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Post-Translational Modification Enzymes: How to Interrogate Key Drug Targets

Dr. Hicham Zegzouti is a Senior Research Scientist in Promega Assay Design-R&D. His group develops Assay technologies to interrogate diverse enzyme activities and cellular pathways (kinases, glycosyltransferases, and other drug targets). Dr. Zegzouti received his PhD in 1997 from the National Polytechnic Institute of Toulouse, France. Prior to joining Promega, he was a postdoctoral researcher in Molecular, Cell and Developmental Biology at UC-Los Angeles studying auxin hormone signaling in an Arabidopsis plant model. His work focused on the identification and characterization of AGC kinase family and its regulation during plant development. Dr. Zegzouti has authored 14 journal articles and book chapters, co-edited a methods book and is an inventor for one issued and 4 pending patents.
  • Hicham Zegzouti, PhD

  • Sr Research Scientist

  • Original Webinar Date: Tuesday, April 11, 2017

Post-translational modifications (PTMs), the addition of functional groups to proteins, play a significant role in regulating cellular biology. Examples include phosphorylation, a common mechanism in regulating enzymatic activity, and the addition of carbohydrates to many eukaryotic proteins, which promotes proper folding, improves stability and serves in regulatory functions. A key objective of research and drug discovery surrounding PTMs is to study the regulation of these enzymes and find specific modulators of their activity. Although mass spectrometry, eastern and western blotting detection technologies have been used traditionally, none are amenable to high throughput or as sensitive as bioluminescent detection of nucleotide-based substrates for such enzymes.

Post-translational modifications (PTMs) amplify diverse cellular functions by covalently adding functional groups such as phosphate, acetate, amide, or methyl groups to proteins. The PTM enzymes and resulting modifications are too numerous to list here. Phosphorylation, a common mechanism in regulating downstream cellular signaling (i.e., via kinases), is one of the most common PTMs. Many eukaryotic proteins can also be modified by glycosylation. Attaching carbohydrates to proteins is implicated in protein folding, improved stability and other regulatory functions such as signaling. Environmental or pathological conditions can lead to dysregulation of PTM activities resulting in the perturbation of the intracellular networks governed by each. As a result, PTM enzymes such as kinases and glycosyltransferases are targets or are starting to be targeted for drug development.

Traditional assay technologies such as mass spectrometry, or antibody-based techniques such as ELISA or western blotting are cumbersome and not easily amenable to high throughput drug discovery. We have developed a detection technology platform highly suitable to screening of PTM enzymatic activities when nucleotides are substrates or products. In this webinar we will demonstrate how cellular mechanisms driven by PTM can be addressed by analyzing the biochemical activities of the involved enzymes using a simple suite of bioluminescent nucleotide detection assays.

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