Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor

Abstract. A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated w...
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Autor*in:	Ichinose, H. [verfasserIn] Wariishi, H. Tanaka, H.

Format:	Artikel
Sprache:	Englisch

Erschienen:	2002

Schlagwörter:	Lignin Phanerochaete Chrysosporium Cunninghamella P450 Oxidoreductase Cunninghamella Elegans

Anmerkung:	© Springer-Verlag 2003

Übergeordnetes Werk:	Enthalten in: Applied microbiology and biotechnology - Springer-Verlag, 1984, 59(2002), 6 vom: 30. Juli, Seite 658-664
Übergeordnetes Werk:	volume:59 ; year:2002 ; number:6 ; day:30 ; month:07 ; pages:658-664

Links:	Volltext

DOI / URN:	10.1007/s00253-002-1083-8

Katalog-ID:	OLC205069511X

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520			\|a Abstract. A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated was 60%. A deduced protein contained 730 amino acid residues with a calculated molecular weight of 80.7 kDa. The conserved amino acid residues involved in functional domains such as FAD-, FMN-, and NADPH-binding domains, were all found in the deduced protein. A phylogenetic analysis demonstrated that C. versicolor CPR is significantly similar to CPR of the basidiomycete Phanerochaete chrysosporium and that they share the same major branch in the fungal cluster. A recombinant CPR protein was expressed using a pET/Escherichia coli system. The recombinant CPR protein migrated at 81 kDa on SDS polyacrylamide gel electrophoresis. It exhibited an NADPH-dependent cytochrome c reducing activity.
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allfields	10.1007/s00253-002-1083-8 doi (DE-627)OLC205069511X (DE-He213)s00253-002-1083-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Ichinose, H. verfasserin aut Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor 2002 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2003 Abstract. A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated was 60%. A deduced protein contained 730 amino acid residues with a calculated molecular weight of 80.7 kDa. The conserved amino acid residues involved in functional domains such as FAD-, FMN-, and NADPH-binding domains, were all found in the deduced protein. A phylogenetic analysis demonstrated that C. versicolor CPR is significantly similar to CPR of the basidiomycete Phanerochaete chrysosporium and that they share the same major branch in the fungal cluster. A recombinant CPR protein was expressed using a pET/Escherichia coli system. The recombinant CPR protein migrated at 81 kDa on SDS polyacrylamide gel electrophoresis. It exhibited an NADPH-dependent cytochrome c reducing activity. Lignin Phanerochaete Chrysosporium Cunninghamella P450 Oxidoreductase Cunninghamella Elegans Wariishi, H. aut Tanaka, H. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 59(2002), 6 vom: 30. Juli, Seite 658-664 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:59 year:2002 number:6 day:30 month:07 pages:658-664 https://doi.org/10.1007/s00253-002-1083-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 59 2002 6 30 07 658-664
spelling	10.1007/s00253-002-1083-8 doi (DE-627)OLC205069511X (DE-He213)s00253-002-1083-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Ichinose, H. verfasserin aut Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor 2002 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2003 Abstract. A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated was 60%. A deduced protein contained 730 amino acid residues with a calculated molecular weight of 80.7 kDa. The conserved amino acid residues involved in functional domains such as FAD-, FMN-, and NADPH-binding domains, were all found in the deduced protein. A phylogenetic analysis demonstrated that C. versicolor CPR is significantly similar to CPR of the basidiomycete Phanerochaete chrysosporium and that they share the same major branch in the fungal cluster. A recombinant CPR protein was expressed using a pET/Escherichia coli system. The recombinant CPR protein migrated at 81 kDa on SDS polyacrylamide gel electrophoresis. It exhibited an NADPH-dependent cytochrome c reducing activity. Lignin Phanerochaete Chrysosporium Cunninghamella P450 Oxidoreductase Cunninghamella Elegans Wariishi, H. aut Tanaka, H. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 59(2002), 6 vom: 30. Juli, Seite 658-664 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:59 year:2002 number:6 day:30 month:07 pages:658-664 https://doi.org/10.1007/s00253-002-1083-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 59 2002 6 30 07 658-664
