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Phylogenetics and enzymology of plant quiescin sulfhydryl oxidase
Author(s) -
Limor-Waisberg Keren,
Alon Assaf,
Mehlman Tevie,
Fass Deborah
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.10.003
Subject(s) - arabidopsis thaliana , biochemistry , enzyme , arabidopsis , concatenation (mathematics) , function (biology) , chemistry , oxidase test , phylogenetics , biology , alternative oxidase , genetics , gene , mutant , mathematics , combinatorics
Quiescin Sulfhydryl Oxidase (QSOX), a catalyst of disulfide bond formation, is found in both plants and animals. Mammalian, avian, and trypanosomal QSOX enzymes have been studied in detail, but plant QSOX has yet to be characterized. Differences between plant and animal QSOXs in domain composition and active‐site sequences raise the question of whether these QSOXs function by the same mechanism. We demonstrate that Arabidopsis thaliana QSOX produced in bacteria is folded and functional as a sulfhydryl oxidase but does not exhibit the interdomain electron transfer observed for its animal counterpart. Based on this finding, further exploration into the respective roles of the redox‐active sites in plant QSOX and the reason for their concatenation is warranted.