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University of Groningen Lanthipeptide engineering: non-canonical amino acids, click chemistry and ring shuffling Deng, Jingjing

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University of Groningen

Lanthipeptide engineering: non-canonical amino acids, click chemistry and ring shuffling

Deng, Jingjing

DOI:

10.33612/diss.112973724

IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below.

Document Version

Publisher's PDF, also known as Version of record

Publication date: 2020

Link to publication in University of Groningen/UMCG research database

Citation for published version (APA):

Deng, J. (2020). Lanthipeptide engineering: non-canonical amino acids, click chemistry and ring shuffling. University of Groningen. https://doi.org/10.33612/diss.112973724

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Lis t o f Pu bli ca tio ns

List of Publications

1. Deng, J., Viel, J. H. & Kuipers, O. P. Generation of nisin derivatives with an altered spectrum by incorporating methionine analogues. Submitted.

2. Deng, J., Viel, J. H, Kubyshkin, V., Chen, J., Budisa, N. & Kuipers, O. P. Synthesis of nisin conjugates via click chemistry and their characterization. Submitted.

3. Montalban-Lopez, M.* Deng, J.*, van Heel, A. & Kuipers, O. P. (2018). Specificity

and application of the lantibiotic protease NisP. Frontiers in microbiology 9:160, doi: 10.3389/fm icb.2018.00160.

4. Deng, J. & Lu, C. (2015). Two new isoflavone 7-O-α-4˝-anhydro-4˝,5˝-didehydro-glucuronides from Streptomyces sp. LZ35 ΔgdmAI. Natural product research 30 (2), 1–5, doi: 10.1080/14786419.2015.1046869.

5. Xie, C.*, Deng, J.*, Wang, H. & Shen, Y. (2015). Activation of a silent ansatrienin gene

cluster by constitutive expression of LAL family regulator gene in Streptomyces sp. XZQH13. Current microbiology 70 (6), 859–864, doi: 10.1007/s00284-015-0798-6. 6. Deng, J., Lu, C., Li, S., Hao, H., Li, Z., Zhu, J., Li, Y. & Shen, Y. (2014). p-terphenyl O-β-glucuronosides, DNA topoisomerase inhibitors from Streptomyces sp. LZ35ΔgdmAI.

Bioorganic and medicinal chemistry letters 24 (5), doi: 10.1016/j.bmcl.2014.01.037.

7. Deng, J.*, Lu, C.*, Li, Y., Li, S. & Shen, Y. (2013). Cuevaenes C-E, New triene

car-boxylic derivatives from Streptomyces sp. LZ35ΔgdmAI. Beilstein journal of organic

chemistry 10 (1), 858-862, doi: 10.3762/bjoc.10.82.

8. Lu, C.*, Li, Y.*, Deng, J.*, Li, S., Shen, Y., Wang, H. & Shen, Y. (2013). Hygrocins

C-G, cytotoxic naphthoquinone ansamycins from gdmAI-disrupted Streptomyces sp. LZ35. Journal of natural products 76 (12), 2175–9, doi: 10.1021/np400474s.

9. Schmitt, S.*, Montalbán-López, M.*, Peterhoff, D., Deng, J., Wagner, R., Held, M.,

Kuipers, O. P. & Panke, S. (2019). Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale. Nature chemical biology 15, 437–443, doi: 10.1038/ s41589-019-0250-5.

10. van Heel, A., Kloosterman, T. G., Montalban-Lopez, M., Deng, J., Plt, A., Baudu, B., Hendriks, D., Moll, G. N. & Kuipers, O. P. (2016). Discovery, production and modification of 5 novel lantibiotics using the promiscuous nisin modification ma-chinery. ACS synthetic biology 5(10), 1146–1154, doi: 10.1021/acssynbio.6b00033. 11. Shi, G., Shi, N., Li, Y., Chen, W., Deng, J., Liu, C., Zhu, J., Wang, H. & Shen, Y. (2016).

D-alanylation in the assembly of ansatrienin side chain is catalyzed by a modular NRPS. ACS chemical biology 11(4), 876–881, doi: 10.1021/acschembio.6b00004. 12. Mu, D., Montalban-Lopez, M., Deng, J. & Kuipers, O. P. (2015). Lantibiotic

re-ductase LtnJ substrate selectivity assessed with a collection of nisin derivatives as substrates. Applied and environmental microbiology 81, 3679-3687, doi:10.1128/ AEM.00475-15.

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13. Li, S., Lu, C., Ou, J., Deng, J. & Shen, Y. (2015). Overexpression of Hgc1 Increases the production and diversity of hygrocins in Streptomyces sp. LZ35. RSC advances 5 (102), 83843-83846, doi:10.1039/C5RA12623A.

14. Zhu, J, Chen, W., Li, Y., Deng, J., Zhu, D., Duan, J., Shi, G., Xie, C., Wang, H. & Shen, Y. (2014). Identification and catalytic characterization of a nonribosomal peptide

synthetase-like (NRPS-like) enzyme involved in the biosynthesis of echosides from

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