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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...
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...
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can exist in...
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 11, 2026

A Semi-quantitative Approach to Assess Biofilm Formation Using Wrinkled Colony Development
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A Semi-quantitative Approach to Assess Biofilm Formation Using Wrinkled Colony Development

Published on: June 7, 2012

Vibrio alginolyticus ("Achromobacter") collagenase: biosynthesis, function and application.

B Keil1

  • 1Institut Pasteur, Paris, France.

Matrix (Stuttgart, Germany). Supplement
|January 1, 1992
PubMed
Summary

Bacterial collagenase from Vibrio alginolyticus is a potent metallo-proteinase. It exhibits high specific activity and shows promise for wound debridement applications.

Area of Science:

  • Biochemistry
  • Enzymology
  • Microbiology

Background:

  • Vibrio alginolyticus produces an inducible extracellular metallo-proteinase known as bacterial collagenase.
  • This enzyme possesses a specific cell-surface receptor for collagen and its fragments.
  • Production can be induced by natural collagen or synthetic peptides.

Purpose of the Study:

  • To characterize the enzymatic properties and specificity of bacterial collagenase from Vibrio alginolyticus.
  • To explore its potential applications, particularly in wound healing.

Main Methods:

  • Investigated enzyme induction by collagen and synthetic peptides.
  • Assessed collagenase activity on native collagen and various protein substrates.
  • Determined substrate specificity and compared it to other collagenases.

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  • Evaluated its efficacy in debriding necrotic tissue.

    • Main Results:

    • Vibrio collagenase exhibits the highest specific activity (180,000 ukat/mg) among known collagenases.
    • It preferentially cleaves collagen at the 3/4 position from the N-terminus.
    • Specificity differs from Clostridium collagenase, targeting sequences with Gly/Ala at P'1 and Pro at P2 or P'2.
    • Demonstrated high efficiency in debriding necrotic burns, ulcers, and decubitus wounds.

    Conclusions:

    • Bacterial collagenase from Vibrio alginolyticus is a highly active and specific metallo-proteinase.
    • Its unique properties and cost-effective production make it suitable for therapeutic applications like wound debridement.