Natural and engineered transglycosylases: Green tools for the enzyme-based synthesis of glycoproducts
An increasing number of transglycosylase-based processes provide access to oligosaccharides or glycoconjugates, some of them reaching performance levels compatible with industrial developments. Nevertheless, the full potential of transglycosylases has not been explored because of the challenges in t...
Ausführliche Beschreibung
Autor*in: |
Moulis, Claire [verfasserIn] Guieysse, David [verfasserIn] Morel, Sandrine [verfasserIn] Séverac, Etienne [verfasserIn] Remaud-Siméon, Magali [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2020 |
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Schlagwörter: |
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Übergeordnetes Werk: |
Enthalten in: Current opinion in chemical biology - London : Current Biology Ltd., 1997, 61, Seite 96-106 |
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Übergeordnetes Werk: |
volume:61 ; pages:96-106 |
DOI / URN: |
10.1016/j.cbpa.2020.11.004 |
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Katalog-ID: |
ELV005952352 |
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520 | |a An increasing number of transglycosylase-based processes provide access to oligosaccharides or glycoconjugates, some of them reaching performance levels compatible with industrial developments. Nevertheless, the full potential of transglycosylases has not been explored because of the challenges in transforming a glycoside hydrolase into an efficient transglycosylase. Advances in studying enzyme structure/function relationships, screening enzyme activity, and generating synthetic libraries guided by computational protein design or machine learning methods should considerably accelerate the development of these catalysts. The time has now come for researchers to uncover their possibilities and learn how to design and precisely refine their activity to respond more rapidly to the growing demand for well-defined glycosidic structures. | ||
650 | 4 | |a Transglycosylases | |
650 | 4 | |a Oligosaccharides | |
650 | 4 | |a Glycoconjugates | |
650 | 4 | |a Glycosides | |
650 | 4 | |a Enzyme engineering | |
700 | 1 | |a Guieysse, David |e verfasserin |4 aut | |
700 | 1 | |a Morel, Sandrine |e verfasserin |4 aut | |
700 | 1 | |a Séverac, Etienne |e verfasserin |4 aut | |
700 | 1 | |a Remaud-Siméon, Magali |e verfasserin |4 aut | |
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2020 |
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42.13 35.71 |
publishDate |
2020 |
allfields |
10.1016/j.cbpa.2020.11.004 doi (DE-627)ELV005952352 (ELSEVIER)S1367-5931(20)30156-3 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 42.13 bkl 35.71 bkl Moulis, Claire verfasserin (orcid)0000-0002-1937-9052 aut Natural and engineered transglycosylases: Green tools for the enzyme-based synthesis of glycoproducts 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier An increasing number of transglycosylase-based processes provide access to oligosaccharides or glycoconjugates, some of them reaching performance levels compatible with industrial developments. Nevertheless, the full potential of transglycosylases has not been explored because of the challenges in transforming a glycoside hydrolase into an efficient transglycosylase. Advances in studying enzyme structure/function relationships, screening enzyme activity, and generating synthetic libraries guided by computational protein design or machine learning methods should considerably accelerate the development of these catalysts. The time has now come for researchers to uncover their possibilities and learn how to design and precisely refine their activity to respond more rapidly to the growing demand for well-defined glycosidic structures. Transglycosylases Oligosaccharides Glycoconjugates Glycosides Enzyme engineering Guieysse, David verfasserin aut Morel, Sandrine verfasserin aut Séverac, Etienne verfasserin aut Remaud-Siméon, Magali verfasserin aut Enthalten in Current opinion in chemical biology London : Current Biology Ltd., 1997 61, Seite 96-106 Online-Ressource (DE-627)32059324X (DE-600)2019216-2 (DE-576)259271713 1879-0402 nnns volume:61 pages:96-106 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 42.13 Molekularbiologie 35.71 Biochemische Methoden AR 61 96-106 |
spelling |
10.1016/j.cbpa.2020.11.004 doi (DE-627)ELV005952352 (ELSEVIER)S1367-5931(20)30156-3 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 42.13 bkl 35.71 bkl Moulis, Claire verfasserin (orcid)0000-0002-1937-9052 aut Natural and engineered transglycosylases: Green tools for the enzyme-based synthesis of glycoproducts 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier An increasing number of transglycosylase-based processes provide access to oligosaccharides or glycoconjugates, some of them reaching performance levels compatible with industrial developments. Nevertheless, the full potential of transglycosylases has not been explored because of the challenges in transforming a glycoside hydrolase into an efficient transglycosylase. Advances in studying enzyme structure/function relationships, screening enzyme activity, and generating synthetic libraries guided by computational protein design or machine learning methods should considerably accelerate the development of these catalysts. The time has now come for researchers to uncover their possibilities and learn how to design and precisely refine their activity to respond more rapidly to the growing demand for well-defined glycosidic structures. Transglycosylases Oligosaccharides Glycoconjugates Glycosides Enzyme engineering Guieysse, David verfasserin aut Morel, Sandrine verfasserin aut Séverac, Etienne verfasserin aut Remaud-Siméon, Magali verfasserin aut Enthalten in Current opinion in chemical biology London : Current Biology Ltd., 1997 61, Seite 96-106 Online-Ressource (DE-627)32059324X (DE-600)2019216-2 (DE-576)259271713 1879-0402 nnns volume:61 pages:96-106 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 42.13 Molekularbiologie 35.71 Biochemische Methoden AR 61 96-106 |
allfields_unstemmed |
