Abstract
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 language | English |
|---|---|
| Pages (from-to) | 213-223 |
| Number of pages | 11 |
| Journal | Journal of the Faculty of Agriculture, Kyushu University |
| Volume | 45 |
| Issue number | 1 |
| Publication status | Published - Nov 1 2000 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Agronomy and Crop Science
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Molecular characterization of Staphylococcus warneri catalase. / Fukuda, Daisuke; Mizuno, Kouhei; Kohno, Mamiko; Sonomoto, Kenji; Ishizaki, Ayaaki.
In: Journal of the Faculty of Agriculture, Kyushu University, Vol. 45, No. 1, 01.11.2000, p. 213-223.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Molecular characterization of Staphylococcus warneri catalase
AU - Fukuda, Daisuke
AU - Mizuno, Kouhei
AU - Kohno, Mamiko
AU - Sonomoto, Kenji
AU - Ishizaki, Ayaaki
PY - 2000/11/1
Y1 - 2000/11/1
N2 - 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.
AB - 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.
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M3 - Article
AN - SCOPUS:0034562575
VL - 45
SP - 213
EP - 223
JO - Journal of the Faculty of Agriculture, Kyushu University
JF - Journal of the Faculty of Agriculture, Kyushu University
SN - 0023-6152
IS - 1
ER -