Is the ubiquitination relatively stable or highly dynamic?  how does ubiquitination become detached from the protein of interest? what enzyme is involved?

Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
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(b)  Is the ubiquitination relatively stable or highly dynamic?  how does ubiquitination become detached from the protein of interest? what enzyme is involved?

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Step 1

The translation is a process through which ribosomes synthesizes polypeptide chains using mRNA. This polypeptide chain then undergoes post-translational modification to form a mature protein. These modifications are generally covalent and enzymatic. Ubiquitinations is one of the post-translational modification.

Step 2

Ubiquitination is an enzymatic and covalent post-translational change. In this process, the glycine residue of ubiquitin-protein gets attached to the lysine residue of the substrate by forming an isopeptide bond. The process of ubiquitination involves three steps activation, conjugation, and ligation for which ubiquitin-activating enzyme E1s, ubiquitin-conjugating enzyme E2s, and ubiquitin ligase enzyme E3s are required respectively. It regulated degradation of proteins, cellular localization, activation, deactivation, modulation of interactions between proteins. It is a highly dynamic process.

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