Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars
Abstract Most of the “repressor, open reading frame, kinase” (ROK) proteins already characterized so far, and exhibiting a kinase activity, take restrictedly d-glucose as substrate. By exploring the sequenced bacterial diversity, 61 ATP-dependent kinases belonging to the ROK family have been identif...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Vergne-Vaxelaire, Carine [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2018 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Berlin : Springer, 1975, 102(2018), 13 vom: 04. Mai, Seite 5569-5583 |
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| Übergeordnetes Werk: |
volume:102 ; year:2018 ; number:13 ; day:04 ; month:05 ; pages:5569-5583 |
| Links: |
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| DOI / URN: |
10.1007/s00253-018-9018-1 |
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| Katalog-ID: |
SPR00302587X |
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| 245 | 1 | 0 | |a Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars |
| 264 | 1 | |c 2018 | |
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| 500 | |a © Springer-Verlag GmbH Germany, part of Springer Nature 2018 | ||
| 520 | |a Abstract Most of the “repressor, open reading frame, kinase” (ROK) proteins already characterized so far, and exhibiting a kinase activity, take restrictedly d-glucose as substrate. By exploring the sequenced bacterial diversity, 61 ATP-dependent kinases belonging to the ROK family have been identified and experimentally assayed for the phosphorylation of hexoses. These kinases were mainly found to be thermotolerant and highly active toward d-mannose and d-fructose with notable activities toward d-tagatose. Among them, the ATP-dependent kinase from the mesophile Streptococcus mitis (named $ ScrK_{mitis} $) was biochemically characterized and its substrate spectrum further studied. This enzyme possessed impressive catalytic efficiencies toward d-mannose and d-fructose of 1.5 $ 10^{6} $ $ s^{−1} $ $ M^{−1} $ and 2.7 $ 10^{5} $ $ s^{−1} $ $ M^{−1} $, respectively, but also significant ones toward d-tagatose (3.5 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $) and the unnatural monosaccharides d-altrose (1.1 $ 10^{4} $ $ s^{−1} $ $ M^{−1} $) and d-talose (3.4 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $). Specific activities measured for all hexoses showed a high stereopreference for d- over l-series. As proof of concept, 8 hexoses were phosphorylated in moderate to good yields, some of them described for the first time like l-sorbose-5-phosphate unusually phosphorylated in position 5. Its thermotolerance, its wide pH tolerance (from 7 to 10), and temperature range (> 85% activity between 40 and 70 °C) open the way to applications in the enzymatic synthesis of monophosphorylated hexoses. | ||
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| 650 | 4 | |a Fructokinase |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Thermotolerance |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a ROK family |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Phosphorylated sugars |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Promiscuity |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Mariage, Aline |4 aut | |
| 700 | 1 | |a Petit, Jean-Louis |4 aut | |
| 700 | 1 | |a Fossey-Jouenne, Aurélie |4 aut | |
| 700 | 1 | |a Guérard-Hélaine, Christine |4 aut | |
| 700 | 1 | |a Darii, Ekaterina |4 aut | |
| 700 | 1 | |a Debard, Adrien |4 aut | |
| 700 | 1 | |a Nepert, Stessy |4 aut | |
| 700 | 1 | |a Pellouin, Virginie |4 aut | |
| 700 | 1 | |a Lemaire, Marielle |4 aut | |
| 700 | 1 | |a Zaparucha, Anne |4 aut | |
| 700 | 1 | |a Salanoubat, Marcel |4 aut | |
| 700 | 1 | |a de Berardinis, Véronique |0 (orcid)0000-0002-3273-4135 |4 aut | |
