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Relationship Between Main Channel Structure of Catalases and the Evolutionary Direction in Cold-Adapted Hydrogen Peroxide-Tolerant Exiguobacteium and Psychrobacter
Author(s) -
Yoshiko Hanaoka,
Hideyuki Kimoto,
Kazuaki Yoshimume,
Isao Hara,
Hidetoshi Matsuyama,
Isao Yumoto
Publication year - 2020
Publication title -
indian journal of microbiology/indian journal of microbiology (print)
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.523
H-Index - 46
eISSN - 0973-7715
pISSN - 0046-8991
DOI - 10.1007/s12088-020-00878-3
Subject(s) - catalase , hydrogen peroxide , peracetic acid , substrate (aquarium) , chemistry , bacteria , stereochemistry , biochemistry , biology , enzyme , genetics , ecology
Catalase has crucial role in adaptive response to H 2 O 2 . Main channel structure responsible for substrate selectivity was estimated to understand the relationship between the evolutionary direction of catalases from Exiguobacterium oxidotolerans and Psychrobacter piscatorii which survive in cold and high concentration of hydrogen peroxide, and their catalytic property. E . oxidotolerans catalase (EKTA) exhibited a higher ratio of compound I formation rate using peracetic acid (a substrate lager than H 2 O 2 )/catalase activity using H 2 O 2 as the substrate than P . piscatori catalase (PKTA). It was considered that the ratio was attributed to the size of the amino acid residues locating at the bottle neck structure in the main channel. The differences in the ratio of the compound I formation rate with peracetic acid to catalase activity with H 2 O 2 between the deeper branches in the phylogenetic tree in both EKTA and PKTA were large. This indicates that catalases from the hydrogen peroxide-tolerant bacteria have evolved in different directions, exhibiting effective catalytic activity and allowing broader substrates size or H 2 O 2 -specific substrate acceptability in EKTA and PKTA, respectively. It is considered that the main channel structure reflected the difference in the evolutionary direction of clade 1 and clade 3 catalases.

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