Substrate phosphorylation can inhibit proteolysis by trypsin-like enzymes☆
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Intracellular peptides as drug prototypes
2022, Peptide and Peptidomimetic Therapeutics: From Bench to BedsideElectrochemical, electrochemiluminescent and photoelectrochemical bioanalysis of epigenetic modifiers: A comprehensive review
2020, Coordination Chemistry ReviewsCitation Excerpt :To accurate and selective detection of phosphoprotein and assay of protein kinase activity, the high specific recognition of phosphoprotein is challenging. The basic method for phosphoprotein recognition mainly contains the following patterns: (1) phosphor-specific recognition protein, such as anti-phosphoserine antibody [270], phosphopeptide-binding protein [271,272], (2) Metal chelator, such as phos-tag-biotin [273], (3) ATP analogs labeled with active group, such as –SH, biotin and ferrocene [274–277], (4) metal ion or metal-based nanomaterial, such as Zr4+ [278], TiO2 [279], Fe3O4@hYPO4 [280], ZnO [281], Zr-MOF [282], (5) ATP concentration change [283], (6) inhibited proteolytic enzyme activity by phosphorylation, such as carboxypeptidase Y and trypsin [284]. Most of these patterns have been applied in the field of protein phosphorylation detection and protein kinase activity assay based on electrochemical methods (Table S7 and Fig. 24).
Analysis and Interpretation of Protein Post-Translational Modification Site Stoichiometry
2019, Trends in Biochemical SciencesCitation Excerpt :This is feasible for some PTMs, such as phosphorylation, but may not be extendible to other PTMs due to unavailability of suitable PTM-removing enzymes. In some instances, phosphorylation near Arg and Lys can reduce the kinetics of trypsin proteolysis [36,37]; this may lead to different phosphorylated and CP sequences and could affect stoichiometry estimation. Most critically, the above-discussed approaches require that changes in CP abundance are measurable.
Purification and identification of β-casein phosphopeptide (1-25)
2016, Journal of Dairy ScienceCitation Excerpt :Such degradation was likely due to the continued exposure to the enzymatic solution. It has been shown that the N terminus 1–25 peptide fragment of β-CN is resilient against proteolysis given its 4 phosphorylated serines that sterically hinder enzymatic cleavage of the amide bonds (Benore-Parsons et al., 1989). Though this steric hindrance may reduce the degradation, extended exposure to peptidases such as trypsin can eventually lead to degradation of βCPP (Boutrou et al., 2010).
Extracellular phosphorylation of collagen XVII by ecto-casein kinase 2 inhibits ectodomain shedding
2007, Journal of Biological Chemistry
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Portions of this work were presented at the 1987 ASBC conference (Benore-Parsons, M., and Wennogle, L. P. (1987) Fed. Proc.46, 2086).