Large α-aminonitrilase activity screening of nitrilase superfamily members: Access to conversion and enantiospecificity by LC–MS
Highlights • We performed a large nitrilase activity screening on α-aminonitriles. • The enzyme collection covers the whole biodiversity of the nitrilase superfamily. • An efficient LC-MS/MS method gave access to both conversion and enantiospecificity. • Five new α-aminonitrilases were found, with n...
Ausführliche Beschreibung
Autor*in: |
Bordier, Franck [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2014 |
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Schlagwörter: |
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Umfang: |
10 |
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Übergeordnetes Werk: |
Enthalten in: CME Activities Calendar - 2014, Amsterdam [u.a.] |
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Übergeordnetes Werk: |
volume:107 ; year:2014 ; pages:79-88 ; extent:10 |
Links: |
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DOI / URN: |
10.1016/j.molcatb.2014.05.019 |
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ELV022412972 |
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520 | |a Highlights • We performed a large nitrilase activity screening on α-aminonitriles. • The enzyme collection covers the whole biodiversity of the nitrilase superfamily. • An efficient LC-MS/MS method gave access to both conversion and enantiospecificity. • Five new α-aminonitrilases were found, with no nitrile hydratase activity. • (S)-Norvaline, (R)-phenylglycine and two phenylglycine derivatives were obtained. | ||
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10.1016/j.molcatb.2014.05.019 doi GBVA2014002000026.pica (DE-627)ELV022412972 (ELSEVIER)S1381-1177(14)00169-6 DE-627 ger DE-627 rakwb eng 540 540 DE-600 610 VZ 610 VZ 44.85 bkl Bordier, Franck verfasserin aut Large α-aminonitrilase activity screening of nitrilase superfamily members: Access to conversion and enantiospecificity by LC–MS 2014 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Highlights • We performed a large nitrilase activity screening on α-aminonitriles. • The enzyme collection covers the whole biodiversity of the nitrilase superfamily. • An efficient LC-MS/MS method gave access to both conversion and enantiospecificity. • Five new α-aminonitrilases were found, with no nitrile hydratase activity. • (S)-Norvaline, (R)-phenylglycine and two phenylglycine derivatives were obtained. LC–MS screening Elsevier Enantiospecificity Elsevier Nitrilase Elsevier Alpha-aminonitrile Elsevier Stam, Mark oth Darii, Ekaterina oth Tricot, Sabine oth Fossey, Aurélie oth Rohault, Johanna oth Debard, Adrien oth Mariage, Aline oth Pellouin, Virginie oth Petit, Jean-Louis oth Perret, Alain oth Vallenet, David oth Salanoubat, Marcel oth Weissenbach, Jean oth Vergne-Vaxelaire, Carine oth de Berardinis, Véronique oth Zaparucha, Anne oth Enthalten in Elsevier Science CME Activities Calendar 2014 Amsterdam [u.a.] (DE-627)ELV011989025 volume:107 year:2014 pages:79-88 extent:10 https://doi.org/10.1016/j.molcatb.2014.05.019 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.85 Kardiologie Angiologie VZ AR 107 2014 79-88 10 045F 540 |
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10.1016/j.molcatb.2014.05.019 doi GBVA2014002000026.pica (DE-627)ELV022412972 (ELSEVIER)S1381-1177(14)00169-6 DE-627 ger DE-627 rakwb eng 540 540 DE-600 610 VZ 610 VZ 44.85 bkl Bordier, Franck verfasserin aut Large α-aminonitrilase activity screening of nitrilase superfamily members: Access to conversion and enantiospecificity by LC–MS 2014 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Highlights • We performed a large nitrilase activity screening on α-aminonitriles. • The enzyme collection covers the whole biodiversity of the nitrilase superfamily. • An efficient LC-MS/MS method gave access to both conversion and enantiospecificity. • Five new α-aminonitrilases were found, with no nitrile hydratase activity. • (S)-Norvaline, (R)-phenylglycine and two phenylglycine derivatives were obtained. LC–MS screening Elsevier Enantiospecificity Elsevier Nitrilase Elsevier Alpha-aminonitrile Elsevier Stam, Mark oth Darii, Ekaterina oth Tricot, Sabine oth Fossey, Aurélie oth Rohault, Johanna oth Debard, Adrien oth Mariage, Aline oth Pellouin, Virginie oth Petit, Jean-Louis oth Perret, Alain oth Vallenet, David oth Salanoubat, Marcel oth Weissenbach, Jean oth Vergne-Vaxelaire, Carine oth de Berardinis, Véronique oth Zaparucha, Anne oth Enthalten in Elsevier Science CME Activities Calendar 2014 Amsterdam [u.a.] (DE-627)ELV011989025 volume:107 year:2014 pages:79-88 extent:10 https://doi.org/10.1016/j.molcatb.2014.05.019 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.85 Kardiologie Angiologie VZ AR 107 2014 79-88 10 045F 540 |
