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dc.contributor.authorKay, Senica Zi Ningen_US
dc.description.abstractCyclotides, 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.publisherNanyang Technological Universityen_US
dc.subjectScience::Biological sciencesen_US
dc.titleOne enzyme with two functions : how to train proteases to perform ligationen_US
dc.typeFinal Year Project (FYP)en_US
dc.contributor.supervisorJames P Tamen_US
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.description.degreeBachelor of Science in Biological Sciencesen_US
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Appears in Collections:SBS Student Reports (FYP/IA/PA/PI)
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