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[SBS Seminar] Peptide asparaginyl ligases as versatile biotechnological tools for the development of protein based theranostics
Peptide asparaginyl ligases ( catalyze transpeptidation reactions at Asx Xaa peptide bonds Structurally, PALs belong to a family of proteases known as asparaginyl endopeptidases ( or legumains that are found in many organisms In plants, many AEPs exert dual endopeptidase ( and transpeptidase (functions and are responsible for post translational
processing and biosynthesis of certain seed proteins and Cys rich cyclotides Butelase 1 is the first member of this
family of enzymes that is characterized as a pure PAL As the most efficient peptide ligase known to date, butelase 1
has found many useful applications, such as peptide/protein macrocyclization and labeling and cell surface modification
Recently, VyPAL 2 a new PAL discovered from the cyclic peptide producing plant Viola yedoensis was shown to be
also a highly efficient ligase Because very short peptide motifs are required for substrate recognition, PAL mediated
ligation reactions leave minimal traces in the products In this talk, we will first give a brief review on the PAL enzymes
and then present their use as a versatile biotechnological tool in biomedical research and for the development of
protein based theranostics