Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/143326
Title: One enzyme with two functions : how to train proteases to perform ligation
Authors: Kay, Senica Zi Ning
Keywords: Science::Biological sciences
Issue Date: 2020
Publisher: Nanyang Technological University
Abstract: Cyclotides, a class of plant-derived cysteine-rich cyclic proteins, are an attractive framework for drug design. Asparaginyl endopeptidases (AEPs) are enzymes that are associated with proteolysis, but there is a class of AEPs that catalyze the backbone cyclization of cyclotide precursors. Here, we report on how to train the bifunctional AEP McPAL-1 to carry out ligation by changing influencing factors. We found that AEPs are substrate specific and the P2” residue affects the directionality of McPAL-1’s activity. The P1 residue and pH is also a determinant of AEP activity. Additionally, we note that the C-terminus of substrates play an important role in catalyzing enzyme reactions. We also made the discovery that previously thought to be ligase-type and protease-type AEPs, are actually all bifunctional in activity.
URI: https://hdl.handle.net/10356/143326
Fulltext Permission: restricted
Fulltext Availability: With Fulltext
Appears in Collections:SBS Student Reports (FYP/IA/PA/PI)

Files in This Item:
File Description SizeFormat 
skay003.pdf
  Restricted Access
1.83 MBAdobe PDFView/Open

Page view(s)

240
Updated on Dec 9, 2022

Download(s)

1
Updated on Dec 9, 2022

Google ScholarTM

Check

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.