Specificity and mode of action of the muscle-type protein-arginine deiminase
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Cited by (39)
Autocitrullination of PAD4 does not alter its enzymatic activity: In vitro and in silico studies
2021, International Journal of Biochemistry and Cell BiologyCitation Excerpt :We investigated the kinetic properties of PAD4 and citPAD4 towards substrates of different size. Free arginine was used as small-sized substrate since we found that PAD4 is able to convert free L-arginine to L-citrulline, which is contrast to previous reports (Nomura, 1992; Takahara et al., 1986). Further, a short arginine-containing peptide, CS-21(66), was chosen as medium-sized PAD4 substrate.
Extracellular vesicles and post-translational protein deimination signatures in haemolymph of the American lobster (Homarus americanus)
2020, Fish and Shellfish ImmunologyPost-translational protein deimination signatures and extracellular vesicles (EVs) in the Atlantic horseshoe crab (Limulus polyphemus)
2020, Developmental and Comparative ImmunologyCitation Excerpt :Protein structures that have been identified to be most prone to undergo deimination are intrinsically disordered proteins and beta-sheets (Tarcsa et al., 1996; György et al., 2006). The position of the arginine furthermore is of importance as arginines placed next to aspartic acid residues are most prone to deimination/citrullination, but arginines that are next to glutamic acid residues are rarely deiminated/citrullinated and arginines that are flanked by proline are poorly deiminated/citrullinated (Nomura, 1992; György et al., 2006). A number of species-specific deiminated protein candidates for Limulus polyphemus, and with other Merostomata, were identified in the current study in horseshoe crab serum using F95-enrichment in tandem with LC-MS/MS analysis.
Post-translational modifications such as citrullination are excellent targets for cancer therapy
2020, Seminars in ImmunologyDeiminated proteins in extracellular vesicles and serum of llama (Lama glama)—Novel insights into camelid immunity
2020, Molecular ImmunologyCitation Excerpt :This can cause functional and structural changes in target proteins (Vossenaar, 2003; György et al., 2006; Wang and Wang, 2013; Bicker and Thompson, 2013). Structures most prone to deimination are beta-sheets and intrinsically disordered proteins, while the position of the arginine is also important; arginines sitting next to aspartic acid residues are most prone to citrullination, arginines next to glutamic acid residues are rarely citrullinated and those flanked by proline are poorly citrullinated (Nomura, 1992; Tarcsa et al., 1996; György et al., 2006). Protein deimination can affect gene regulation, cause generation of neoepitopes (Witalison et al., 2015; Lange et al., 2017) and may also allow for protein moonlighting, an evolutionary acquired phenomenon facilitating proteins to exhibit several physiologically relevant functions within one polypeptide chain (Henderson and Martin, 2014; Jeffrey, 2018; Magnadóttir et al., 2018a).
Development of a highly sensitive fluorescence probe for peptidyl arginine deiminase (PAD) activity
2019, Bioorganic and Medicinal Chemistry LettersCitation Excerpt :Next, to examine potential applicability for high-throughput screening, we measured the fluorescence intensity after cycloaddition reaction with l-citrulline with a microplate reader (Fig. S3), and observed significant fluorescence increments especially with 4MEBz-FluCOOH, 4MEBz-FluME and diCF3Bz-FluME. However, in this experiment, we used l-citrulline, whose amino and carboxyl groups are not protected, so its reactivity with the benzil-type fluorescence probes may be different from that of Nα-benzoyl-l-citrulline ethyl ester (BCEE), which is the actual product of the enzymatic reaction of Nα-benzoyl-l-arginine ethyl ester (BAEE), a well-known artificial substrate for PADs44. Thus, we performed the same functional evaluation using commercially available Nα-benzoyl-l-citrulline methyl ester (BCME).