Laboratory of Microbial Technology, Division of Microbial Science and Technology, Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
九州大学大学院生物資源環境科学府応用微生物学
Laboratory of Microbial Technology, Division of Microbial Science and Technology, Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
九州大学大学院生物資源環境科学府応用微生物学
Laboratory of Microbial Technology, Division of Microbial Science and Technology, Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
Laboratery of Microbial Technology, Division of Microbial Science and Technology, Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University
九州大学大学院農学研究院応用微生物学
Laboratery of Microbial Technology, Division of Microbial Science and Technology, Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University
九州大学大学院農学研究院応用微生物学
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 previously purified ISK-1 catalase. Catalase activity was lost when the 135 amino acids were deleted from the C-termial region.