allfields_unstemmed	10.1007/s00253-002-1083-8 doi (DE-627)OLC205069511X (DE-He213)s00253-002-1083-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Ichinose, H. verfasserin aut Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor 2002 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2003 Abstract. A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated was 60%. A deduced protein contained 730 amino acid residues with a calculated molecular weight of 80.7 kDa. The conserved amino acid residues involved in functional domains such as FAD-, FMN-, and NADPH-binding domains, were all found in the deduced protein. A phylogenetic analysis demonstrated that C. versicolor CPR is significantly similar to CPR of the basidiomycete Phanerochaete chrysosporium and that they share the same major branch in the fungal cluster. A recombinant CPR protein was expressed using a pET/Escherichia coli system. The recombinant CPR protein migrated at 81 kDa on SDS polyacrylamide gel electrophoresis. It exhibited an NADPH-dependent cytochrome c reducing activity. Lignin Phanerochaete Chrysosporium Cunninghamella P450 Oxidoreductase Cunninghamella Elegans Wariishi, H. aut Tanaka, H. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 59(2002), 6 vom: 30. Juli, Seite 658-664 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:59 year:2002 number:6 day:30 month:07 pages:658-664 https://doi.org/10.1007/s00253-002-1083-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 59 2002 6 30 07 658-664
allfieldsGer	10.1007/s00253-002-1083-8 doi (DE-627)OLC205069511X (DE-He213)s00253-002-1083-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Ichinose, H. verfasserin aut Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor 2002 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2003 Abstract. A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated was 60%. A deduced protein contained 730 amino acid residues with a calculated molecular weight of 80.7 kDa. The conserved amino acid residues involved in functional domains such as FAD-, FMN-, and NADPH-binding domains, were all found in the deduced protein. A phylogenetic analysis demonstrated that C. versicolor CPR is significantly similar to CPR of the basidiomycete Phanerochaete chrysosporium and that they share the same major branch in the fungal cluster. A recombinant CPR protein was expressed using a pET/Escherichia coli system. The recombinant CPR protein migrated at 81 kDa on SDS polyacrylamide gel electrophoresis. It exhibited an NADPH-dependent cytochrome c reducing activity. Lignin Phanerochaete Chrysosporium Cunninghamella P450 Oxidoreductase Cunninghamella Elegans Wariishi, H. aut Tanaka, H. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 59(2002), 6 vom: 30. Juli, Seite 658-664 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:59 year:2002 number:6 day:30 month:07 pages:658-664 https://doi.org/10.1007/s00253-002-1083-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 59 2002 6 30 07 658-664
allfieldsSound	10.1007/s00253-002-1083-8 doi (DE-627)OLC205069511X (DE-He213)s00253-002-1083-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Ichinose, H. verfasserin aut Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor 2002 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2003 Abstract. A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated was 60%. A deduced protein contained 730 amino acid residues with a calculated molecular weight of 80.7 kDa. The conserved amino acid residues involved in functional domains such as FAD-, FMN-, and NADPH-binding domains, were all found in the deduced protein. A phylogenetic analysis demonstrated that C. versicolor CPR is significantly similar to CPR of the basidiomycete Phanerochaete chrysosporium and that they share the same major branch in the fungal cluster. A recombinant CPR protein was expressed using a pET/Escherichia coli system. The recombinant CPR protein migrated at 81 kDa on SDS polyacrylamide gel electrophoresis. It exhibited an NADPH-dependent cytochrome c reducing activity. Lignin Phanerochaete Chrysosporium Cunninghamella P450 Oxidoreductase Cunninghamella Elegans Wariishi, H. aut Tanaka, H. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 59(2002), 6 vom: 30. Juli, Seite 658-664 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:59 year:2002 number:6 day:30 month:07 pages:658-664 https://doi.org/10.1007/s00253-002-1083-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 59 2002 6 30 07 658-664
language	English
source	Enthalten in Applied microbiology and biotechnology 59(2002), 6 vom: 30. Juli, Seite 658-664 volume:59 year:2002 number:6 day:30 month:07 pages:658-664
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topic_facet	Lignin Phanerochaete Chrysosporium Cunninghamella P450 Oxidoreductase Cunninghamella Elegans
