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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
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Putative kallikrein substrates and their (patho)biological functions.

Yijing Yu, Ioannis Prassas, Eleftherios P Diamandis

    Biological Chemistry
    |May 24, 2014
    PubMed
    Summary

    Human tissue kallikreins (KLKs) are a large gene group involved in many processes. This review details methods to identify their substrates and understand their in vivo roles.

    Area of Science:

    • Biochemistry
    • Genetics
    • Proteomics

    Background:

    • Human tissue kallikreins (KLKs) comprise the largest contiguous protease gene group in the human genome, located on chromosome 19q13.3-13.4.
    • These enzymes are widely expressed and play crucial roles in various physiological and pathological functions.
    • Identifying the specific substrates of KLKs is essential for understanding their biological roles but remains challenging.

    Purpose of the Study:

    • To review techniques used to determine KLK substrate specificities.
    • To discuss emerging in vivo substrates of KLKs.
    • To provide a deeper appreciation of the in vivo functional roles of KLKs.

    Main Methods:

    • Phage display, positional scanning, and combinatorial peptide library screens for initial specificity insights.

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  • Proteomic technologies for systemic identification of KLK substrates in physiological settings.
  • Degradomic technologies to uncover putative physiological substrates and in vivo functions.

    • Main Results:

    • Various methods have been employed to investigate KLK substrate preferences.
    • Proteomic and degradomic approaches have identified several putative KLK substrates.
    • These studies enhance the understanding of KLK enzymes' in vivo functions.

    Conclusions:

    • Elucidating KLK substrate repertoires is crucial for understanding their physiological and pathological roles.
    • Advancements in proteomic and degradomic technologies are key to identifying in vivo substrates.
    • This review synthesizes current knowledge on KLK substrate identification and function.