Structural and functional characterization of a small chitin‐active lytic polysaccharide monooxygenase domain of a multi‐modular chitinase from Jonesia denitrificans
Lytic polysaccharide monooxygenases ( LPMO s) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin‐active LPMO domain ( Jd LPMO 10A) that is considerably smaller (15.5 kD a) than all structurally characterized LPMO s so far and that...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Vaaje‐Kolstad, Gustav [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016 |
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| Rechteinformationen: |
Nutzungsrecht: © 2015 Federation of European Biochemical Societies |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: FEBS letters - Amsterdam [u.a.] : Elsevier, 1968, 590(2016), 1, Seite 34-42 |
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| Übergeordnetes Werk: |
volume:590 ; year:2016 ; number:1 ; pages:34-42 |
| Links: |
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| DOI / URN: |
10.1002/1873-3468.12025 |
|---|
| Katalog-ID: |
OLC1970666749 |
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| 520 | |a Lytic polysaccharide monooxygenases ( LPMO s) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin‐active LPMO domain ( Jd LPMO 10A) that is considerably smaller (15.5 kD a) than all structurally characterized LPMO s so far and that is part of a modular protein containing a GH 18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β‐sandwich scaffold in larger LPMO 10s. Despite these deletions, the enzyme is active on alpha‐ and beta‐chitin, and the chitin‐binding surface previously described for larger LPMO s is fully conserved. Jd LPMO 10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction. | ||
| 540 | |a Nutzungsrecht: © 2015 Federation of European Biochemical Societies | ||
| 650 | 4 | |a Jonesia denitrificans | |
| 650 | 4 | |a chitin | |
| 650 | 4 | |a chitinase | |
| 650 | 4 | |a lytic polysaccharide monooxygenase | |
| 700 | 1 | |a Choudhary, Swati |4 oth | |
| 700 | 1 | |a Mekasha, Sophanit |4 oth | |
| 700 | 1 | |a Eijsink, Vincent G. H |4 oth | |
| 700 | 1 | |a Bacik, John‐Paul |4 oth | |
| 700 | 1 | |a Dalhus, Bjørn |4 oth | |
| 700 | 1 | |a Schmidt‐Dannert, Claudia |4 oth | |
| 700 | 1 | |a Ferguson, Stuart |4 oth | |
| 700 | 1 | |a Forsberg, Zarah |4 oth | |
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10.1002/1873-3468.12025 doi PQ20160212 (DE-627)OLC1970666749 (DE-599)GBVOLC1970666749 (PRQ)wiley_primary_10_1002_1873_3468_12025_FEB2120250 (KEY)0045922420160000590000100034structuralandfunctionalcharacterizationofasmallchi DE-627 ger DE-627 rakwb eng 570 530 610 DNB Vaaje‐Kolstad, Gustav verfasserin aut Structural and functional characterization of a small chitin‐active lytic polysaccharide monooxygenase domain of a multi‐modular chitinase from Jonesia denitrificans 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lytic polysaccharide monooxygenases ( LPMO s) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin‐active LPMO domain ( Jd LPMO 10A) that is considerably smaller (15.5 kD a) than all structurally characterized LPMO s so far and that is part of a modular protein containing a GH 18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β‐sandwich scaffold in larger LPMO 10s. Despite these deletions, the enzyme is active on alpha‐ and beta‐chitin, and the chitin‐binding surface previously described for larger LPMO s is fully conserved. Jd LPMO 10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction. Nutzungsrecht: © 2015 Federation of European Biochemical Societies Jonesia denitrificans chitin chitinase lytic polysaccharide monooxygenase Choudhary, Swati oth Mekasha, Sophanit oth Eijsink, Vincent G. H oth Bacik, John‐Paul oth Dalhus, Bjørn oth Schmidt‐Dannert, Claudia oth Ferguson, Stuart oth Forsberg, Zarah oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 590(2016), 1, Seite 34-42 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:590 year:2016 number:1 pages:34-42 http://dx.doi.org/10.1002/1873-3468.12025 Volltext http://onlinelibrary.wiley.com/doi/10.1002/1873-3468.12025/abstract GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 AR 590 2016 1 34-42 |
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10.1002/1873-3468.12025 doi PQ20160212 (DE-627)OLC1970666749 (DE-599)GBVOLC1970666749 (PRQ)wiley_primary_10_1002_1873_3468_12025_FEB2120250 (KEY)0045922420160000590000100034structuralandfunctionalcharacterizationofasmallchi DE-627 ger DE-627 rakwb eng 570 530 610 DNB Vaaje‐Kolstad, Gustav verfasserin aut Structural and functional characterization of a small chitin‐active lytic polysaccharide monooxygenase domain of a multi‐modular chitinase from Jonesia denitrificans 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lytic polysaccharide monooxygenases ( LPMO s) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin‐active LPMO domain ( Jd LPMO 10A) that is considerably smaller (15.5 kD a) than all structurally characterized LPMO s so far and that is part of a modular protein containing a GH 18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β‐sandwich scaffold in larger LPMO 10s. Despite these deletions, the enzyme is active on alpha‐ and beta‐chitin, and the chitin‐binding surface previously described for larger LPMO s is fully conserved. Jd LPMO 10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction. Nutzungsrecht: © 2015 Federation of European Biochemical Societies Jonesia denitrificans chitin chitinase lytic polysaccharide monooxygenase Choudhary, Swati oth Mekasha, Sophanit oth Eijsink, Vincent G. H oth Bacik, John‐Paul oth Dalhus, Bjørn oth Schmidt‐Dannert, Claudia oth Ferguson, Stuart oth Forsberg, Zarah oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 590(2016), 1, Seite 34-42 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:590 year:2016 number:1 pages:34-42 http://dx.doi.org/10.1002/1873-3468.12025 Volltext http://onlinelibrary.wiley.com/doi/10.1002/1873-3468.12025/abstract GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 AR 590 2016 1 34-42 |
