Title: Characteristic fragment ions associated with dansyl cadaverine and biotin cadaverine adducts on glutamine.
Authors: Biberoglu, Kevser; Schopfer, Lawrence M; Tacal, Ozden; Lockridge, Oksana
Published In Anal Biochem, (2020 07 01)
Abstract: Glutamine residues susceptible to transglutaminase-catalyzed crosslinking can be identified by incorporation of dansyl cadaverine or biotin cadaverine. Bacterial transglutaminase and human transglutaminase 2 were used to modify residues in beta-casein with dansyl cadaverine. Bacterial transglutaminase was used to modify residues in human butyrylcholinesterase with biotin cadaverine. Tryptic peptides were analyzed by LC-MS/MS on an Orbitrap Fusion Lumos mass spectrometer. Modified residues were identified in Protein Prospector searches of mass spectrometry data. The MS/MS spectra from modified casein included intense peaks at 336.2, 402.2, and 447.2 for fragments of dansyl cadaverine adducts on glutamine. The MS/MS spectra from modified butyrylcholinesterase included intense peaks at 329.2, 395.2, and 440.2 for fragments of biotin cadaverine adducts on glutamine. No evidence for transglutaminase-catalyzed adducts on glutamic acid, aspartic acid, or asparagine was found. Consistent with expectation, it was concluded that bacterial transglutaminase and human transglutaminase 2 specifically modify glutamine. The characteristic ions associated with dansyl cadaverine and biotin cadaverine adducts on glutamine are useful markers for modified peptides.
PubMed ID: 32335065
MeSH Terms: Biotin/chemistry*; Biotin/metabolism; Butyrylcholinesterase/metabolism; Cadaverine/chemistry*; Cadaverine/metabolism; Glutamine/chemistry*; Glutamine/metabolism; Humans; Ions/chemistry; Ions/metabolism; Streptomyces/enzymology; Transglutaminases/metabolism