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Related Concept Videos

Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult body.
A...
Determinants of Bacterial Pathogenicity and Virulence01:20

Determinants of Bacterial Pathogenicity and Virulence

Pathogenic bacteria employ a variety of strategies to establish infections, including the secretion of extracellular enzymes that act as potent virulence factors. These enzymes facilitate bacterial colonization of host tissues and help evade immune surveillance. By targeting structural components of host tissues and interfering with immune mechanisms, these enzymes play a pivotal role in disease progression.Extracellular Enzymes Facilitating Tissue Invasion: Several bacterial pathogens secrete...

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Related Experiment Video

Updated: Jul 12, 2026

Manual Isolation of Adipose-derived Stem Cells from Human Lipoaspirates
07:23

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Published on: September 27, 2013

[Collagenolytic enzymes synthesized by microorganisms]

N S Demina, S V Lysenko

    Mikrobiologiia
    |May 1, 1996
    PubMed
    Summary

    Microbial collagenolytic enzymes, including metalloenzymes and serine proteases, are vital in research, biotech, and medicine. Their biosynthesis is induced by collagen-containing substrates, highlighting their versatile applications.

    Area of Science:

    • Microbiology
    • Biochemistry
    • Enzymology

    Context:

    • Microbial collagenolytic enzymes are crucial tools in scientific research, biotechnology, and medicine.
    • These enzymes exhibit diverse structures and specificities in their action on collagen fibrils.
    • Sources include bacteria, actinomycetes, and fungi, with notable examples from Clostridium histolyticum and Achromobacter iophagus.

    Purpose:

    • To review microbial collagenolytic enzymes, their characteristics, and applications.
    • To discuss the structural and functional diversity of microbial collagenases.
    • To explore the biosynthesis and induction of these enzymes.

    Summary:

    • Collagenases from microorganisms are classified as metalloenzymes (e.g., Zn2+-containing) or serine proteases, differing in active site structure.

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    Published on: September 27, 2013

    Isolation of Lamina Propria Mononuclear Cells from Murine Colon Using Collagenase E
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    Isolation of Lamina Propria Mononuclear Cells from Murine Colon Using Collagenase E

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  • Metalloenzymes from C. histolyticum and A. iophagus are well-studied, requiring Zn2+ and tolerating Ca2+.
  • Streptomyces and Actinomyces strains produce potent serine proteases and metalloproteases, with biosynthesis induced by collagen substrates.

    • Impact:

    • Understanding microbial collagenases enhances their application in scientific research.
    • Exploiting these enzymes in biotechnology and medicine offers new therapeutic and diagnostic possibilities.
    • Characterizing diverse collagenolytic enzymes expands knowledge of microbial enzymatic capabilities.