Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/154929
Title: Asparaginyl endopeptidase : a multifaceted enzyme for making and breaking peptide bonds
Authors: Liew, Heng Tai
Keywords: Science::Biological sciences::Biochemistry
Issue Date: 2021
Publisher: Nanyang Technological University
Source: Liew, H. T. (2021). Asparaginyl endopeptidase : a multifaceted enzyme for making and breaking peptide bonds. Doctoral thesis, Nanyang Technological University, Singapore. https://hdl.handle.net/10356/154929
Abstract: Asparaginyl endopeptidases (AEPs), or legumains, are Asn/Asp (Asx)-specific proteases. Plant AEPs have multifaceted roles in nature, including seed storage protein maturation and cyclic peptides production. They are also useful biological tools for precision modification and biomanufacturing of peptides and proteins. Besides, substrate-binding pockets and pH have been shown recently as the major factors affecting the AEP's ligase and protease activity. However, how the substrates affect the AEP's enzymatic directionality is still poorly understood. Here, we have shown that protease-AEPs could perform ligation using specific peptide substrates. This study is important as it would expand the utility of these AEPs in biotechnological applications and highlight the need to elucidate ligation mechanisms in AEPs. Besides, we have also discovered and characterized a highly stable Asx-ligase displaying a pH-dependent enzymatic profile from Momordica cochinchinensis. McPAL1 catalyzes both P1-Asp ligation and P1-Asn hydrolysis from pH 4 to 6, but predominantly Asn-ligation at pH 6.5-8, making it a valuable tool for peptide and protein engineering and cell surface modification.
URI: https://hdl.handle.net/10356/154929
DOI: 10.32657/10356/154929
Rights: This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0).
Fulltext Permission: embargo_20240130
Fulltext Availability: With Fulltext
Appears in Collections:SBS Theses

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