Abstract
Chemical synthesis of a peptide-ubiquitin conjugate linked by an N-hydroxy isopeptide bond to determine what effect the N-hydroxy group has on the enzymatic hydrolysis of the isopeptide linkage by deubiquitinases is reported. This conjugate was subjected to proteolysis by UCH-L3 in the presence and absence of various metal ions, and no substantive difference in hydrolysis was seen compared to a control lacking the N-hydroxy group. The accessibility of N-hydroxy ubiquitinated substrates may find uses to study other deubiquitinases in particular those which use a zinc ion as a part of their catalytic mechanism.
Original language | English |
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Pages (from-to) | 3438-3441 |
Number of pages | 4 |
Journal | Organic Letters |
Volume | 17 |
Issue number | 14 |
DOIs | |
State | Published - 17 Jul 2015 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Physical and Theoretical Chemistry
- Organic Chemistry