Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02
Abstract By sequence comparison, the majority of 1,4-α-glucan-branching enzymes (GBEs) consist of an N-terminal carbohydrate-binding domain, a TIM-barrel catalytic domain, and a C-terminal all-beta domain. Among these structures, the GBE from Geobacillus thermoglucosidans STB02 uniquely has a highly...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Ban, Xiaofeng [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2019 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer Science+Business Media, LLC, part of Springer Nature 2019 |
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| Übergeordnetes Werk: |
Enthalten in: Applied biochemistry and biotechnology / A - Springer US, 1994, 190(2019), 3 vom: 25. Okt., Seite 1010-1022 |
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| Übergeordnetes Werk: |
volume:190 ; year:2019 ; number:3 ; day:25 ; month:10 ; pages:1010-1022 |
| Links: |
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| DOI / URN: |
10.1007/s12010-019-03150-7 |
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OLC2116868289 |
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| 520 | |a Abstract By sequence comparison, the majority of 1,4-α-glucan-branching enzymes (GBEs) consist of an N-terminal carbohydrate-binding domain, a TIM-barrel catalytic domain, and a C-terminal all-beta domain. Among these structures, the GBE from Geobacillus thermoglucosidans STB02 uniquely has a highly charged 26-amino-acid C-terminal extension, whose functional roles are the least understood. In this research, the functional significance of the C-terminal domain in GBE from G. thermoglucosidans STB02 and its extension were assessed using a C-terminal deletion analysis. Mutants lacking of more than 7 residues of the C-terminal all-beta domain could not be detected in lysates of their Escherichia coli expression strains, suggesting that an intact all-beta domain is required for structural stability. In contrast, truncation of the C-terminal extension resulted in greater stability and solubility than the wild type, as well as a lower sensitivity to the presence of added metal ions. Comparison of this mutant with the wild type suggests that the interaction of metal ions with the C-terminal extension influences performance of this enzyme. | ||
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10.1007/s12010-019-03150-7 doi (DE-627)OLC2116868289 (DE-He213)s12010-019-03150-7-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Ban, Xiaofeng verfasserin aut Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02 2019 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC, part of Springer Nature 2019 Abstract By sequence comparison, the majority of 1,4-α-glucan-branching enzymes (GBEs) consist of an N-terminal carbohydrate-binding domain, a TIM-barrel catalytic domain, and a C-terminal all-beta domain. Among these structures, the GBE from Geobacillus thermoglucosidans STB02 uniquely has a highly charged 26-amino-acid C-terminal extension, whose functional roles are the least understood. In this research, the functional significance of the C-terminal domain in GBE from G. thermoglucosidans STB02 and its extension were assessed using a C-terminal deletion analysis. Mutants lacking of more than 7 residues of the C-terminal all-beta domain could not be detected in lysates of their Escherichia coli expression strains, suggesting that an intact all-beta domain is required for structural stability. In contrast, truncation of the C-terminal extension resulted in greater stability and solubility than the wild type, as well as a lower sensitivity to the presence of added metal ions. Comparison of this mutant with the wild type suggests that the interaction of metal ions with the C-terminal extension influences performance of this enzyme. 1,4-α-Glucan-branching enzyme C-terminal Metal ion dependency Solubility Thermostability Li, Caiming aut Zhang, Yuzhu aut Gu, Zhengbiao aut Cheng, Li aut Hong, Yan aut Li, Zhaofeng (orcid)0000-0001-7571-1083 aut Enthalten in Applied biochemistry and biotechnology / A Springer US, 1994 190(2019), 3 vom: 25. Okt., Seite 1010-1022 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:190 year:2019 number:3 day:25 month:10 pages:1010-1022 https://doi.org/10.1007/s12010-019-03150-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 42.00 VZ AR 190 2019 3 25 10 1010-1022 |
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10.1007/s12010-019-03150-7 doi (DE-627)OLC2116868289 (DE-He213)s12010-019-03150-7-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Ban, Xiaofeng verfasserin aut Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02 2019 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC, part of Springer Nature 2019 Abstract By sequence comparison, the majority of 1,4-α-glucan-branching enzymes (GBEs) consist of an N-terminal carbohydrate-binding domain, a TIM-barrel catalytic domain, and a C-terminal all-beta domain. Among these structures, the GBE from Geobacillus thermoglucosidans STB02 uniquely has a highly charged 26-amino-acid C-terminal extension, whose functional roles are the least understood. In this research, the functional significance of the C-terminal domain in GBE from G. thermoglucosidans STB02 and its extension were assessed using a C-terminal deletion analysis. Mutants lacking of more than 7 residues of the C-terminal all-beta domain could not be detected in lysates of their Escherichia coli expression strains, suggesting that an intact all-beta domain is required for structural stability. In contrast, truncation of the C-terminal extension resulted in greater stability and solubility than the wild type, as well as a lower sensitivity to the presence of added metal ions. Comparison of this mutant with the wild type suggests that the interaction of metal ions with the C-terminal extension influences performance of this enzyme. 1,4-α-Glucan-branching enzyme C-terminal Metal ion dependency Solubility Thermostability Li, Caiming aut Zhang, Yuzhu aut Gu, Zhengbiao aut Cheng, Li aut Hong, Yan aut Li, Zhaofeng (orcid)0000-0001-7571-1083 aut Enthalten in Applied biochemistry and biotechnology / A Springer US, 1994 190(2019), 3 vom: 25. Okt., Seite 1010-1022 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:190 year:2019 number:3 day:25 month:10 pages:1010-1022 https://doi.org/10.1007/s12010-019-03150-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 42.00 VZ AR 190 2019 3 25 10 1010-1022 |