10.1016/j.cbpa.2020.11.004 doi (DE-627)ELV005952352 (ELSEVIER)S1367-5931(20)30156-3 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 42.13 bkl 35.71 bkl Moulis, Claire verfasserin (orcid)0000-0002-1937-9052 aut Natural and engineered transglycosylases: Green tools for the enzyme-based synthesis of glycoproducts 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier An increasing number of transglycosylase-based processes provide access to oligosaccharides or glycoconjugates, some of them reaching performance levels compatible with industrial developments. Nevertheless, the full potential of transglycosylases has not been explored because of the challenges in transforming a glycoside hydrolase into an efficient transglycosylase. Advances in studying enzyme structure/function relationships, screening enzyme activity, and generating synthetic libraries guided by computational protein design or machine learning methods should considerably accelerate the development of these catalysts. The time has now come for researchers to uncover their possibilities and learn how to design and precisely refine their activity to respond more rapidly to the growing demand for well-defined glycosidic structures. Transglycosylases Oligosaccharides Glycoconjugates Glycosides Enzyme engineering Guieysse, David verfasserin aut Morel, Sandrine verfasserin aut Séverac, Etienne verfasserin aut Remaud-Siméon, Magali verfasserin aut Enthalten in Current opinion in chemical biology London : Current Biology Ltd., 1997 61, Seite 96-106 Online-Ressource (DE-627)32059324X (DE-600)2019216-2 (DE-576)259271713 1879-0402 nnns volume:61 pages:96-106 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 42.13 Molekularbiologie 35.71 Biochemische Methoden AR 61 96-106 |
allfieldsGer |
10.1016/j.cbpa.2020.11.004 doi (DE-627)ELV005952352 (ELSEVIER)S1367-5931(20)30156-3 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 42.13 bkl 35.71 bkl Moulis, Claire verfasserin (orcid)0000-0002-1937-9052 aut Natural and engineered transglycosylases: Green tools for the enzyme-based synthesis of glycoproducts 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier An increasing number of transglycosylase-based processes provide access to oligosaccharides or glycoconjugates, some of them reaching performance levels compatible with industrial developments. Nevertheless, the full potential of transglycosylases has not been explored because of the challenges in transforming a glycoside hydrolase into an efficient transglycosylase. Advances in studying enzyme structure/function relationships, screening enzyme activity, and generating synthetic libraries guided by computational protein design or machine learning methods should considerably accelerate the development of these catalysts. The time has now come for researchers to uncover their possibilities and learn how to design and precisely refine their activity to respond more rapidly to the growing demand for well-defined glycosidic structures. Transglycosylases Oligosaccharides Glycoconjugates Glycosides Enzyme engineering Guieysse, David verfasserin aut Morel, Sandrine verfasserin aut Séverac, Etienne verfasserin aut Remaud-Siméon, Magali verfasserin aut Enthalten in Current opinion in chemical biology London : Current Biology Ltd., 1997 61, Seite 96-106 Online-Ressource (DE-627)32059324X (DE-600)2019216-2 (DE-576)259271713 1879-0402 nnns volume:61 pages:96-106 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 42.13 Molekularbiologie 35.71 Biochemische Methoden AR 61 96-106 |
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Natural and engineered transglycosylases: Green tools for the enzyme-based synthesis of glycoproducts |
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Natural and engineered transglycosylases: Green tools for the enzyme-based synthesis of glycoproducts |
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Moulis, Claire |
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Moulis, Claire Guieysse, David Morel, Sandrine Séverac, Etienne Remaud-Siméon, Magali |
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Moulis, Claire |
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natural and engineered transglycosylases: green tools for the enzyme-based synthesis of glycoproducts |
title_auth |
Natural and engineered transglycosylases: Green tools for the enzyme-based synthesis of glycoproducts |
abstract |
An increasing number of transglycosylase-based processes provide access to oligosaccharides or glycoconjugates, some of them reaching performance levels compatible with industrial developments. Nevertheless, the full potential of transglycosylases has not been explored because of the challenges in transforming a glycoside hydrolase into an efficient transglycosylase. Advances in studying enzyme structure/function relationships, screening enzyme activity, and generating synthetic libraries guided by computational protein design or machine learning methods should considerably accelerate the development of these catalysts. The time has now come for researchers to uncover their possibilities and learn how to design and precisely refine their activity to respond more rapidly to the growing demand for well-defined glycosidic structures. |
abstractGer |
An increasing number of transglycosylase-based processes provide access to oligosaccharides or glycoconjugates, some of them reaching performance levels compatible with industrial developments. Nevertheless, the full potential of transglycosylases has not been explored because of the challenges in transforming a glycoside hydrolase into an efficient transglycosylase. Advances in studying enzyme structure/function relationships, screening enzyme activity, and generating synthetic libraries guided by computational protein design or machine learning methods should considerably accelerate the development of these catalysts. The time has now come for researchers to uncover their possibilities and learn how to design and precisely refine their activity to respond more rapidly to the growing demand for well-defined glycosidic structures. |
abstract_unstemmed |
An increasing number of transglycosylase-based processes provide access to oligosaccharides or glycoconjugates, some of them reaching performance levels compatible with industrial developments. Nevertheless, the full potential of transglycosylases has not been explored because of the challenges in transforming a glycoside hydrolase into an efficient transglycosylase. Advances in studying enzyme structure/function relationships, screening enzyme activity, and generating synthetic libraries guided by computational protein design or machine learning methods should considerably accelerate the development of these catalysts. The time has now come for researchers to uncover their possibilities and learn how to design and precisely refine their activity to respond more rapidly to the growing demand for well-defined glycosidic structures. |
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title_short |
Natural and engineered transglycosylases: Green tools for the enzyme-based synthesis of glycoproducts |
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Guieysse, David Morel, Sandrine Séverac, Etienne Remaud-Siméon, Magali |
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up_date |
2024-07-06T19:43:00.774Z |
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