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author	Ichinose, H.
spellingShingle	Ichinose, H. ddc 570 ssgn 12 fid BIODIV misc Lignin misc Phanerochaete Chrysosporium misc Cunninghamella misc P450 Oxidoreductase misc Cunninghamella Elegans Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor
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topic_title	570 VZ 12 ssgn BIODIV DE-30 fid Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor Lignin Phanerochaete Chrysosporium Cunninghamella P450 Oxidoreductase Cunninghamella Elegans
topic	ddc 570 ssgn 12 fid BIODIV misc Lignin misc Phanerochaete Chrysosporium misc Cunninghamella misc P450 Oxidoreductase misc Cunninghamella Elegans
topic_unstemmed	ddc 570 ssgn 12 fid BIODIV misc Lignin misc Phanerochaete Chrysosporium misc Cunninghamella misc P450 Oxidoreductase misc Cunninghamella Elegans
topic_browse	ddc 570 ssgn 12 fid BIODIV misc Lignin misc Phanerochaete Chrysosporium misc Cunninghamella misc P450 Oxidoreductase misc Cunninghamella Elegans
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title	Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor
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title_full	Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor
author_sort	Ichinose, H.
journal	Applied microbiology and biotechnology
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dewey-full	570
title_sort	identification and heterologous expression of the cytochrome p450 oxidoreductase from the white-rot basidiomycete coriolus versicolor
title_auth	Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor
abstract	Abstract. A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated was 60%. A deduced protein contained 730 amino acid residues with a calculated molecular weight of 80.7 kDa. The conserved amino acid residues involved in functional domains such as FAD-, FMN-, and NADPH-binding domains, were all found in the deduced protein. A phylogenetic analysis demonstrated that C. versicolor CPR is significantly similar to CPR of the basidiomycete Phanerochaete chrysosporium and that they share the same major branch in the fungal cluster. A recombinant CPR protein was expressed using a pET/Escherichia coli system. The recombinant CPR protein migrated at 81 kDa on SDS polyacrylamide gel electrophoresis. It exhibited an NADPH-dependent cytochrome c reducing activity. © Springer-Verlag 2003
abstractGer	Abstract. A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated was 60%. A deduced protein contained 730 amino acid residues with a calculated molecular weight of 80.7 kDa. The conserved amino acid residues involved in functional domains such as FAD-, FMN-, and NADPH-binding domains, were all found in the deduced protein. A phylogenetic analysis demonstrated that C. versicolor CPR is significantly similar to CPR of the basidiomycete Phanerochaete chrysosporium and that they share the same major branch in the fungal cluster. A recombinant CPR protein was expressed using a pET/Escherichia coli system. The recombinant CPR protein migrated at 81 kDa on SDS polyacrylamide gel electrophoresis. It exhibited an NADPH-dependent cytochrome c reducing activity. © Springer-Verlag 2003
abstract_unstemmed	Abstract. A cDNA encoding cytochrome P450 oxidoreductase (CPR) from the lignin-degrading basidiomycete Coriolus versicolor was identified using RT-PCR. The full-length cDNA consisted of 2,484 nucleotides with a poly(A) tail, and contained an open reading frame. The G+C content of the cDNA isolated was 60%. A deduced protein contained 730 amino acid residues with a calculated molecular weight of 80.7 kDa. The conserved amino acid residues involved in functional domains such as FAD-, FMN-, and NADPH-binding domains, were all found in the deduced protein. A phylogenetic analysis demonstrated that C. versicolor CPR is significantly similar to CPR of the basidiomycete Phanerochaete chrysosporium and that they share the same major branch in the fungal cluster. A recombinant CPR protein was expressed using a pET/Escherichia coli system. The recombinant CPR protein migrated at 81 kDa on SDS polyacrylamide gel electrophoresis. It exhibited an NADPH-dependent cytochrome c reducing activity. © Springer-Verlag 2003
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container_issue	6
title_short	Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor
url	https://doi.org/10.1007/s00253-002-1083-8
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up_date	2024-07-04T02:36:31.422Z
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Identification and heterologous expression of the cytochrome P450 oxidoreductase from the white-rot basidiomycete Coriolus versicolor

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