One enzyme with two functions : how to train proteases to perform ligation
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 r...
| Main Author: | |
|---|---|
| Other Authors: | |
| Format: | Final Year Project (FYP) |
| Language: | English |
| Published: |
Nanyang Technological University
2020
|
| Subjects: | |
| Online Access: | https://hdl.handle.net/10356/143326 |
| _version_ | 1826128545277018112 |
|---|---|
| author | Kay, Senica Zi Ning |
| author2 | James P Tam |
| author_facet | James P Tam Kay, Senica Zi Ning |
| author_sort | Kay, Senica Zi Ning |
| collection | NTU |
| description | 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. |
| first_indexed | 2024-10-01T07:26:41Z |
| format | Final Year Project (FYP) |
| id | ntu-10356/143326 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T07:26:41Z |
| publishDate | 2020 |
| publisher | Nanyang Technological University |
| record_format | dspace |
| spelling | ntu-10356/1433262023-02-28T18:08:11Z One enzyme with two functions : how to train proteases to perform ligation Kay, Senica Zi Ning James P Tam School of Biological Sciences JPTam@ntu.edu.sg Science::Biological sciences 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. Bachelor of Science in Biological Sciences 2020-08-24T05:40:11Z 2020-08-24T05:40:11Z 2020 Final Year Project (FYP) https://hdl.handle.net/10356/143326 en application/pdf Nanyang Technological University |
| spellingShingle | Science::Biological sciences Kay, Senica Zi Ning One enzyme with two functions : how to train proteases to perform ligation |
| title | One enzyme with two functions : how to train proteases to perform ligation |
| title_full | One enzyme with two functions : how to train proteases to perform ligation |
| title_fullStr | One enzyme with two functions : how to train proteases to perform ligation |
| title_full_unstemmed | One enzyme with two functions : how to train proteases to perform ligation |
| title_short | One enzyme with two functions : how to train proteases to perform ligation |
| title_sort | one enzyme with two functions how to train proteases to perform ligation |
| topic | Science::Biological sciences |
| url | https://hdl.handle.net/10356/143326 |
| work_keys_str_mv | AT kaysenicazining oneenzymewithtwofunctionshowtotrainproteasestoperformligation |