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Alkyl hydroperoxide reductase from Bacillus aquimaris MKSC 6.2 protects Esherichia coli from oxidative stress
Author(s) -
Natalia Dessy,
Jumadila Ozi,
Anggraini Irika Devi,
Meutia Febrina,
Puspasari Fernita,
Hasan Khomaini
Publication year - 2016
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.201500406
Subject(s) - oxidative stress , chemistry , oxidative phosphorylation , reductase , escherichia coli , biochemistry , microbiology and biotechnology , enzyme , biology , gene
Alkyl hydroperoxide reductase genes ( ahpCF ) from the soft coral associated Bacillus aquimaris MKSC6.2 have been isolated. The cloned 546 bp ahpC gene encodes a 181 amino acid residues polypeptide. The AhpC belongs to typical 2‐Cys peroxiredoxin (Prx) containing conserved peroxidatic cysteine residue (C 46 ) required for hydroperoxide reduction and conserved resolving cysteine (C 166 ). The isolated 1530 bp ahpF gene encodes a polypeptide of 509 amino acid residues with two conserved C 128 HNC 131 and C 337 PHC 340 catalytic residues required for reduction of oxidized‐AhpC during catalytic turnover. A survival study with Escherichia coli showed that overexpression of AhpC and AhpF resulted in a total protection against 0.16 mM t‐butyl hydroperoxide.