[1] WALSH C T. Insights into the chemical logic and enzymatic machinery of NRPS assembly lines[J]. Natural Product Reports, 2016, 33(2):127-135.
[2] CACHO R A, TANG Y. Reconstitution of fungal nonribosomal peptide synthetases in yeast and in vitro[J]. Methods in Molecular Biology, 2016, 1401:103-119.
[3] MOOTZ H D, SCHWARZER D, MARAHIEL M A. Ways of assembling complex natural products on modular nonribosomal peptide synthetases[J]. Chembiochem: a European Journal of Chemical Biology, 2002, 3(6):490-504.
[4] BOZHÜYÜK K A, MICKLEFIELD J, WILKINSON B. Engineering enzymatic assembly lines to produce new antibiotics[J]. Current Opinion in Microbiology, 2019, 51:88-96.
[5] YU D Y, XU F C, ZHANG S W, et al. Decoding and reprogramming fungal iterative nonribosomal peptide synthetases[J]. Nature Communications, 2017, 8:15349.
[6] KIM M S, BAE M, JUNG Y E, et al. Unprecedented noncanonical features of the nonlinear nonribosomal peptide synthetase assembly line for WS9326A biosynthesis[J]. Angewandte Chemie (International Ed. in English), 2021, 60(36):19766-19773.
[7] SÜSSMUTH R D, MAINZ A. Nicht-ribosomale peptidsynthese-prinzipien und perspektiven[J]. Angewandte Chemie, 2017, 129(14):3824-3878.
[8] BAUNACH M, CHOWDHURY S, STALLFORTH P,et al.The landscape of recombination events that create nonribosomal peptide diversity[J]. Molecular Biology and Evolution, 2021, 38(5):2116-2130.
[9] CALCOTT M J, OWEN J G, ACKERLEY D F. Efficient rational modification of non-ribosomal peptides by adenylation domain substitution[J]. Nature Communications, 2020, 11(1):4554.
[10] NIQUILLE D L, HANSEN D A, MORI T, et al. Nonribosomal biosynthesis of backbone-modified peptides[J]. Nature Chemistry, 2018, 10(3):282-287.
[11] STANIIĆ A, HÜSKEN A, STEPHAN P, et al. Engineered nonribosomal peptide synthetase shows opposite amino acid loading and condensation specificity[J]. ACS Catalysis, 2021, 11(14):8692-8700.
[12] LEE T V, JOHNSON R D, ARCUS V L, et al. Prediction of the substrate for nonribosomal peptide synthetase (NRPS) adenylation domains by virtual screening[J]. Proteins, 2015, 83(11):2052-2066.
[13] HARA R, SUZUKI R, KINO K. Hydroxamate-based colorimetric assay to assess amide bond formation by adenylation domain of nonribosomal peptide synthetases[J]. Analytical Biochemistry, 2015, 477:89-91.
[14] KALJUNEN H, SCHIEFELBEIN S H H, STUMMER D D, et al. Strukturelle Aufklärung der Bispezifität von A-Domänen als Basis für die Aktivierung nicht-natürlicher Aminosäuren[J].Angewandte Chemie, 2015, 127(30):8957-8961.
[15] ABE T, KOBAYASHI K, KAWAMURA S, et al. Dipeptide synthesis by internal adenylation domains of a multidomain enzyme involved in nonribosomal peptide synthesis[J]. The Journal of General and Applied Microbiology, 2019, 65(1):1-10.
[16] KANO S, SUZUKI S, HARA R, et al. Synthesis of d-amino acid-containing dipeptides using the adenylation domains of nonribosomal peptide synthetase[J]. Applied and Environmental Microbiology, 2019, 85(13): e00120-e00119.
[17] WU Z Y, LI Y R, FANG Y K, et al. Adenylation domains of nonribosomal peptide synthetase: A potential biocatalyst for synthesis of dipeptides and their derivatives[J]. Enzyme and Microbial Technology, 2022, 160:110089.
[18] IZORÉ T, CRYLE M J. The many faces and important roles of protein-protein interactions during non-ribosomal peptide synthesis[J]. Natural Product Reports, 2018, 35(11):1120-1139.
[19] CALCOTT M J, ACKERLEY D F. Portability of the thiolation domain in recombinant pyoverdine non-ribosomal peptide synthetases[J]. BMC Microbiology, 2015, 15:162.
