A variety of catalases and bromoperoxidases in genus Pseudomonas and their characterization.
A survey of bromoperoxidase in some Pseudomonas strains revealed that they contain different types of bromoperoxidase, catalase-bromoperoxidase and catalase. Although all Pseudomonas strains exhibited catalase activity, the enzyme isolated from P. pyrrolnitrica was named catalase-bromoperoxidase, because it catalyzed not only a catalase reaction, but also the bromination of monochlorodimedone. Except heme-type catalase-bromoperoxidase, this strain contained four isoenzymes of general nonheme bromoperoxidase, and their molecular weights were about 73,000. On the other hand, P. putida and P. aeruginosa had the usual heme-type catalase, but they differed in molecular weight and pI value. Both strains also had a nonheme bromoperoxidase which catalyzed the bromination of monochlorodimedone and aniline, and the molecular weight of each enzyme was 68,000 for P. putida and 86,000 for P. aeruginosa. Considering the results reported by Van Pée et al. [1] and Weisner et al. [2], regarding the haloperoxidases of Pseudomonas, the genus was revealed to contain a wide variety of bromoperoxidase and catalase.
Itoh
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Department of Applied Chemistry and Biotechnology, Faculty of Engineering, Fukui University, Japan.
Morinaga
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N
Nomura
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A
D002374:Catalase / Q000737:chemistry* / Q000302:isolation & purification; D007526:Isoelectric Point; D008970:Molecular Weight; D010544:Peroxidases / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification; D011549:Pseudomonas / Q000201:enzymology* / Q000235:genetics; D011764:Pyrrolnitrin / Q000096:biosynthesis
D010544:Peroxidases; C026195:bromide peroxidase; D002374:Catalase; D011764:Pyrrolnitrin