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10.1007/s00253-018-9018-1 doi (DE-627)SPR00302587X (SPR)s00253-018-9018-1-e DE-627 ger DE-627 rakwb eng Vergne-Vaxelaire, Carine verfasserin aut Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract Most of the “repressor, open reading frame, kinase” (ROK) proteins already characterized so far, and exhibiting a kinase activity, take restrictedly d-glucose as substrate. By exploring the sequenced bacterial diversity, 61 ATP-dependent kinases belonging to the ROK family have been identified and experimentally assayed for the phosphorylation of hexoses. These kinases were mainly found to be thermotolerant and highly active toward d-mannose and d-fructose with notable activities toward d-tagatose. Among them, the ATP-dependent kinase from the mesophile Streptococcus mitis (named $ ScrK_{mitis} $) was biochemically characterized and its substrate spectrum further studied. This enzyme possessed impressive catalytic efficiencies toward d-mannose and d-fructose of 1.5 $ 10^{6} $ $ s^{−1} $ $ M^{−1} $ and 2.7 $ 10^{5} $ $ s^{−1} $ $ M^{−1} $, respectively, but also significant ones toward d-tagatose (3.5 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $) and the unnatural monosaccharides d-altrose (1.1 $ 10^{4} $ $ s^{−1} $ $ M^{−1} $) and d-talose (3.4 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $). Specific activities measured for all hexoses showed a high stereopreference for d- over l-series. As proof of concept, 8 hexoses were phosphorylated in moderate to good yields, some of them described for the first time like l-sorbose-5-phosphate unusually phosphorylated in position 5. Its thermotolerance, its wide pH tolerance (from 7 to 10), and temperature range (> 85% activity between 40 and 70 °C) open the way to applications in the enzymatic synthesis of monophosphorylated hexoses. Hexokinase (dpeaa)DE-He213 Fructokinase (dpeaa)DE-He213 Thermotolerance (dpeaa)DE-He213 ROK family (dpeaa)DE-He213 Phosphorylated sugars (dpeaa)DE-He213 Promiscuity (dpeaa)DE-He213 Mariage, Aline aut Petit, Jean-Louis aut Fossey-Jouenne, Aurélie aut Guérard-Hélaine, Christine aut Darii, Ekaterina aut Debard, Adrien aut Nepert, Stessy aut Pellouin, Virginie aut Lemaire, Marielle aut Zaparucha, Anne aut Salanoubat, Marcel aut de Berardinis, Véronique (orcid)0000-0002-3273-4135 aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 102(2018), 13 vom: 04. Mai, Seite 5569-5583 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:102 year:2018 number:13 day:04 month:05 pages:5569-5583 https://dx.doi.org/10.1007/s00253-018-9018-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 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_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 102 2018 13 04 05 5569-5583 |
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10.1007/s00253-018-9018-1 doi (DE-627)SPR00302587X (SPR)s00253-018-9018-1-e DE-627 ger DE-627 rakwb eng Vergne-Vaxelaire, Carine verfasserin aut Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract Most of the “repressor, open reading frame, kinase” (ROK) proteins already characterized so far, and exhibiting a kinase activity, take restrictedly d-glucose as substrate. By exploring the sequenced bacterial diversity, 61 ATP-dependent kinases belonging to the ROK family have been identified and experimentally assayed for the phosphorylation of hexoses. These kinases were mainly found to be thermotolerant and highly active toward d-mannose and d-fructose with notable activities toward d-tagatose. Among them, the ATP-dependent kinase from the mesophile Streptococcus mitis (named $ ScrK_{mitis} $) was biochemically characterized and its substrate spectrum further studied. This enzyme possessed impressive catalytic efficiencies toward d-mannose and d-fructose of 1.5 $ 10^{6} $ $ s^{−1} $ $ M^{−1} $ and 2.7 $ 10^{5} $ $ s^{−1} $ $ M^{−1} $, respectively, but also significant ones toward d-tagatose (3.5 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $) and the unnatural monosaccharides d-altrose (1.1 $ 10^{4} $ $ s^{−1} $ $ M^{−1} $) and d-talose (3.4 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $). Specific activities measured for all hexoses showed a high stereopreference for d- over l-series. As proof of concept, 8 hexoses were phosphorylated in moderate to good yields, some of them described for the first time like l-sorbose-5-phosphate unusually phosphorylated in position 5. Its thermotolerance, its wide pH tolerance (from 7 to 10), and temperature range (> 85% activity between 40 and 70 °C) open the way to applications in the enzymatic synthesis of monophosphorylated hexoses. Hexokinase (dpeaa)DE-He213 Fructokinase (dpeaa)DE-He213 Thermotolerance (dpeaa)DE-He213 ROK family (dpeaa)DE-He213 Phosphorylated sugars (dpeaa)DE-He213 Promiscuity (dpeaa)DE-He213 Mariage, Aline aut Petit, Jean-Louis aut Fossey-Jouenne, Aurélie aut Guérard-Hélaine, Christine aut Darii, Ekaterina aut Debard, Adrien aut Nepert, Stessy aut Pellouin, Virginie aut Lemaire, Marielle aut Zaparucha, Anne aut Salanoubat, Marcel aut de Berardinis, Véronique (orcid)0000-0002-3273-4135 aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 102(2018), 13 vom: 04. Mai, Seite 5569-5583 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:102 year:2018 number:13 day:04 month:05 pages:5569-5583 https://dx.doi.org/10.1007/s00253-018-9018-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 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_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 102 2018 13 04 05 5569-5583 |