[20] LINNE U, DOEKEL S, MARAHIEL M A. Portability of epimerization domain and role of peptidyl carrier protein on epimerization activity in nonribosomal peptide synthetases[J]. Biochemistry, 2001, 40(51):15824-15834.
[21] OWEN J G, ROBINS K J, PARACHIN N S, et al. A functional screen for recovery of 4'-phosphopantetheinyl transferase and associated natural product biosynthesis genes from metagenome libraries[J]. Environmental Microbiology, 2012, 14(5):1198-1209.
[22] GAO L, LIU H X, MA Z, et al. Translocation of the thioesterase domain for the redesign of plipastatin synthetase[J]. Scientific Reports, 2016, 6:38467.
[23] KANIUSAITE M, GOODE R J A, TAILHADES J, et al. Exploring modular reengineering strategies to redesign the teicoplanin non-ribosomal peptide synthetase[J]. Chemical Science, 2020, 11(35):9443-9458.
[24] STACHELHAUS T, MOOTZ H D, MARAHIEL M A. The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases[J]. Chemistry & Biology, 1999, 6(8):493-505.
[25] BERGENDAHL V, LINNE U, MARAHIEL M A. Mutational analysis of the C-domain in nonribosomal peptide synthesis[J]. European Journal of Biochemistry, 2002, 269(2):620-629.
[26] SAMEL S A, SCHOENAFINGER G, KNAPPE T A, et al. Structural and functional insights into a peptide bond-forming bidomain from a nonribosomal peptide synthetase. Structure, 2007, 15(7):781-792.
[27] ZHONG L, DIAO X T, ZHANG N, et al. Engineering and elucidation of the lipoinitiation process in nonribosomal peptide biosynthesis[J]. Nature Communications, 2021, 12(1):296.
[28] BOZHÜYÜK K A J, FLEISCHHACKER F, LINCK A, et al. De novo design and engineering of non-ribosomal peptide synthetases[J]. Nature Chemistry, 2018, 10(3):275-281.
[29] BOZHÜYÜK K A J, LINCK A, TIETZE A, et al. Modification and de novo design of non-ribosomal peptide synthetases using specific assembly points within condensation domains[J]. Nature Chemistry, 2019, 11(7):653-661.
[30] TURGAY K, KRAUSE M, MARAHIEL M A. Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes[J]. Molecular Microbiology, 1992, 6(18):2743-2744.
[31] KOHLI R M, TAKAGI J, WALSH C T. The thioesterase domain from a nonribosomal peptide synthetase as a cyclization catalyst for integrin binding peptides[J]. Proceedings of the National Academy of Sciences of the United States of America, 2002, 99(3):1247-1252.
[32] KIM B S, CROPP T A, BECK B J, et al. Biochemical evidence for an editing role of thioesterase II in the biosynthesis of the polyketide pikromycin[J]. The Journal of Biological Chemistry, 2002, 277(50):48028-48034.
[33] SCHWARZER D, MOOTZ H D, MARAHIEL M A. Exploring the impact of different thioesterase domains for the design of hybrid peptide synthetases[J]. Chemistry & Biology, 2001, 8(10):997-1010.
[34] WANG H, FEWER D P, HOLM L, et al. Atlas of nonribosomal peptide and polyketide biosynthetic pathways reveals common occurrence of nonmodular enzymes[J]. Proceedings of the National Academy of Sciences of the United States of America, 2014, 111(25):9259-9264.
[35] KRIES H. Biosynthetic engineering of nonribosomal peptide synthetases[J]. Journal of Peptide Science: an Official Publication of the European Peptide Society, 2016, 22(9):564-570.
[36] HACKER C, CAI X F, KEGLER C, et al. Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS[J]. Nature Communications, 2018, 9(1):4366.
[37] DOWLING D P, KUNG Y, CROFT A K, et al. Structural elements of an NRPS cyclization domain and its intermodule docking domain[J]. Proceedings of the National Academy of Sciences of the United States of America, 2016, 113(44):12432-12437.
[38] KOSOL S, GALLO A, GRIFFITHS D, et al. Structural basis for chain release from the enacyloxin polyketide synthase[J]. Nature Chemistry, 2019, 11(10):913-923.
[39] THOMPSON K E, BASHOR C J, LIM W A, et al. SYNZIP protein interaction toolbox: in vitro and in vivo specifications of heterospecific coiled-coil interaction domains[J]. ACS Synthetic Biology, 2012, 1(4):118-129.