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10.1016/j.molcatb.2014.05.019 doi GBVA2014002000026.pica (DE-627)ELV022412972 (ELSEVIER)S1381-1177(14)00169-6 DE-627 ger DE-627 rakwb eng 540 540 DE-600 610 VZ 610 VZ 44.85 bkl Bordier, Franck verfasserin aut Large α-aminonitrilase activity screening of nitrilase superfamily members: Access to conversion and enantiospecificity by LC–MS 2014 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Highlights • We performed a large nitrilase activity screening on α-aminonitriles. • The enzyme collection covers the whole biodiversity of the nitrilase superfamily. • An efficient LC-MS/MS method gave access to both conversion and enantiospecificity. • Five new α-aminonitrilases were found, with no nitrile hydratase activity. • (S)-Norvaline, (R)-phenylglycine and two phenylglycine derivatives were obtained. LC–MS screening Elsevier Enantiospecificity Elsevier Nitrilase Elsevier Alpha-aminonitrile Elsevier Stam, Mark oth Darii, Ekaterina oth Tricot, Sabine oth Fossey, Aurélie oth Rohault, Johanna oth Debard, Adrien oth Mariage, Aline oth Pellouin, Virginie oth Petit, Jean-Louis oth Perret, Alain oth Vallenet, David oth Salanoubat, Marcel oth Weissenbach, Jean oth Vergne-Vaxelaire, Carine oth de Berardinis, Véronique oth Zaparucha, Anne oth Enthalten in Elsevier Science CME Activities Calendar 2014 Amsterdam [u.a.] (DE-627)ELV011989025 volume:107 year:2014 pages:79-88 extent:10 https://doi.org/10.1016/j.molcatb.2014.05.019 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.85 Kardiologie Angiologie VZ AR 107 2014 79-88 10 045F 540 |
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10.1016/j.molcatb.2014.05.019 doi GBVA2014002000026.pica (DE-627)ELV022412972 (ELSEVIER)S1381-1177(14)00169-6 DE-627 ger DE-627 rakwb eng 540 540 DE-600 610 VZ 610 VZ 44.85 bkl Bordier, Franck verfasserin aut Large α-aminonitrilase activity screening of nitrilase superfamily members: Access to conversion and enantiospecificity by LC–MS 2014 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Highlights • We performed a large nitrilase activity screening on α-aminonitriles. • The enzyme collection covers the whole biodiversity of the nitrilase superfamily. • An efficient LC-MS/MS method gave access to both conversion and enantiospecificity. • Five new α-aminonitrilases were found, with no nitrile hydratase activity. • (S)-Norvaline, (R)-phenylglycine and two phenylglycine derivatives were obtained. LC–MS screening Elsevier Enantiospecificity Elsevier Nitrilase Elsevier Alpha-aminonitrile Elsevier Stam, Mark oth Darii, Ekaterina oth Tricot, Sabine oth Fossey, Aurélie oth Rohault, Johanna oth Debard, Adrien oth Mariage, Aline oth Pellouin, Virginie oth Petit, Jean-Louis oth Perret, Alain oth Vallenet, David oth Salanoubat, Marcel oth Weissenbach, Jean oth Vergne-Vaxelaire, Carine oth de Berardinis, Véronique oth Zaparucha, Anne oth Enthalten in Elsevier Science CME Activities Calendar 2014 Amsterdam [u.a.] (DE-627)ELV011989025 volume:107 year:2014 pages:79-88 extent:10 https://doi.org/10.1016/j.molcatb.2014.05.019 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.85 Kardiologie Angiologie VZ AR 107 2014 79-88 10 045F 540 |
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10.1016/j.molcatb.2014.05.019 doi GBVA2014002000026.pica (DE-627)ELV022412972 (ELSEVIER)S1381-1177(14)00169-6 DE-627 ger DE-627 rakwb eng 540 540 DE-600 610 VZ 610 VZ 44.85 bkl Bordier, Franck verfasserin aut Large α-aminonitrilase activity screening of nitrilase superfamily members: Access to conversion and enantiospecificity by LC–MS 2014 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Highlights • We performed a large nitrilase activity screening on α-aminonitriles. • The enzyme collection covers the whole biodiversity of the nitrilase superfamily. • An efficient LC-MS/MS method gave access to both conversion and enantiospecificity. • Five new α-aminonitrilases were found, with no nitrile hydratase activity. • (S)-Norvaline, (R)-phenylglycine and two phenylglycine derivatives were obtained. LC–MS screening Elsevier Enantiospecificity Elsevier