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10.1002/1873-3468.12025 doi PQ20160212 (DE-627)OLC1970666749 (DE-599)GBVOLC1970666749 (PRQ)wiley_primary_10_1002_1873_3468_12025_FEB2120250 (KEY)0045922420160000590000100034structuralandfunctionalcharacterizationofasmallchi DE-627 ger DE-627 rakwb eng 570 530 610 DNB Vaaje‐Kolstad, Gustav verfasserin aut Structural and functional characterization of a small chitin‐active lytic polysaccharide monooxygenase domain of a multi‐modular chitinase from Jonesia denitrificans 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lytic polysaccharide monooxygenases ( LPMO s) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin‐active LPMO domain ( Jd LPMO 10A) that is considerably smaller (15.5 kD a) than all structurally characterized LPMO s so far and that is part of a modular protein containing a GH 18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β‐sandwich scaffold in larger LPMO 10s. Despite these deletions, the enzyme is active on alpha‐ and beta‐chitin, and the chitin‐binding surface previously described for larger LPMO s is fully conserved. Jd LPMO 10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction. Nutzungsrecht: © 2015 Federation of European Biochemical Societies Jonesia denitrificans chitin chitinase lytic polysaccharide monooxygenase Choudhary, Swati oth Mekasha, Sophanit oth Eijsink, Vincent G. H oth Bacik, John‐Paul oth Dalhus, Bjørn oth Schmidt‐Dannert, Claudia oth Ferguson, Stuart oth Forsberg, Zarah oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 590(2016), 1, Seite 34-42 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:590 year:2016 number:1 pages:34-42 http://dx.doi.org/10.1002/1873-3468.12025 Volltext http://onlinelibrary.wiley.com/doi/10.1002/1873-3468.12025/abstract GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 AR 590 2016 1 34-42 |
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10.1002/1873-3468.12025 doi PQ20160212 (DE-627)OLC1970666749 (DE-599)GBVOLC1970666749 (PRQ)wiley_primary_10_1002_1873_3468_12025_FEB2120250 (KEY)0045922420160000590000100034structuralandfunctionalcharacterizationofasmallchi DE-627 ger DE-627 rakwb eng 570 530 610 DNB Vaaje‐Kolstad, Gustav verfasserin aut Structural and functional characterization of a small chitin‐active lytic polysaccharide monooxygenase domain of a multi‐modular chitinase from Jonesia denitrificans 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lytic polysaccharide monooxygenases ( LPMO s) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin‐active LPMO domain ( Jd LPMO 10A) that is considerably smaller (15.5 kD a) than all structurally characterized LPMO s so far and that is part of a modular protein containing a GH 18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β‐sandwich scaffold in larger LPMO 10s. Despite these deletions, the enzyme is active on alpha‐ and beta‐chitin, and the chitin‐binding surface previously described for larger LPMO s is fully conserved. Jd LPMO 10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction. Nutzungsrecht: © 2015 Federation of European Biochemical Societies Jonesia denitrificans chitin chitinase lytic polysaccharide monooxygenase Choudhary, Swati oth Mekasha, Sophanit oth Eijsink, Vincent G. H oth Bacik, John‐Paul oth Dalhus, Bjørn oth Schmidt‐Dannert, Claudia oth Ferguson, Stuart oth Forsberg, Zarah oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 590(2016), 1, Seite 34-42 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:590 year:2016 number:1 pages:34-42 http://dx.doi.org/10.1002/1873-3468.12025 Volltext http://onlinelibrary.wiley.com/doi/10.1002/1873-3468.12025/abstract GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 AR 590 2016 1 34-42 |
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10.1002/1873-3468.12025 doi PQ20160212 (DE-627)OLC1970666749 (DE-599)GBVOLC1970666749 (PRQ)wiley_primary_10_1002_1873_3468_12025_FEB2120250 (KEY)0045922420160000590000100034structuralandfunctionalcharacterizationofasmallchi DE-627 ger DE-627 rakwb eng 570 530 610 DNB Vaaje‐Kolstad, Gustav verfasserin aut Structural and functional characterization of a small chitin‐active lytic polysaccharide monooxygenase domain of a multi‐modular chitinase from Jonesia denitrificans 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lytic polysaccharide monooxygenases ( LPMO s) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin‐active LPMO domain ( Jd LPMO 10A) that is considerably smaller (15.5 kD a) than all structurally characterized LPMO s so far and that is part of a modular protein containing a GH 18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β‐sandwich scaffold in larger LPMO 10s. Despite these deletions, the enzyme is active on alpha‐ and beta‐chitin, and the chitin‐binding surface previously described for larger LPMO s is fully conserved. Jd LPMO 10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction. Nutzungsrecht: © 2015 Federation of European Biochemical Societies Jonesia denitrificans chitin chitinase lytic polysaccharide monooxygenase Choudhary, Swati oth Mekasha, Sophanit oth Eijsink, Vincent G. H oth Bacik, John‐Paul oth Dalhus, Bjørn oth Schmidt‐Dannert, Claudia oth Ferguson, Stuart oth Forsberg, Zarah oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 590(2016), 1, Seite 34-42 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:590 year:2016 number:1 pages:34-42 http://dx.doi.org/10.1002/1873-3468.12025 Volltext http://onlinelibrary.wiley.com/doi/10.1002/1873-3468.12025/abstract GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 AR 590 2016 1 34-42 |
