@ARTICLE{TreeBASE2Ref15222,
author = {Theodorus H. de Koker and M. D. Muzuch and Daniel Cullen and Jill Gaskell and Philip J. Kersten},
title = {Pyranose 2-oxidase from Phanerochaete chrysosporium: Isolation from solid substrate, protein purification, and characterization of gene structure and regulation.},
year = {2004},
keywords = {},
doi = {},
url = {},
pmid = {},
journal = {Applied and Environmental Microbiology},
volume = {},
number = {},
pages = {},
abstract = {Pyranose 2-oxidase (POX) was recovered from Phanerochaete chrysosporium BKM-F-1767 solid substrate culture using mild extraction conditions and purified. 13CNMR confirmed production of Darabino-hexos-2-ulose (glucosone) from Dglucose with the oxidase. Peptide fingerprints generated by LCMS/MS of tryptic digests and analysis of the corresponding cDNA revealed a structurally unusual sequence for the P. chrysosporium POX. Relatively high levels of pox transcript were detected under carbon-starved culture conditions but not under nutrient-sufficiency. This regulation pattern is similar to that observed for lignin peroxidases, manganese peroxidases and glyoxal oxidase of P. chrysosporium, supporting evidence that POX has a role in lignocellulose degradation.}
}
Trees for Study 1192
Citation title:
"Pyranose 2-oxidase from Phanerochaete chrysosporium: Isolation from solid substrate, protein purification, and characterization of gene structure and regulation.".
This study was previously identified under the legacy study ID S1100
(Status: Published).
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