Nitrilase Elsevier Alpha-aminonitrile Elsevier Stam, Mark oth Darii, Ekaterina oth Tricot, Sabine oth Fossey, Aurélie oth Rohault, Johanna oth Debard, Adrien oth Mariage, Aline oth Pellouin, Virginie oth Petit, Jean-Louis oth Perret, Alain oth Vallenet, David oth Salanoubat, Marcel oth Weissenbach, Jean oth Vergne-Vaxelaire, Carine oth de Berardinis, Véronique oth Zaparucha, Anne oth Enthalten in Elsevier Science CME Activities Calendar 2014 Amsterdam [u.a.] (DE-627)ELV011989025 volume:107 year:2014 pages:79-88 extent:10 https://doi.org/10.1016/j.molcatb.2014.05.019 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.85 Kardiologie Angiologie VZ AR 107 2014 79-88 10 045F 540 |
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Large α-aminonitrilase activity screening of nitrilase superfamily members: Access to conversion and enantiospecificity by LC–MS |
author_sort |
Bordier, Franck |
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CME Activities Calendar |
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CME Activities Calendar |
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eng |
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false |
dewey-hundreds |
500 - Science 600 - Technology |
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2014 |
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79 |
author_browse |
Bordier, Franck |
container_volume |
107 |
physical |
10 |
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540 540 DE-600 610 VZ 44.85 bkl |
format_se |
Elektronische Aufsätze |
author-letter |
Bordier, Franck |
doi_str_mv |
10.1016/j.molcatb.2014.05.019 |
dewey-full |
540 610 |
title_sort |
large α-aminonitrilase activity screening of nitrilase superfamily members: access to conversion and enantiospecificity by lc–ms |
title_auth |
Large α-aminonitrilase activity screening of nitrilase superfamily members: Access to conversion and enantiospecificity by LC–MS |
abstract |
Highlights • We performed a large nitrilase activity screening on α-aminonitriles. • The enzyme collection covers the whole biodiversity of the nitrilase superfamily. • An efficient LC-MS/MS method gave access to both conversion and enantiospecificity. • Five new α-aminonitrilases were found, with no nitrile hydratase activity. • (S)-Norvaline, (R)-phenylglycine and two phenylglycine derivatives were obtained. |
abstractGer |
Highlights • We performed a large nitrilase activity screening on α-aminonitriles. • The enzyme collection covers the whole biodiversity of the nitrilase superfamily. • An efficient LC-MS/MS method gave access to both conversion and enantiospecificity. • Five new α-aminonitrilases were found, with no nitrile hydratase activity. • (S)-Norvaline, (R)-phenylglycine and two phenylglycine derivatives were obtained. |
abstract_unstemmed |
Highlights • We performed a large nitrilase activity screening on α-aminonitriles. • The enzyme collection covers the whole biodiversity of the nitrilase superfamily. • An efficient LC-MS/MS method gave access to both conversion and enantiospecificity. • Five new α-aminonitrilases were found, with no nitrile hydratase activity. • (S)-Norvaline, (R)-phenylglycine and two phenylglycine derivatives were obtained. |
collection_details |
GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA |
title_short |
Large α-aminonitrilase activity screening of nitrilase superfamily members: Access to conversion and enantiospecificity by LC–MS |
url |
https://doi.org/10.1016/j.molcatb.2014.05.019 |
remote_bool |
true |
author2 |
Stam, Mark Darii, Ekaterina Tricot, Sabine Fossey, Aurélie Rohault, Johanna Debard, Adrien Mariage, Aline Pellouin, Virginie Petit, Jean-Louis Perret, Alain Vallenet, David Salanoubat, Marcel Weissenbach, Jean Vergne-Vaxelaire, Carine de Berardinis, Véronique Zaparucha, Anne |
author2Str |
Stam, Mark Darii, Ekaterina Tricot, Sabine Fossey, Aurélie Rohault, Johanna Debard, Adrien Mariage, Aline Pellouin, Virginie Petit, Jean-Louis Perret, Alain Vallenet, David Salanoubat, Marcel Weissenbach, Jean Vergne-Vaxelaire, Carine de Berardinis, Véronique Zaparucha, Anne |
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ELV011989025 |
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author2_role |
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doi_str |
10.1016/j.molcatb.2014.05.019 |
up_date |
2024-07-06T21:55:29.725Z |
_version_ |
1803868364840370176 |
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