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Protein Digestion01:02

Protein Digestion

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Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
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Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Papain-like peptidases: structure, function, and evolution.

Marko Novinec, Brigita Lenarčič

    Biomolecular Concepts
    |December 2, 2014
    PubMed
    Summary

    Papain-like cysteine peptidases are vital enzymes in all organisms. This review details their structure, function, and roles in human health and disease, as well as in host-pathogen interactions.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Evolutionary Biology

    Background:

    • Papain-like cysteine peptidases are a widespread enzyme family.
    • They exhibit diverse structures and functions, acting as endo- or exopeptidases.
    • In humans, they are known as cysteine cathepsins and are crucial for physiological processes.

    Purpose of the Study:

    • To provide a comprehensive overview of papain-like peptidases.
    • To describe their structure, phylogeny, and evolutionary groups.
    • To elucidate their physiological and pathological roles in humans and other organisms.

    Main Methods:

    • Review of existing literature on papain-like peptidases.
    • Analysis of structural characteristics of proenzymes for classification.

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  • Comparative study of enzyme functions across different species.

    • Main Results:

    • Papain-like peptidases are classified into distinct evolutionary groups based on proenzyme structure.
    • Human cysteine cathepsins are involved in antigen presentation, ECM remodeling, and hormone processing.
    • Dysregulation is linked to diseases like cancer and cardiovascular conditions.
    • These enzymes play roles in host-pathogen interactions, including parasite invasion and plant defense.

    Conclusions:

    • Papain-like peptidases are essential enzymes with diverse roles in biology.
    • Understanding their structure and function is key to comprehending health and disease.
    • Their involvement in host-pathogen interactions highlights their evolutionary significance.