Effects of the deletion and substitution of thioesterase on bacillomycin D synthesis.

Ping Zhang, Ziyan Lv, Zhaoxin Lu, Wenjie Ma, Xiaomei Bie

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Article in Biotechnology letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

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5 authors at 1 institution in 1 country.

Ping Zhang *College of Food Science and Technology, Nanjing Agricultural University, Nanjing, 210095, People's Republic of China.

Ziyan Lv *College of Food Science and Technology, Nanjing Agricultural University, Nanjing, 210095, People's Republic of China.

Zhaoxin LuCollege of Food Science and Technology, Nanjing Agricultural University, Nanjing, 210095, People's Republic of China.

Wenjie MaCollege of Food Science and Technology, Nanjing Agricultural University, Nanjing, 210095, People's Republic of China.

Xiaomei BieCollege of Food Science and Technology, Nanjing Agricultural University, Nanjing, 210095, People's Republic of China. bxm43@njau.edu.cn.ORCID http://orcid.org/0000-0002-2175-0164

Nanjing Agricultural University · CN

Funding

National Natural Science Foundation of China 31972174

6 · The paper itself

Abstract

objectivesThe importance of thioesterase domains on bacillomycin D synthesis and the ability of different thioesterase domains to selectively recognize and catalyze peptide chain hydrolysis and cyclization were studied by deleting and substituting thioesterase domains.

resultsNo bacillomycin D analogs were found in the thioesterase-deleted strain fmbJ-ΔTE, indicating that the TE domain was essential for bacillomycin D synthesis. Then the thioesterase in bacillomycin D synthetases was replaced by the thioesterase in bacillomycin F, iturin A, mycosubtilin, plipastatin and surfactin synthetases. Except for fmbJ-S-TE, all others were able to synthesize bacillomycin D homologs because a suitable recombination site was selected, which maintained the integrity of NRPSs. In particular, the yield of bacillomycin D in fmbJ-IA-TE, fmbJ-M-TE and fmbJ-P-TE was significantly increased.

conclusionThis study expands our understanding of the TE domain in bacillomycin D synthetases and shows that thioesterase has excellent potential in the chemical-enzymatic synthesis of natural products or their analogs.

Indexed as

Bacillomycin DHomologous recombinationProtein structureThioesterase

Identifiers

PMID37266877

DOI10.1007/s00253-009-2276-1

OpenAlexW4379093582

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.