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Enterococcus faecalis heme-dependent catalase.

Lena Frankenberg1, Myriam Brugna, Lars Hederstedt

  • 1Department of Cell and Organism Biology, Lund University, Sweden. lena.frankenberg@mikrbiol.lu.se

Journal of Bacteriology
|October 26, 2002
PubMed
Summary

Enterococcus faecalis acquires heme to produce KatA catalase, an enzyme crucial for its growth. This finding highlights E. faecalis as a model for studying heme uptake and metalloprotein synthesis.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Enzymology

Background:

  • Enterococcus faecalis cannot synthesize porphyrins or rely on heme for growth.
  • E. faecalis can uptake heme and utilize it for heme protein synthesis.
  • A cytochrome bd complex in E. faecalis strain V583 was previously identified.

Purpose of the Study:

  • To identify and characterize a heme-dependent catalase in E. faecalis.
  • To investigate the role of heme in catalase production in E. faecalis.
  • To establish E. faecalis as a model system for heme transport and metalloprotein studies.

Main Methods:

  • Identification of the katA gene encoding a cytoplasmic catalase.
  • Purification and characterization of a hexahistidyl-tagged KatA polypeptide.
  • Determination of heme content and catalase activity in E. faecalis under varying hemin concentrations.

Main Results:

  • The katA gene encodes a 54-kDa polypeptide with sequence similarity to monofunctional catalases.
  • Purified KatA contains one protoheme IX group per polypeptide.
  • Catalase activity was detected only in E. faecalis grown in the presence of hemin, with maximal production at 10 micro M.

Conclusions:

  • Heme acquisition is essential for catalase synthesis in E. faecalis.
  • The heme-dependent catalase (KatA) in E. faecalis may have clinical significance.
  • E. faecalis serves as a potential experimental system for studying cellular heme transport, heme protein assembly, and in vivo metalloprotein analog synthesis.

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