Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Bacterial tyrosinases.

Harald Claus1, Heinz Decker

  • 1Institute for Microbiology and Wine Research, University of Mainz, Becherweg 15, D-55099 Mainz, Germany. hclaus@uni-mainz.de

Systematic and Applied Microbiology
|January 21, 2006
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Jumping on the Edge-First Evidence for a 2 × 6-meric Hemocyanin in Springtails.

Biomolecules·2019
Same author

The Recent Crystal Structure of Human Tyrosinase Related Protein 1 (HsTYRP1) Solves an Old Problem and Poses a New One.

Angewandte Chemie (International ed. in English)·2017
Same author

Proteomic profiling of German Dornfelder grape berries using data-independent acquisition.

Plant physiology and biochemistry : PPB·2017
Same author

Antioxidant capacity of phenolic compounds on human cell lines as affected by grape-tyrosinase and Botrytis-laccase oxidation.

Food chemistry·2017
Same author

Past, present and future of immunology in Mainz.

Cellular immunology·2016
Same author

The Potential of the Yeast Debaryomyces hansenii H525 to Degrade Biogenic Amines in Food.

Microorganisms·2016

Bacterial tyrosinases, particularly from Streptomyces, are valuable models for understanding type 3 copper proteins. Their well-characterized structure and function offer insights into enzymatic mechanisms and melanin production.

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Tyrosinases are ubiquitous enzymes crucial for pigmentation, wound healing, and immune response.
  • Their active site features a type 3 copper center (CuA and CuB), common to catecholoxidases and hemocyanins.
  • Tyrosinases catalyze monophenol hydroxylation and o-diphenol oxidation, essential for melanin biosynthesis.

Purpose of the Study:

  • To review current knowledge on bacterial tyrosinases, focusing on Streptomyces species.
  • To highlight bacterial tyrosinases as promising models for understanding type 3 copper proteins.
  • To elucidate the structure, enzymatic reactions, and functions of these enzymes.

Main Methods:

  • Genetic and spectroscopic characterization of prokaryotic tyrosinases from Streptomyces.

Related Experiment Videos

  • Analysis of the melC operon, including the tyrosinase gene (melC2) and regulatory ORF (melC1).
  • Review of existing literature on bacterial tyrosinase properties and functions.

    • Main Results:

    • Streptomyces tyrosinases are small (ca. 30kDa), secreted, monomeric proteins.
    • These enzymes are involved in extracellular melanin production.
    • The melC1 gene is essential for the correct expression of the tyrosinase enzyme.

    Conclusions:

    • Prokaryotic tyrosinases provide accessible models for studying type 3 copper proteins due to ease of isolation and characterization.
    • Further research on bacterial tyrosinases can yield significant insights into the complex mechanisms of copper-containing enzymes.
    • Understanding tyrosinase function is key to advancements in pigmentation research and biotechnological applications.