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10.1007/s00253-018-9018-1 doi (DE-627)SPR00302587X (SPR)s00253-018-9018-1-e DE-627 ger DE-627 rakwb eng Vergne-Vaxelaire, Carine verfasserin aut Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract Most of the “repressor, open reading frame, kinase” (ROK) proteins already characterized so far, and exhibiting a kinase activity, take restrictedly d-glucose as substrate. By exploring the sequenced bacterial diversity, 61 ATP-dependent kinases belonging to the ROK family have been identified and experimentally assayed for the phosphorylation of hexoses. These kinases were mainly found to be thermotolerant and highly active toward d-mannose and d-fructose with notable activities toward d-tagatose. Among them, the ATP-dependent kinase from the mesophile Streptococcus mitis (named $ ScrK_{mitis} $) was biochemically characterized and its substrate spectrum further studied. This enzyme possessed impressive catalytic efficiencies toward d-mannose and d-fructose of 1.5 $ 10^{6} $ $ s^{−1} $ $ M^{−1} $ and 2.7 $ 10^{5} $ $ s^{−1} $ $ M^{−1} $, respectively, but also significant ones toward d-tagatose (3.5 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $) and the unnatural monosaccharides d-altrose (1.1 $ 10^{4} $ $ s^{−1} $ $ M^{−1} $) and d-talose (3.4 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $). Specific activities measured for all hexoses showed a high stereopreference for d- over l-series. As proof of concept, 8 hexoses were phosphorylated in moderate to good yields, some of them described for the first time like l-sorbose-5-phosphate unusually phosphorylated in position 5. Its thermotolerance, its wide pH tolerance (from 7 to 10), and temperature range (> 85% activity between 40 and 70 °C) open the way to applications in the enzymatic synthesis of monophosphorylated hexoses. Hexokinase (dpeaa)DE-He213 Fructokinase (dpeaa)DE-He213 Thermotolerance (dpeaa)DE-He213 ROK family (dpeaa)DE-He213 Phosphorylated sugars (dpeaa)DE-He213 Promiscuity (dpeaa)DE-He213 Mariage, Aline aut Petit, Jean-Louis aut Fossey-Jouenne, Aurélie aut Guérard-Hélaine, Christine aut Darii, Ekaterina aut Debard, Adrien aut Nepert, Stessy aut Pellouin, Virginie aut Lemaire, Marielle aut Zaparucha, Anne aut Salanoubat, Marcel aut de Berardinis, Véronique (orcid)0000-0002-3273-4135 aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 102(2018), 13 vom: 04. Mai, Seite 5569-5583 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:102 year:2018 number:13 day:04 month:05 pages:5569-5583 https://dx.doi.org/10.1007/s00253-018-9018-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 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_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 102 2018 13 04 05 5569-5583 |
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10.1007/s00253-018-9018-1 doi (DE-627)SPR00302587X (SPR)s00253-018-9018-1-e DE-627 ger DE-627 rakwb eng Vergne-Vaxelaire, Carine verfasserin aut Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract Most of the “repressor, open reading frame, kinase” (ROK) proteins already characterized so far, and exhibiting a kinase activity, take restrictedly d-glucose as substrate. By exploring the sequenced bacterial diversity, 61 ATP-dependent kinases belonging to the ROK family have been identified and experimentally assayed for the phosphorylation of hexoses. These kinases were mainly found to be thermotolerant and highly active toward d-mannose and d-fructose with notable activities toward d-tagatose. Among them, the ATP-dependent kinase from the mesophile Streptococcus mitis (named $ ScrK_{mitis} $) was biochemically characterized and its substrate spectrum further studied. This enzyme possessed impressive catalytic efficiencies toward d-mannose and d-fructose of 1.5 $ 10^{6} $ $ s^{−1} $ $ M^{−1} $ and 2.7 $ 10^{5} $ $ s^{−1} $ $ M^{−1} $, respectively, but also significant ones toward d-tagatose (3.5 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $) and the unnatural monosaccharides d-altrose (1.1 $ 10^{4} $ $ s^{−1} $ $ M^{−1} $) and d-talose (3.4 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $). Specific activities measured for all hexoses showed a high stereopreference for d- over l-series. As proof of concept, 8 hexoses were phosphorylated in moderate to good yields, some of them described for the first time like l-sorbose-5-phosphate unusually phosphorylated in position 5. Its thermotolerance, its wide pH tolerance (from 7 to 10), and temperature range (> 85% activity between 40 and 70 °C) open the way to applications in the enzymatic synthesis of monophosphorylated hexoses. Hexokinase (dpeaa)DE-He213 Fructokinase (dpeaa)DE-He213 Thermotolerance (dpeaa)DE-He213 ROK family (dpeaa)DE-He213 Phosphorylated sugars (dpeaa)DE-He213 Promiscuity (dpeaa)DE-He213 Mariage, Aline aut Petit, Jean-Louis aut Fossey-Jouenne, Aurélie aut Guérard-Hélaine, Christine aut Darii, Ekaterina aut Debard, Adrien aut Nepert, Stessy aut Pellouin, Virginie aut Lemaire, Marielle aut Zaparucha, Anne aut Salanoubat, Marcel aut de Berardinis, Véronique (orcid)0000-0002-3273-4135 aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 102(2018), 13 vom: 04. Mai, Seite 5569-5583 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:102 year:2018 number:13 day:04 month:05 pages:5569-5583 https://dx.doi.org/10.1007/s00253-018-9018-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 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_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 102 2018 13 04 05 5569-5583 |
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10.1007/s00253-018-9018-1 doi (DE-627)SPR00302587X (SPR)s00253-018-9018-1-e DE-627 ger DE-627 rakwb eng Vergne-Vaxelaire, Carine verfasserin aut Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract Most of the “repressor, open reading frame, kinase” (ROK) proteins already characterized so far, and exhibiting a kinase activity, take restrictedly d-glucose as substrate. By exploring the sequenced bacterial diversity, 61 ATP-dependent kinases belonging to the ROK family have been identified and experimentally assayed for the phosphorylation of hexoses. These kinases were mainly found to be thermotolerant and highly active toward d-mannose and d-fructose with notable activities toward d-tagatose. Among them, the ATP-dependent kinase from the mesophile Streptococcus mitis (named $ ScrK_{mitis} $) was biochemically characterized and its substrate spectrum further studied. This enzyme possessed impressive catalytic efficiencies toward d-mannose and d-fructose of 1.5 $ 10^{6} $ $ s^{−1} $ $ M^{−1} $ and 2.7 $ 10^{5} $ $ s^{−1} $ $ M^{−1} $, respectively, but also significant ones toward d-tagatose (3.5 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $) and the unnatural monosaccharides d-altrose (1.1 $ 10^{4} $ $ s^{−1} $ $ M^{−1} $) and d-talose (3.4 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $). Specific activities measured for all hexoses showed a high stereopreference for d- over l-series. As proof of concept, 8 hexoses were phosphorylated in moderate to good yields, some of them described for the first time like l-sorbose-5-phosphate unusually phosphorylated in position 5. Its thermotolerance, its wide pH tolerance (from 7 to 10), and temperature range (> 85% activity between 40 and 70 °C) open the way to applications in the enzymatic synthesis of monophosphorylated hexoses. Hexokinase (dpeaa)DE-He213 Fructokinase (dpeaa)DE-He213 Thermotolerance (dpeaa)DE-He213 ROK family (dpeaa)DE-He213 Phosphorylated sugars (dpeaa)DE-He213 Promiscuity (dpeaa)DE-He213 Mariage, Aline aut Petit, Jean-Louis aut Fossey-Jouenne, Aurélie aut Guérard-Hélaine, Christine aut Darii, Ekaterina aut Debard, Adrien aut Nepert, Stessy aut Pellouin, Virginie aut Lemaire, Marielle aut Zaparucha, Anne aut Salanoubat, Marcel aut de Berardinis, Véronique (orcid)0000-0002-3273-4135 aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 102(2018), 13 vom: 04. Mai, Seite 5569-5583 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:102 year:2018 number:13 day:04 month:05 pages:5569-5583 https://dx.doi.org/10.1007/s00253-018-9018-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 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_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 102 2018 13 04 05 5569-5583 |
