title: Synthesis of N-Hydroxy Isopeptide Containing Proteins.
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.
authors.affiliation: Schulich Faculty of Chemistry Technion-Israel Institute of Technology, 3200008 Haifa, Israel.
authors.forename: Suman Kumar
authors.initials: SK
authors.lastname: Maity
authors.affiliation: Schulich Faculty of Chemistry Technion-Israel Institute of Technology, 3200008 Haifa, Israel.
authors.forename: Shimrit
authors.initials: S
authors.lastname: Ohayon
authors.affiliation: Schulich Faculty of Chemistry Technion-Israel Institute of Technology, 3200008 Haifa, Israel.
authors.forename: Ashraf
authors.initials: A
authors.lastname: Brik
mesh_terms: D002384:Catalysis; D006868:Hydrolysis; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry; D013379:Substrate Specificity; D064570:Ubiquitin-Specific Proteases / Q000737:chemistry*; D014452:Ubiquitins / Q000138:chemical synthesis* / Q000737:chemistry; D015032:Zinc / Q000737:chemistry
chemical_list: D010455:Peptides; D011506:Proteins; D014452:Ubiquitins; D064570:Ubiquitin-Specific Proteases; D015032:Zinc