jbiotec.2019.11.015 |
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