Advances in the Biosynthesis of Nonribosomal Peptide

doi:10.13523/j.cb.2302010

China Biotechnology

2023, Vol. 43

Issue (8): 86-99 DOI: 10.13523/j.cb.2302010

Advances in the Biosynthesis of Nonribosomal Peptide

JIANG Ji-peng,SUN Ya-nan,ZHANG Chen-chen,HAO Man,LI Xiang-xun,LIU Fu-feng,WANG Hai-kuan,LU Fu-ping,ZHANG Hui-tu^**(

)

Laboratory of Applied Microbiology and Enzyme Engineering, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China

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Abstract

Nonribosomal peptides are a class of small molecule secondary metabolites synthesized by a variety of microorganisms through nonribosomal peptide synthetase and other catalytic synthesis. With antibacterial, antitumor, immunosuppressive and other biological activities, they are an important class of microbial drugs, with high clinical application value. This paper reviews the biological functions, synthesis and assembly mechanisms of small molecule peptides, as well as the recent progress in engineering modifications, and discusses future research directions for the efficient synthesis of more types of small molecule peptides through combinatorial biosynthesis.

Key words： Nonribosomal peptide Nonribosomal peptide synthetase Multi-enzyme complex Combinatorial biosynthesis

Received: 06 February 2023 Published: 05 September 2023

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	Ji-peng JIANG
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	Fu-ping LU
	Hui-tu ZHANG

Cite this article:

JIANG Ji-peng, SUN Ya-nan, ZHANG Chen-chen, HAO Man, LI Xiang-xun, LIU Fu-feng, WANG Hai-kuan, LU Fu-ping, ZHANG Hui-tu. Advances in the Biosynthesis of Nonribosomal Peptide. China Biotechnology, 2023, 43(8): 86-99.

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https://manu60.magtech.com.cn/biotech/10.13523/j.cb.2302010 OR https://manu60.magtech.com.cn/biotech/Y2023/V43/I8/86

Fig.1 Structures of several nonribosomal peptides

Table 1 Common reported nonribosomal peptide drugs

Fig.2 Schematic diagram of basic structure and biosynthesis mechanism of NRPS

Fig.3 NRPS pathway in the biosynthesis of Ramoplanin

Fig.4 Yersiniabactin and NRPS involved in its biosynthesis

Fig.5 NRPS pathway in the biosynthesis of Myxochromide S

涉及NRPS	具体手段	结果	参考文献
Surfactin 合成酶SrfA-C	异源替换A域	获得系列7位氨基酸取代的 Surfactin 类似物,但产量均明显下降	[36]
Gramicidin S 合成酶	替换A域的亚结构域FSD	改变了起始模块A域的底物特异性,但未充分证明重组NRPS是否有活性	[37]
Enduracidin 合成酶	用CRISPR-Cas9技术替换FSD	得到了一些产量接近天然NRPS的新型脂肽	[38]
Andrimid合成酶	对“特异性代码”进行饱和突变	高通量筛选得到4种新型Andrimid类似物	[39]
Tyrocidine合成酶	采用饱和突变的定向进化手段	A域产生40 000倍的α / β特异性转变,且能以近似原酶的效率合成含β-氨基酸的NRP	[40]
Enterobactin合成酶	对芳基酸特异识别A域进行单点突变	A域的底物结合口袋扩大,可以活化多种经过修饰的非天然芳基酸	[41]
Thiocoraline合成酶	在A域保守特征序列间插入M域	得到具有腺苷化、N-甲基化和S-甲基化三种活性的A域	[42]
Echinomycin合成酶	在A域保守特征序列间插入2个连续的M域	A域的腺苷化活性被保留,但以两种顺序插入M结构域均未引起预期的甲基化能力增加	[43]
Pyoverdine合成酶PvdD	异源替换起始模块的C-A域	获得了少数几个产Pyoverdine及其类似物的重组NRPS,但与原酶相比合成效率极度下降	[44]
Tyrocidine合成酶	以C-A-T为基本单元将多个模块进行重组	获得了预期三肽产物	[45]
Ambactin等的生物合成酶	定义A-T-C作为XU交换单元进行多结构域替换	获得的重组NRPS可以合成新型NRP,甚至有些NRP的产量较野生型有很大提升	[46]
Ambactin等的生物合成酶	定义C_Asub-A-T-C_Dsub作为XUC交换单元进行多模块重组替换	解决了杂合NRPS上下游C域和A域不适配的问题,使某些肽的产量提高1.6倍	[47]
Plipastatin合成酶	对通信域进行氨基酸定点突变	获得了具有抗微生物活性的新型多肽产物	[48]
Rhabdopeptide/Xenortide(RXP)合成酶	替换通信域间相互作用的关键残基	获得了不同于原产物链长的RXP	[49]
Rhabdopeptide/Xenortide(RXP)合成酶	用两种不同NRPS的通信域替换RXP合成酶的通信域	获得了特定链长和结构的新型RXP	[50]
Xefoampeptide合成酶 XfpS	引入天然通信域将XfpS拆分成2到3个人工NRPS亚单元	得到的某些拆分XfpS比完整野生型酶肽产量更高	[51]
Gramicidin S合成酶GrsB	引入天然通信域拆分GrsB	拆分蛋白质异源表达的产率和纯度得到了提高	[52]
Xefoampeptide合成酶 XfpS	利用“合成拉链”将不同来源的NRPS片段结合	合成了滴度高达220 mg/L的新肽	[53]
GameXPeptide(GXP)合成酶GxpS	利用合成拉链将NRPS分成多达3个亚基	构建了不同的双模块和三模块NRPS文库,产生了49个多肽、多肽衍生物和从头合成肽,滴度高达145 mg/L	[54]

Table 2 Research progress of partial NRPS engineering


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