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10.1007/s12010-019-03150-7 doi (DE-627)OLC2116868289 (DE-He213)s12010-019-03150-7-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Ban, Xiaofeng verfasserin aut Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02 2019 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC, part of Springer Nature 2019 Abstract By sequence comparison, the majority of 1,4-α-glucan-branching enzymes (GBEs) consist of an N-terminal carbohydrate-binding domain, a TIM-barrel catalytic domain, and a C-terminal all-beta domain. Among these structures, the GBE from Geobacillus thermoglucosidans STB02 uniquely has a highly charged 26-amino-acid C-terminal extension, whose functional roles are the least understood. In this research, the functional significance of the C-terminal domain in GBE from G. thermoglucosidans STB02 and its extension were assessed using a C-terminal deletion analysis. Mutants lacking of more than 7 residues of the C-terminal all-beta domain could not be detected in lysates of their Escherichia coli expression strains, suggesting that an intact all-beta domain is required for structural stability. In contrast, truncation of the C-terminal extension resulted in greater stability and solubility than the wild type, as well as a lower sensitivity to the presence of added metal ions. Comparison of this mutant with the wild type suggests that the interaction of metal ions with the C-terminal extension influences performance of this enzyme. 1,4-α-Glucan-branching enzyme C-terminal Metal ion dependency Solubility Thermostability Li, Caiming aut Zhang, Yuzhu aut Gu, Zhengbiao aut Cheng, Li aut Hong, Yan aut Li, Zhaofeng (orcid)0000-0001-7571-1083 aut Enthalten in Applied biochemistry and biotechnology / A Springer US, 1994 190(2019), 3 vom: 25. Okt., Seite 1010-1022 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:190 year:2019 number:3 day:25 month:10 pages:1010-1022 https://doi.org/10.1007/s12010-019-03150-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 42.00 VZ AR 190 2019 3 25 10 1010-1022 |
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10.1007/s12010-019-03150-7 doi (DE-627)OLC2116868289 (DE-He213)s12010-019-03150-7-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Ban, Xiaofeng verfasserin aut Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02 2019 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC, part of Springer Nature 2019 Abstract By sequence comparison, the majority of 1,4-α-glucan-branching enzymes (GBEs) consist of an N-terminal carbohydrate-binding domain, a TIM-barrel catalytic domain, and a C-terminal all-beta domain. Among these structures, the GBE from Geobacillus thermoglucosidans STB02 uniquely has a highly charged 26-amino-acid C-terminal extension, whose functional roles are the least understood. In this research, the functional significance of the C-terminal domain in GBE from G. thermoglucosidans STB02 and its extension were assessed using a C-terminal deletion analysis. Mutants lacking of more than 7 residues of the C-terminal all-beta domain could not be detected in lysates of their Escherichia coli expression strains, suggesting that an intact all-beta domain is required for structural stability. In contrast, truncation of the C-terminal extension resulted in greater stability and solubility than the wild type, as well as a lower sensitivity to the presence of added metal ions. Comparison of this mutant with the wild type suggests that the interaction of metal ions with the C-terminal extension influences performance of this enzyme. 1,4-α-Glucan-branching enzyme C-terminal Metal ion dependency Solubility Thermostability Li, Caiming aut Zhang, Yuzhu aut Gu, Zhengbiao aut Cheng, Li aut Hong, Yan aut Li, Zhaofeng (orcid)0000-0001-7571-1083 aut Enthalten in Applied biochemistry and biotechnology / A Springer US, 1994 190(2019), 3 vom: 25. Okt., Seite 1010-1022 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:190 year:2019 number:3 day:25 month:10 pages:1010-1022 https://doi.org/10.1007/s12010-019-03150-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 42.00 VZ AR 190 2019 3 25 10 1010-1022 |
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10.1007/s12010-019-03150-7 doi (DE-627)OLC2116868289 (DE-He213)s12010-019-03150-7-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Ban, Xiaofeng verfasserin aut Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02 2019 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC, part of Springer Nature 2019 Abstract By sequence comparison, the majority of 1,4-α-glucan-branching enzymes (GBEs) consist of an N-terminal carbohydrate-binding domain, a TIM-barrel catalytic domain, and a C-terminal all-beta domain. Among these structures, the GBE from Geobacillus thermoglucosidans STB02 uniquely has a highly charged 26-amino-acid C-terminal extension, whose functional roles are the least understood. In this research, the functional significance of the C-terminal domain in GBE from G. thermoglucosidans STB02 and its extension were assessed using a C-terminal deletion analysis. Mutants lacking of more than 7 residues of the C-terminal all-beta domain could not be detected in lysates of their Escherichia coli expression strains, suggesting that an intact all-beta domain is required for structural stability. In contrast, truncation of the C-terminal extension resulted in greater stability and solubility than the wild type, as well as a lower sensitivity to the presence of added metal ions. Comparison of this mutant with the wild type suggests that the interaction of metal ions with the C-terminal extension influences performance of this enzyme. 