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https://hdl.handle.net/10356/143326
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DC Field | Value | Language |
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dc.contributor.author | Kay, Senica Zi Ning | en_US |
dc.date.accessioned | 2020-08-24T05:40:11Z | - |
dc.date.available | 2020-08-24T05:40:11Z | - |
dc.date.issued | 2020 | - |
dc.identifier.uri | https://hdl.handle.net/10356/143326 | - |
dc.description.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. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Nanyang Technological University | en_US |
dc.subject | Science::Biological sciences | en_US |
dc.title | One enzyme with two functions : how to train proteases to perform ligation | en_US |
dc.type | Final Year Project (FYP) | en_US |
dc.contributor.supervisor | James P Tam | en_US |
dc.contributor.school | School of Biological Sciences | en_US |
dc.description.degree | Bachelor of Science in Biological Sciences | en_US |
dc.contributor.supervisoremail | JPTam@ntu.edu.sg | en_US |
item.fulltext | With Fulltext | - |
item.grantfulltext | restricted | - |
Appears in Collections: | SBS Student Reports (FYP/IA/PA/PI) |
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File | Description | Size | Format | |
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skay003.pdf Restricted Access | 1.83 MB | Adobe PDF | View/Open |
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