[40] HAHN M, STACHELHAUS T. Selective interaction between nonribosomal peptide synthetases is facilitated by short communication-mediating domains[J]. Proceedings of the National Academy of Sciences of the United States of America, 2004, 101(44):15585-15590.
[41] CHIOCCHINI C, LINNE U, STACHELHAUS T. In vivo biocombinatorial synthesis of lipopeptides by COM domain-mediated reprogramming of the surfactin biosynthetic complex[J]. Chemistry & Biology, 2006, 13(8):899-908.
[42] HAHN M, STACHELHAUS T. Harnessing the potential of communication-mediating domains for the biocombinatorial synthesis of nonribosomal peptides[J]. Proceedings of the National Academy of Sciences of the United States of America, 2006, 103(2):275-280.
[43] KEGLER C, BODE H B. Artificial splitting of a non-ribosomal peptide synthetase by inserting natural docking domains[J]. Angewandte Chemie International Edition, 2020, 59(32):13463-13467.
[44] REINKE A W, GRANT R A, KEATING A E. A synthetic coiled-coil interactome provides heterospecific modules for molecular engineering[J]. Journal of the American Chemical Society, 2010, 132(17):6025-6031.
[45] BOZHUEYUEK K A J, WATZEL J, ABBOOD N, et al. Synthetic zippers as an enabling tool for engineering of non-ribosomal peptide synthetases[J]. Angewandte Chemie International Edition, 2021, 60(32):17531-17538.
[46] KLAUS M, D’SOUZA A D, NIVINA A, et al. Engineering of chimeric polyketide synthases using SYNZIP docking domains[J]. ACS Chemical Biology, 2019, 14(3):426-433.
[47] RANG J, LI Y L, CAO L, et al. Deletion of a hybrid NRPS-T1PKS biosynthetic gene cluster via Latour gene knockout system in Saccharopolyspora pogona and its effect on butenyl-spinosyn biosynthesis and growth development[J]. Microbial Biotechnology, 2021, 14(6):2369-2384.
[48] GEIB E, BALDEWEG F, DOERFER M, et al. Cross-chemistry leads to product diversity from atromentin synthetases in aspergilli from section nigri[J]. Cell Chemical Biology, 2019, 26(2):223-234.e6.
[49] TAYLOR J T, MUKHERJEE P K, PUCKHABER L S, et al. Deletion of the Trichoderma virens NRPS, Tex7, induces accumulation of the anti-cancer compound heptelidic acid[J]. Biochemical and Biophysical Research Communications, 2020, 529(3):672-677.
[50] LIU X F, HUANG C R, BERGEN P J, et al. Chinese consensus guidelines for therapeutic drug monitoring of polymyxin B, endorsed by the Infection and Chemotherapy Committee of the Shanghai Medical Association and the Therapeutic Drug Monitoring Committee of the Chinese Pharmacological Society[J]. Journal of Zhejiang University. Science. B, 2023, 24(2):130-142.
[51] MOOTZ H D, MARAHIEL M A. Biosynthetic systems for nonribosomal peptide antibiotic assembly[J]. Current Opinion in Chemical Biology, 1997, 1(4):543-551.
[52] STACHELHAUS T, SCHNEIDER A, MARAHIEL M A. Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains[J]. Science, 1995, 269(5220):69-72.
[53] NGUYEN K T, HE X W, ALEXANDER D C, et al. Genetically engineered lipopeptide antibiotics related to A54145 and daptomycin with improved properties[J]. Antimicrobial Agents and Chemotherapy, 2010, 54(4):1404-1413.
[54] DHANEESHA M, BENJAMIN NAMAN C, KRISHNAN K P, et al. Streptomyces artemisiae MCCB 248 isolated from Arctic fjord sediments has unique PKS and NRPS biosynthetic genes and produces potential new anticancer natural products[J]. 3 Biotech, 2017, 7(1):32.
[55] SUBKO K, WANG X H, NIELSEN F H, et al. Mass spectrometry guided discovery and design of novel asperphenamate analogs from Penicillium astrolabium reveals an extraordinary NRPS flexibility[J]. Frontiers in Microbiology, 2021, 11:618730.
[56] IORIO M, GENTILE A, BRUNATI C, et al. Allopeptimicins: Unique antibacterial metabolites generated by hybrid PKS-NRPS, with original self-defense mechanism in Actinoallomurus[J]. RSC Advances, 2022, 12(26):16640-16655.