TreeBASE Search-Citation for study 1192

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Citation 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).

Citation

De koker T., Muzuch M., Cullen D., Gaskell J., & Kersten P. 2004. Pyranose 2-oxidase from Phanerochaete chrysosporium: Isolation from solid substrate, protein purification, and characterization of gene structure and regulation. Applied and Environmental Microbiology, null.

Authors

De koker T.
Muzuch M.
Cullen D.
Gaskell J.
Kersten P.

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.

About this resource

Canonical resource URI: http://purl.org/phylo/treebase/phylows/study/TB2:S1192
Other versions: Nexus NeXML

Show BibTeX reference

		@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.}
}

Show RIS reference

		TY  - JOUR
ID  - 15222
AU  - de Koker,Theodorus H. 
AU  - Muzuch,M. D. 
AU  - Cullen,Daniel 
AU  - Gaskell,Jill 
AU  - Kersten,Philip J. 
T1  - Pyranose 2-oxidase from Phanerochaete chrysosporium: Isolation from solid substrate, protein purification, and characterization of gene structure and regulation.
PY  - 2004
KW  - 
UR  - 
N2  - 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.
L3  - 
JF  - Applied and Environmental Microbiology
VL  - 
IS  - 
ER  -