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首页> 美国卫生研究院文献>Scientific Reports >One-pot synthesis of class II lanthipeptide bovicin HJ50 via an engineered lanthipeptide synthetase
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One-pot synthesis of class II lanthipeptide bovicin HJ50 via an engineered lanthipeptide synthetase

机译：通过工程化的多肽肽合成酶一锅法合成II类多肽肽Bovicin HJ50

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摘要

Lanthipeptides are a large class of bacteria-produced, ribosomally-synthesized and post-translationally modified peptides. They are recognized as peptide antibiotics because most of them exhibit potent antimicrobial activities against Gram-positive bacteria especially those that are phylogenetically related to producers. Maturation of class II lanthipeptide like bovicin HJ50 undergoes precursor modification by LanM and a subsequent leader peptide cleavage by LanT. Herein, via co-expression of precursor gene bovA, modification gene bovM and transporter gene bovT in Escherichia coli C43 (DE3), bioactive bovicin HJ50 was successfully produced and secreted. To further achieve in vitro one-pot synthesis of bovicin HJ50, an engineered bovicin HJ50 synthetase BovT150M was obtained by fusing the peptidase domain of BovT (BovT150) to the N-terminus of BovM. BovT150M exhibited dual functions of precursor modification and leader peptide cleavage to release mature bovicin HJ50. Under the guidance of BovA leader peptide, BovT150M exhibited substrate tolerance to modify non-native substrates including suicin and lacticin 481. This work exemplifies the feasibility of enzyme chimera of peptidase domain (LanT150) and modification enzyme (LanM) as a one-pot lanthipeptide synthetase.
机译：多肽是一类细菌产生的，核糖体合成的和翻译后修饰的肽。它们被认为是肽类抗生素，因为它们大多数对革兰氏阳性细菌，特别是与生产者发生系统发育的细菌，表现出有效的抗菌活性。 II类lantepteptide的成熟，如bovicin HJ50，会受到LanM的前体修饰，随后会受到LanT的前导肽切割。在此，通过在大肠杆菌C43（DE3）中共表达前体基因bovA，修饰基因bovM和转运蛋白基因bovT，成功地生产并分泌了具有生物活性的波维菌素HJ50。为了进一步实现波维菌素HJ50的体外一锅法合成，通过将BovT的肽酶结构域（BovT150）融合到BovM的N末端，获得了工程化的波维菌素HJ50合成酶BovT150M。 BovT150M表现出前体修饰和前导肽裂解双重功能，以释放成熟的波维菌素HJ50。在BovA前导肽的指导下，BovT150M表现出对修饰非天然底物（包括suicin和lacticin 481）的底物耐受性。这项工作例证了肽酶结构域（LanT150）和修饰酶（LanM）作为一罐长肽的酶嵌合体的可行性。合成酶。

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