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Enthalten in Applied microbiology and biotechnology 102(2018), 13 vom: 04. Mai, Seite 5569-5583 volume:102 year:2018 number:13 day:04 month:05 pages:5569-5583 |
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Vergne-Vaxelaire, Carine @@aut@@ Mariage, Aline @@aut@@ Petit, Jean-Louis @@aut@@ Fossey-Jouenne, Aurélie @@aut@@ Guérard-Hélaine, Christine @@aut@@ Darii, Ekaterina @@aut@@ Debard, Adrien @@aut@@ Nepert, Stessy @@aut@@ Pellouin, Virginie @@aut@@ Lemaire, Marielle @@aut@@ Zaparucha, Anne @@aut@@ Salanoubat, Marcel @@aut@@ de Berardinis, Véronique @@aut@@ |
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By exploring the sequenced bacterial diversity, 61 ATP-dependent kinases belonging to the ROK family have been identified and experimentally assayed for the phosphorylation of hexoses. These kinases were mainly found to be thermotolerant and highly active toward d-mannose and d-fructose with notable activities toward d-tagatose. Among them, the ATP-dependent kinase from the mesophile Streptococcus mitis (named $ ScrK_{mitis} $) was biochemically characterized and its substrate spectrum further studied. This enzyme possessed impressive catalytic efficiencies toward d-mannose and d-fructose of 1.5 $ 10^{6} $ $ s^{−1} $ $ M^{−1} $ and 2.7 $ 10^{5} $ $ s^{−1} $ $ M^{−1} $, respectively, but also significant ones toward d-tagatose (3.5 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $) and the unnatural monosaccharides d-altrose (1.1 $ 10^{4} $ $ s^{−1} $ $ M^{−1} $) and d-talose (3.4 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $). Specific activities measured for all hexoses showed a high stereopreference for d- over l-series. As proof of concept, 8 hexoses were phosphorylated in moderate to good yields, some of them described for the first time like l-sorbose-5-phosphate unusually phosphorylated in position 5. 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Vergne-Vaxelaire, Carine |
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Vergne-Vaxelaire, Carine misc Hexokinase misc Fructokinase misc Thermotolerance misc ROK family misc Phosphorylated sugars misc Promiscuity Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars |
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Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars Hexokinase (dpeaa)DE-He213 Fructokinase (dpeaa)DE-He213 Thermotolerance (dpeaa)DE-He213 ROK family (dpeaa)DE-He213 Phosphorylated sugars (dpeaa)DE-He213 Promiscuity (dpeaa)DE-He213 |
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Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars |
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Vergne-Vaxelaire, Carine Mariage, Aline Petit, Jean-Louis Fossey-Jouenne, Aurélie Guérard-Hélaine, Christine Darii, Ekaterina Debard, Adrien Nepert, Stessy Pellouin, Virginie Lemaire, Marielle Zaparucha, Anne Salanoubat, Marcel de Berardinis, Véronique |
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Elektronische Aufsätze |
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Vergne-Vaxelaire, Carine |
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10.1007/s00253-018-9018-1 |
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characterization of a thermotolerant rok-type mannofructokinase from streptococcus mitis: application to the synthesis of phosphorylated sugars |
| title_auth |
Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars |
| abstract |
Abstract Most of the “repressor, open reading frame, kinase” (ROK) proteins already characterized so far, and exhibiting a kinase activity, take restrictedly d-glucose as substrate. By exploring the sequenced bacterial diversity, 61 ATP-dependent kinases belonging to the ROK family have been identified and experimentally assayed for the phosphorylation of hexoses. These kinases were mainly found to be thermotolerant and highly active toward d-mannose and d-fructose with notable activities toward d-tagatose. Among them, the ATP-dependent kinase from the mesophile Streptococcus mitis (named $ ScrK_{mitis} $) was biochemically characterized and its substrate spectrum further studied. This enzyme possessed impressive catalytic efficiencies toward d-mannose and d-fructose of 1.5 $ 10^{6} $ $ s^{−1} $ $ M^{−1} $ and 