Dataset Information

Asparaginyl endopeptidases: enzymology, applications and limitations.

ABSTRACT: Asparaginyl endopeptidases (AEP) are cysteine proteases found in mammalian and plant cells. Several AEP isoforms from plant species were found to exhibit transpeptidase activity which is integral for the key head-to-tail cyclisation reaction during the biosynthesis of cyclotides. Since many plant AEPs exhibit excellent enzyme kinetics for peptide ligation via a relatively short substrate recognition sequence, they have become appealing tools for peptide and protein modification. In this review, research focused on the enzymology of AEPs and their applications in polypeptide cyclisation and labelling will be presented. Importantly, the limitations of using AEPs and opportunities for future research and innovation will also be discussed.

SUBMITTER: Tang TMS

PROVIDER: S-EPMC8209628 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Asparaginyl endopeptidases: enzymology, applications and limitations.

Tang T M Simon TMS Luk Louis Y P LYP

Organic & biomolecular chemistry 20210601 23

Asparaginyl endopeptidases (AEP) are cysteine proteases found in mammalian and plant cells. Several AEP isoforms from plant species were found to exhibit transpeptidase activity which is integral for the key head-to-tail cyclisation reaction during the biosynthesis of cyclotides. Since many plant AEPs exhibit excellent enzyme kinetics for peptide ligation via a relatively short substrate recognition sequence, they have become appealing tools for peptide and protein modification. In this review, ...[more]

PMID: 34037066

Similar Datasets

Project description:BackgroundFascioliasis is a zoonotic parasitic disease caused by Fasciola hepatica and Fasciola gigantica, which poses a serious threat to global public health and livestock farming. Fasciola gigantica secretes and excretes various components to manipulate the immune response, thereby enhancing its invasion, migration, and survival in vivo. However, the roles of specific components in immune modulation, such as asparagine endopeptidase, remain unknown.MethodsThe transcriptional abundance of members of the asparagine endopeptidase family (also known as the legumain family) from F. gigantica was analyzed. Two highly transcribed asparagine endopeptidases in metacercariae, juveniles and adults were cloned, and their recombinant proteins-recombinant F. gigantica legumain (rFgLGMN-1) and (rFgLGMN-2)-were expressed in prokaryotic expression system. Their regulatory effects on buffalo peripheral blood mononuclear cells (PBMCs), including proliferation, migration, total nitric oxide (NO) production, cytokine secretion, and phagocytosis were explored in vitro.ResultsTen members of the legumain family were detected in F. gigantica, among of which FgLGMN-1 and FgLGMN-2 exhibited high transcription levels in juveniles and adults. The isolation of sequences indicated that FgLGMN-1 encodes 409 amino acids, while FgLGMN-2 encodes 403 amino acids. Both recombinant FgLGMN-1 (rFgLGMN-1) and rFgLGMN-2 were recognized by serum from buffaloes infected with F. gigantica. Both rFgLGMN-1 and rFgLGMN-2 inhibited the proliferation of PBMCs, and rFgLGMN-1 also inhibited the migration of PBMCs. While rFgLGMN-1 increased the production of total NO, rFgLGMN-2 decreased NO production. Both rFgLGMN-1 and rFgLGMN-2 increased the transcription of the cytokines interleukin-10 and transforming growth factor β. The effect of rFgLGMN-1 and rFgLGMN-2 on the phagocytosis of PBMCs varied depending on their concentrations.ConclusionsrFgLGMN-1 and rFgLGMN-2 modulate several cellular and immunological functions of PBMCs, and exhibited distinct regulatory effects on these in vitro, which indicated that they may play roles in immune modulation and facilitate fluke development. However, due to uncertainties associated with in vitro experiments, further studies are necessary to elucidate the precise functions of these legumains.

Dataset Information

Asparaginyl endopeptidases: enzymology, applications and limitations.

Publications

Asparaginyl endopeptidases: enzymology, applications and limitations.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets