Developing crosslinkers specific for epimerization domain in NRPS initiation modules to evaluate mechanism

Kim, Woojoo E.; Ishikawa, Fumihiro; Re, Rebecca N.; Suzuki, Takehiro; Dohmae, Naoshi; Kakeya, Hideaki; Tanabe, Genzoh; Burkart, Michael D.

doi:10.1039/d2cb00005a

Cited by 4 publications

(3 citation statements)

References 33 publications

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“…Before the condensation reaction takes place, it is possible that each T domain may require interaction with additional tailoring domains, such as the E domain. The E domain plays a role in modifying the substrate carried by each module, including the ability to catalyze racemization ( Kim et al, 2022 ). Once the peptide chain reaches the termination module, the product is released by a thioesterase (TE) domain through hydrolysis or intramolecular cyclization.…”

Section: Introductionmentioning

confidence: 99%

Structure modification of an antibiotic: by engineering the fusaricidin bio-synthetase A in Paenibacillus polymyxa

Li,

Chen

2023

Front. Microbiol.

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Fusaricidin, a lipopeptide antibiotic, is specifically produced by Paenibacillus polymyxa strains, which could strongly inhibit Fusarium species fungi. Fusaricidin bio-synthetase A (FusA) is composed of six modules and is essential for synthesizing the peptide moiety of fusaricidin. In this study, we confirmed the FusA of Paenibacillus polymyxa strain WLY78 involved in producing Fusaricidin LI-F07a. We constructed six engineered strains by deletion of each module within FusA from the genome of strain WLY78. One of the engineered strains is able to produce a novel compound that exhibits better antifungal activity than that of fusaricidin LI-F07a. This new compound, known as fusaricidin [ΔAla6] LI-F07a, has a molecular weight of 858. Our findings reveal that it exhibits a remarkable 1-fold increase in antifungal activity compared to previous fusaricidin, and the fermentation yield reaches ~55 mg/L. This research holds promising implications for plant protection against infections caused by Fusarium and Botrytis pathogen infection.

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Section: Introductionmentioning

confidence: 99%

Structure modification of an antibiotic: by engineering the fusaricidin bio-synthetase A in Paenibacillus polymyxa

Li,

Chen

2023

Front. Microbiol.

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“…Some also have domains such as keepeduktase (KR), dehydratase (DH), enoylreduktase (ER), and methyltransferase (MT) to explain the large number of structurally complex and diverse metabolites available through this common pathway [20,21]. The domain of NRPS is usually composed of adenylation (A) and condensation (C) [22,23]. With our current technology, it is very difficult to obtain the TSs.…”

Section: Introductionmentioning

confidence: 99%

Genomic Comparison of Two Species of Samsoniella with Other Genera in the Family Cordycipitaceae

Lu,

Wang,

Wang

et al. 2023

JoF

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Whole genomes of Samsoniella hepiali ICMM 82-2 and S. yunnanensis YFCC 1527 were sequenced and annotated, as well as compared with whole genome sequences of other species in the family Cordycipitaceae. S. hepiali ICMM 82-2, S. hepiali FENG and S. yunnanensis YFCC 1527 had 54, 57 and 58 putative secondary metabolite biosynthetic gene clusters, respectively. S. hepiali had one unique domain and S. yunnanensis YFCC 1527 six. Both S. hepiali and S. yunnanensis YFCC 1527 had curvupallide-B, fumosorinone and fujikurin putative biosynthetic gene clusters. C. javanica had biosynthetic gene clusters for fumonisin. The 14 genomes had common domains, namely A-P-C-P-C and KS-AT-DH-ER-KR-ACP. The A-P-C-P-C domain may be involved in the biosynthesis of dimethylcoprogen. The maximum likelihood and the Bayesian inference trees of KS-AT-DH-ER-KR-ACP were highly consistent with the multigene phylogenetic tree for the 13 species of Cordycipitaceae. This study facilitates the discovery of novel biologically active SMs from Cordycipitaceae using heterologous expression and gene knockdown methods.

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“…Each module has a core C-A-T domain responsible for recognizing, activating, and loading the corresponding amino acid [ 9 ]. Some modules also have an Epimerization (E) domain, which can transform L-type amino acid to D-type amino acid to maintain the correct three-dimensional structure of the lipopetides [ 10 , 11 ]. In addition, there is a thioesterase (Te) domain at the end of the termination module, which is responsible for cyclizing and releasing the mature peptide products [ 12 ].…”

Section: Introductionmentioning

confidence: 99%

Translocation of subunit PPSE in plipastatin synthase and synthesis of novel lipopeptides

Gao

et al. 2022

Synthetic and Systems Biotechnology

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Developing crosslinkers specific for epimerization domain in NRPS initiation modules to evaluate mechanism

Abstract: Nonribosomal peptide synthetases (NRPSs) are complex multi-modular enzymes containing catalytic domains responsible for the loading and incorporation of amino acids into natural products. These unique molecular factories can produce peptides...

Cited by 4 publications

References 33 publications

Structure modification of an antibiotic: by engineering the fusaricidin bio-synthetase A in Paenibacillus polymyxa

Structure modification of an antibiotic: by engineering the fusaricidin bio-synthetase A in Paenibacillus polymyxa

Genomic Comparison of Two Species of Samsoniella with Other Genera in the Family Cordycipitaceae

Translocation of subunit PPSE in plipastatin synthase and synthesis of novel lipopeptides

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