Chemically synthesized ubiquitin extension proteins detect distinct catalytic capacities of deubiquitinating enzymes

Layfield, RFranklin, KLandon, MWalker, GWang, PRamage, RBrown, Anthony Hugh DeanLove, SUrquhart, KMuir, TBaker, RohanMayer, R. John2015-12-130003-2697http://hdl.handle.net/1885/92521We have used solid-phase chemistry to synthesize proteins equivalent to a human ubiquitin precursor (ubiquitin-52-amino-acid ribosomal protein fusion; UBICEP52) and representative of isopeptide-linked ubiquitin-protein conjugates [ubiquitin-(εN)-lysine];Keywords: cysteine proteinase; lysine; peptidase; proteasome; protein precursor; ribosome protein; synthetic peptide; ubiquitin; valine; article; catalysis; conjugate; controlled study; enzyme activity; enzyme specificity; enzyme substrate; escherichia coli; nonhumChemically synthesized ubiquitin extension proteins detect distinct catalytic capacities of deubiquitinating enzymes199910.1006/abio.1999.42342015-12-12