Ocean University of China

Huayue Li

Wenli Li

Jing Liu

Tingting Yao

Tong Li

Yang Liu

Fei Xiao

An enzyme with an acyl transfer function has an amino acid sequence identical to a SEQ ID NO:, which is capable of acylation modification for macrolactins, filipins macrolides, chloramphenicol, and glycosylated piericidin A. An application of an acyltransferase of the present invention is to bind an acyl group of an acyl donor to macrolide compounds, chloramphenicol and glycosylated piericidins. The enzyme with the acyl transfer function can improve pharmacological activity of the macrolide compounds through acylation reaction of macrolactins, thereby improving bioavailability, enhancing efficacy, and reducing toxic as well as side effects, which provides a new strategy for the drug development of macrolide compounds.

Enzyme with acyl transfer function and application thereof

A novel PSL family prenyltransferase has relaxed substrate specificity, which can use a variety of cyclic dipeptides and prenyl donors as substrates to produce various terpenylated diketopiperazines. An amino acid sequence of the prenyltransferase is SEQ ID NO: 1. An application of the prenyltransferase is transferring different prenyl groups to Trp-containing cyclic dipeptides. The prenyltransferase catalyzes the formation of terpenylated diketopiperazines by assembling prenyl groups onto cyclic dipeptides, which provides a new strategy for drug development of diketopiperazines.

Method for assembling prenyl groups onto cyclic dipeptides

A novel PSL family prenyltransferase has relaxed substrate specificity, which can use a variety of cyclic dipeptides and prenyl donors as substrates to produce various terpenylated diketopiperazines. An amino acid sequence of the prenyltransferase is SEQ ID NO:1. An application of the prenyltransferase is transferring different prenyl groups to Trp-containing cyclic dipeptides. The prenyltransferase catalyzes the formation of terpenylated diketopiperazines by assembling prenyl groups onto cyclic di peptides, which provides a new strategy for drug development of diketopiperazines.

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Shandong, China

Huayue Li