Molecular characterization of Staphylococcus warneri catalase

Daisuke Fukuda, Kouhei Mizuno, Mamiko Kohno, Kenji Sonomoto, Ayaaki Ishizaki

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1 Citation (Scopus)


The catalase gene was cloned by screening a genomic DNA library of S. warneri ISK-1 strain with a strong catalase activity for complementation of the activity in catalase-deficient E. coli strain. Nucleotide sequence analysis of a 2.2-kb DNA fragment revealed an open reading frame, called katA, encoding a peptide of 504 amino acids with a calculated molecular mass of 58kDa. The predicted amino acid sequence showed high similarities with the monofunctional catalases. No similarities were found between katA product and catalase-peroxidase type enzymes. Electrophoretic mobility of katA product was close to that of the previously purified ISK-1 catalase. Catalase activity was lost when the 135 amino acids were deleted from the C-terminal region.

Original languageEnglish
Pages (from-to)213-223
Number of pages11
JournalJournal of the Faculty of Agriculture, Kyushu University
Issue number1
Publication statusPublished - Nov 2000

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Agronomy and Crop Science


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