2.7 $ 10^{5} $ $ s^{−1} $ $ M^{−1} $, respectively, but also significant ones toward d-tagatose (3.5 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $) and the unnatural monosaccharides d-altrose (1.1 $ 10^{4} $ $ s^{−1} $ $ M^{−1} $) and d-talose (3.4 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $). Specific activities measured for all hexoses showed a high stereopreference for d- over l-series. As proof of concept, 8 hexoses were phosphorylated in moderate to good yields, some of them described for the first time like l-sorbose-5-phosphate unusually phosphorylated in position 5. Its thermotolerance, its wide pH tolerance (from 7 to 10), and temperature range (> 85% activity between 40 and 70 °C) open the way to applications in the enzymatic synthesis of monophosphorylated hexoses. © Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
| abstractGer |
Abstract Most of the “repressor, open reading frame, kinase” (ROK) proteins already characterized so far, and exhibiting a kinase activity, take restrictedly d-glucose as substrate. By exploring the sequenced bacterial diversity, 61 ATP-dependent kinases belonging to the ROK family have been identified and experimentally assayed for the phosphorylation of hexoses. These kinases were mainly found to be thermotolerant and highly active toward d-mannose and d-fructose with notable activities toward d-tagatose. Among them, the ATP-dependent kinase from the mesophile Streptococcus mitis (named $ ScrK_{mitis} $) was biochemically characterized and its substrate spectrum further studied. This enzyme possessed impressive catalytic efficiencies toward d-mannose and d-fructose of 1.5 $ 10^{6} $ $ s^{−1} $ $ M^{−1} $ and 2.7 $ 10^{5} $ $ s^{−1} $ $ M^{−1} $, respectively, but also significant ones toward d-tagatose (3.5 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $) and the unnatural monosaccharides d-altrose (1.1 $ 10^{4} $ $ s^{−1} $ $ M^{−1} $) and d-talose (3.4 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $). Specific activities measured for all hexoses showed a high stereopreference for d- over l-series. As proof of concept, 8 hexoses were phosphorylated in moderate to good yields, some of them described for the first time like l-sorbose-5-phosphate unusually phosphorylated in position 5. Its thermotolerance, its wide pH tolerance (from 7 to 10), and temperature range (> 85% activity between 40 and 70 °C) open the way to applications in the enzymatic synthesis of monophosphorylated hexoses. © Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
| abstract_unstemmed |
Abstract Most of the “repressor, open reading frame, kinase” (ROK) proteins already characterized so far, and exhibiting a kinase activity, take restrictedly d-glucose as substrate. By exploring the sequenced bacterial diversity, 61 ATP-dependent kinases belonging to the ROK family have been identified and experimentally assayed for the phosphorylation of hexoses. These kinases were mainly found to be thermotolerant and highly active toward d-mannose and d-fructose with notable activities toward d-tagatose. Among them, the ATP-dependent kinase from the mesophile Streptococcus mitis (named $ ScrK_{mitis} $) was biochemically characterized and its substrate spectrum further studied. This enzyme possessed impressive catalytic efficiencies toward d-mannose and d-fructose of 1.5 $ 10^{6} $ $ s^{−1} $ $ M^{−1} $ and 2.7 $ 10^{5} $ $ s^{−1} $ $ M^{−1} $, respectively, but also significant ones toward d-tagatose (3.5 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $) and the unnatural monosaccharides d-altrose (1.1 $ 10^{4} $ $ s^{−1} $ $ M^{−1} $) and d-talose (3.4 $ 10^{2} $ $ s^{−1} $ $ M^{−1} $). Specific activities measured for all hexoses showed a high stereopreference for d- over l-series. As proof of concept, 8 hexoses were phosphorylated in moderate to good yields, some of them described for the first time like l-sorbose-5-phosphate unusually phosphorylated in position 5. Its thermotolerance, its wide pH tolerance (from 7 to 10), and temperature range (> 85% activity between 40 and 70 °C) open the way to applications in the enzymatic synthesis of monophosphorylated hexoses. © Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
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Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars |
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| score |
7.3984175 |