1,4-α-Glucan-branching enzyme C-terminal Metal ion dependency Solubility Thermostability Li, Caiming aut Zhang, Yuzhu aut Gu, Zhengbiao aut Cheng, Li aut Hong, Yan aut Li, Zhaofeng (orcid)0000-0001-7571-1083 aut Enthalten in Applied biochemistry and biotechnology / A Springer US, 1994 190(2019), 3 vom: 25. Okt., Seite 1010-1022 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:190 year:2019 number:3 day:25 month:10 pages:1010-1022 https://doi.org/10.1007/s12010-019-03150-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 42.00 VZ AR 190 2019 3 25 10 1010-1022 |
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Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02 |
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Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02 |
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Ban, Xiaofeng |
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Ban, Xiaofeng Li, Caiming Zhang, Yuzhu Gu, Zhengbiao Cheng, Li Hong, Yan Li, Zhaofeng |
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importance of c-terminal extension in thermophilic 1,4-α-glucan branching enzyme from geobacillus thermoglucosidans stb02 |
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Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02 |
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Abstract By sequence comparison, the majority of 1,4-α-glucan-branching enzymes (GBEs) consist of an N-terminal carbohydrate-binding domain, a TIM-barrel catalytic domain, and a C-terminal all-beta domain. Among these structures, the GBE from Geobacillus thermoglucosidans STB02 uniquely has a highly charged 26-amino-acid C-terminal extension, whose functional roles are the least understood. In this research, the functional significance of the C-terminal domain in GBE from G. thermoglucosidans STB02 and its extension were assessed using a C-terminal deletion analysis. Mutants lacking of more than 7 residues of the C-terminal all-beta domain could not be detected in lysates of their Escherichia coli expression strains, suggesting that an intact all-beta domain is required for structural stability. In contrast, truncation of the C-terminal extension resulted in greater stability and solubility than the wild type, as well as a lower sensitivity to the presence of added metal ions. Comparison of this mutant with the wild type suggests that the interaction of metal ions with the C-terminal extension influences performance of this enzyme. © Springer Science+Business Media, LLC, part of Springer Nature 2019 |
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Abstract By sequence comparison, the majority of 1,4-α-glucan-branching enzymes (GBEs) consist of an N-terminal carbohydrate-binding domain, a TIM-barrel catalytic domain, and a C-terminal all-beta domain. Among these structures, the GBE from Geobacillus thermoglucosidans STB02 uniquely has a highly charged 26-amino-acid C-terminal extension, whose functional roles are the least understood. In this research, the functional significance of the C-terminal domain in GBE from G. thermoglucosidans STB02 and its extension were assessed using a C-terminal deletion analysis. Mutants lacking of more than 7 residues of the C-terminal all-beta domain could not be detected in lysates of their Escherichia coli expression strains, suggesting that an intact all-beta domain is required for structural stability. In contrast, truncation of the C-terminal extension resulted in greater stability and solubility than the wild type, as well as a lower sensitivity to the presence of added metal ions. Comparison of this mutant with the wild type suggests that the interaction of metal ions with the C-terminal extension influences performance of this enzyme. © Springer Science+Business Media, LLC, part of Springer Nature 2019 |
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Abstract By sequence comparison, the majority of 1,4-α-glucan-branching enzymes (GBEs) consist of an N-terminal carbohydrate-binding domain, a TIM-barrel catalytic domain, and a C-terminal all-beta domain. Among these structures, the GBE from Geobacillus thermoglucosidans STB02 uniquely has a highly charged 26-amino-acid C-terminal extension, whose functional roles are the least understood. In this research, the functional significance of the C-terminal domain in GBE from G. thermoglucosidans STB02 and its extension were assessed using a C-terminal deletion analysis. Mutants lacking of more than 7 residues of the C-terminal all-beta domain could not be detected in lysates of their Escherichia coli expression strains, suggesting that an intact all-beta domain is required for structural stability. In contrast, truncation of the C-terminal extension resulted in greater stability and solubility than the wild type, as well as a lower sensitivity to the presence of added metal ions. Comparison of this mutant with the wild type suggests that the interaction of metal ions with the C-terminal extension influences performance of this enzyme. © Springer Science+Business Media, LLC, part of Springer Nature 2019 |
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Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02 |
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