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Vaaje‐Kolstad, Gustav @@aut@@ Choudhary, Swati @@oth@@ Mekasha, Sophanit @@oth@@ Eijsink, Vincent G. H @@oth@@ Bacik, John‐Paul @@oth@@ Dalhus, Bjørn @@oth@@ Schmidt‐Dannert, Claudia @@oth@@ Ferguson, Stuart @@oth@@ Forsberg, Zarah @@oth@@ |
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570 530 610 DNB Structural and functional characterization of a small chitin‐active lytic polysaccharide monooxygenase domain of a multi‐modular chitinase from Jonesia denitrificans Jonesia denitrificans chitin chitinase lytic polysaccharide monooxygenase |
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Structural and functional characterization of a small chitin‐active lytic polysaccharide monooxygenase domain of a multi‐modular chitinase from Jonesia denitrificans |
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(DE-627)OLC1970666749 (DE-599)GBVOLC1970666749 (PRQ)wiley_primary_10_1002_1873_3468_12025_FEB2120250 (KEY)0045922420160000590000100034structuralandfunctionalcharacterizationofasmallchi |
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Structural and functional characterization of a small chitin‐active lytic polysaccharide monooxygenase domain of a multi‐modular chitinase from Jonesia denitrificans |
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Vaaje‐Kolstad, Gustav |
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Vaaje‐Kolstad, Gustav |
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structural and functional characterization of a small chitin‐active lytic polysaccharide monooxygenase domain of a multi‐modular chitinase from jonesia denitrificans |
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Structural and functional characterization of a small chitin‐active lytic polysaccharide monooxygenase domain of a multi‐modular chitinase from Jonesia denitrificans |
| abstract |
Lytic polysaccharide monooxygenases ( LPMO s) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin‐active LPMO domain ( Jd LPMO 10A) that is considerably smaller (15.5 kD a) than all structurally characterized LPMO s so far and that is part of a modular protein containing a GH 18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β‐sandwich scaffold in larger LPMO 10s. Despite these deletions, the enzyme is active on alpha‐ and beta‐chitin, and the chitin‐binding surface previously described for larger LPMO s is fully conserved. Jd LPMO 10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction. |
| abstractGer |
Lytic polysaccharide monooxygenases ( LPMO s) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin‐active LPMO domain ( Jd LPMO 10A) that is considerably smaller (15.5 kD a) than all structurally characterized LPMO s so far and that is part of a modular protein containing a GH 18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β‐sandwich scaffold in larger LPMO 10s. Despite these deletions, the enzyme is active on alpha‐ and beta‐chitin, and the chitin‐binding surface previously described for larger LPMO s is fully conserved. Jd LPMO 10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction. |
| abstract_unstemmed |
Lytic polysaccharide monooxygenases ( LPMO s) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin‐active LPMO domain ( Jd LPMO 10A) that is considerably smaller (15.5 kD a) than all structurally characterized LPMO s so far and that is part of a modular protein containing a GH 18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β‐sandwich scaffold in larger LPMO 10s. Despite these deletions, the enzyme is active on alpha‐ and beta‐chitin, and the chitin‐binding surface previously described for larger LPMO s is fully conserved. Jd LPMO 10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction. |
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| title_short |
Structural and functional characterization of a small chitin‐active lytic polysaccharide monooxygenase domain of a multi‐modular chitinase from Jonesia denitrificans |
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http://dx.doi.org/10.1002/1873-3468.12025 http://onlinelibrary.wiley.com/doi/10.1002/1873-3468.12025/abstract |
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Choudhary, Swati Mekasha, Sophanit Eijsink, Vincent G. H Bacik, John‐Paul Dalhus, Bjørn Schmidt‐Dannert, Claudia Ferguson, Stuart Forsberg, Zarah |
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Choudhary, Swati Mekasha, Sophanit Eijsink, Vincent G. H Bacik, John‐Paul Dalhus, Bjørn Schmidt‐Dannert, Claudia Ferguson, Stuart Forsberg, Zarah |
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