Open AccessDimethoxyphenol oxidase activity of different microbial blue multicopper proteins
Author(s) -
Solano Francisco,
LucasElı́o Patricia,
LópezSerrano Daniel,
Fernández Eva,
SanchezAmat Antonio
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10882.x
Subject(s) - multicopper oxidase , bacillus subtilis , laccase , biochemistry , enzyme , escherichia coli , oxidase test , bacteria , ceruloplasmin , biology , saccharomyces cerevisiae , pseudomonas , chemistry , yeast , gene , genetics
2,6‐Dimethoxyphenol is a versatile substrate for Pyricularia oryzae laccase, PpoA from Marinomonas mediterranea , phenoxazinone synthase from Streptomyces antibioticus and mammalian ceruloplasmin. In addition, in cellular extracts of microorganisms expressing other blue multicopper proteins with no enzymatic activity previously described, such as Escherichia coli (copper resistance CueO), Pseudomonas syringae and Xanthomonas campestris (copper resistance CopA), Bacillus subtilis (sporulation protein CotA) and Saccharomyces cerevisiae (iron transporter Fet3p), laccase activity is detected under appropriate conditions. This oxidase activity can be spectrophotometrically followed by the oxidation of 2,6‐dimethoxyphenol. Specific staining after SDS–PAGE is also possible for some of these proteins. This detection assay can facilitate the study of the multiple functions that such proteins seem to carry out in a variety of microorganisms.