Characterization of the endopeptidase activity of tripeptidyl-peptidase II
作者： Sandra Eklund , Jakob Dogan , Per Jemth , Hubert Kalbacher , Birgitta Tomkinson
DOI: 10.1016/J.BBRC.2012.06.144
关键词:
摘要: Abstract Tripeptidyl-peptidase II (TPP II) is a giant cytosolic peptidase with proposed role in cellular protein degradation and protection against apoptosis. Beside its well-characterised exopeptidase activity, TPP also has an endopeptidase activity. Little known about this since it could be important for the physiological of II, we have investigated more detail. Two peptides, Nef69–87 LL37, were incubated wild-type murine variants thereof as well from human Drosophila melanogaster. intrinsically disordered proteins included study. We conclude that activity promiscuous than previously reported. It clear can attack longer peptides up to 75 amino acid residues. Using novel FRET substrate, catalytic efficiency determined 5 orders magnitude lower
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