Studies on the enzymatic synthesis of optically pure tertiary alcohols: Biocatalysis and Protein Design
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Studies on the enzymatic synthesis of optically pure tertiary alcohols (2009)
DE PB NW RPISBN: 9783639193510 bzw. 3639193512, in Deutsch, Vdm Verlag Sep 2009, Taschenbuch, neu, Nachdruck.
Von Händler/Antiquariat, AHA-BUCH GmbH [51283250], Einbeck, NDS, Germany.
This item is printed on demand - Print on Demand Titel. - This books deals with a catalytic platform for the enzymatic synthesis of tertiary alcohols. A certain class of hydrolases bearing the GGG(A)X-motif are efficient and highly selective catalysts for this difficult reaction. The number of available biocatalysts could be extended by making use of a structure-guided screening in metagenome-derived enzyme libraries. Two highly selective enzymes were identified. One model enzyme, esterase BS2, was optimized and the hydrolysis of tertiary esters was studied in detail. In a protein design study, novel enzyme variants were generated by semi-rational protein design methods, which led to the identification of mutants with strongly increased or even inverse enantioselectivity. The application of the platform to the kinetic resolution of a building block of pharmaceutical interest is described. 76 pp. Englisch.
This item is printed on demand - Print on Demand Titel. - This books deals with a catalytic platform for the enzymatic synthesis of tertiary alcohols. A certain class of hydrolases bearing the GGG(A)X-motif are efficient and highly selective catalysts for this difficult reaction. The number of available biocatalysts could be extended by making use of a structure-guided screening in metagenome-derived enzyme libraries. Two highly selective enzymes were identified. One model enzyme, esterase BS2, was optimized and the hydrolysis of tertiary esters was studied in detail. In a protein design study, novel enzyme variants were generated by semi-rational protein design methods, which led to the identification of mutants with strongly increased or even inverse enantioselectivity. The application of the platform to the kinetic resolution of a building block of pharmaceutical interest is described. 76 pp. Englisch.
2
Symbolbild
Studies on the enzymatic synthesis of optically pure tertiary alcohols (2009)
DE PB NW RPISBN: 9783639193510 bzw. 3639193512, in Deutsch, VDM Verlag Sep 2009, Taschenbuch, neu, Nachdruck.
Von Händler/Antiquariat, AHA-BUCH GmbH [51283250], Einbeck, Germany.
This item is printed on demand - Print on Demand Titel. Neuware - This books deals with a catalytic platform for the enzymatic synthesis of tertiary alcohols. A certain class of hydrolases bearing the GGG(A)X-motif are efficient and highly selective catalysts for this difficult reaction. The number of available biocatalysts could be extended by making use of a structure-guided screening in metagenome-derived enzyme libraries. Two highly selective enzymes were identified. One model enzyme, esterase BS2, was optimized and the hydrolysis of tertiary esters was studied in detail. In a protein design study, novel enzyme variants were generated by semi-rational protein design methods, which led to the identification of mutants with strongly increased or even inverse enantioselectivity. The application of the platform to the kinetic resolution of a building block of pharmaceutical interest is described. 76 pp. Englisch.
This item is printed on demand - Print on Demand Titel. Neuware - This books deals with a catalytic platform for the enzymatic synthesis of tertiary alcohols. A certain class of hydrolases bearing the GGG(A)X-motif are efficient and highly selective catalysts for this difficult reaction. The number of available biocatalysts could be extended by making use of a structure-guided screening in metagenome-derived enzyme libraries. Two highly selective enzymes were identified. One model enzyme, esterase BS2, was optimized and the hydrolysis of tertiary esters was studied in detail. In a protein design study, novel enzyme variants were generated by semi-rational protein design methods, which led to the identification of mutants with strongly increased or even inverse enantioselectivity. The application of the platform to the kinetic resolution of a building block of pharmaceutical interest is described. 76 pp. Englisch.
3
Studies on the enzymatic synthesis of optically pure tertiary alcohols
DE PB NWISBN: 9783639193510 bzw. 3639193512, in Deutsch, Vdm Verlag Dr. Müller, Taschenbuch, neu.
Lieferung aus: Deutschland, Versandkostenfrei.
buecher.de GmbH & Co. KG, [1].
This books deals with a catalytic platform for the enzymatic synthesis of tertiary alcohols. A certain class of hydrolases bearing the GGG(A)X-motif are efficient and highly selective catalysts for this difficult reaction. The number of available biocatalysts could be extended by making use of a structure-guided screening in metagenome-derived enzyme libraries. Two highly selective enzymes were identified. One model enzyme, esterase BS2, was optimized and the hydrolysis of tertiary esters was studied in detail. In a protein design study, novel enzyme variants were generated by semi-rational protein design methods, which led to the identification of mutants with strongly increased or even inverse enantioselectivity. The application of the platform to the kinetic resolution of a building block of pharmaceutical interest is described.2009. 76 S.Versandfertig in 3-5 Tagen, Softcover.
buecher.de GmbH & Co. KG, [1].
This books deals with a catalytic platform for the enzymatic synthesis of tertiary alcohols. A certain class of hydrolases bearing the GGG(A)X-motif are efficient and highly selective catalysts for this difficult reaction. The number of available biocatalysts could be extended by making use of a structure-guided screening in metagenome-derived enzyme libraries. Two highly selective enzymes were identified. One model enzyme, esterase BS2, was optimized and the hydrolysis of tertiary esters was studied in detail. In a protein design study, novel enzyme variants were generated by semi-rational protein design methods, which led to the identification of mutants with strongly increased or even inverse enantioselectivity. The application of the platform to the kinetic resolution of a building block of pharmaceutical interest is described.2009. 76 S.Versandfertig in 3-5 Tagen, Softcover.
4
Symbolbild
Studies on the enzymatic synthesis of optically pure tertiary alcohols (2009)
DE PB NW RPISBN: 9783639193510 bzw. 3639193512, in Deutsch, VDM Verlag Dr. Müller, Saarbrücken, Deutschland, Taschenbuch, neu, Nachdruck.
Von Händler/Antiquariat, English-Book-Service - A Fine Choice [1048135], Waldshut-Tiengen, BW, Germany.
This item is printed on demand for shipment within 3 working days.
This item is printed on demand for shipment within 3 working days.
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Studies on the enzymatic synthe (2009)
~EN PB NWISBN: 9783639193510 bzw. 3639193512, vermutlich in Englisch, VDM Verlag Dr. Müller, Saarbrücken, Deutschland, Taschenbuch, neu.
Lieferung aus: Deutschland, Next Day, Versandkostenfrei.
Die Beschreibung dieses Angebotes ist von geringer Qualität oder in einer Fremdsprache. Trotzdem anzeigen
Die Beschreibung dieses Angebotes ist von geringer Qualität oder in einer Fremdsprache. Trotzdem anzeigen
6
Studies on the enzymatic synthesis of optically pure tertiary alcohols
DE NWISBN: 9783639193510 bzw. 3639193512, in Deutsch, VDM Verlag Dr. Müller, Saarbrücken, Deutschland, neu.
Lieferung aus: Deutschland, zzgl. Versandkosten, Sofort lieferbar.
Biocatalysis and Protein Design, Biocatalysis and Protein Design.
Biocatalysis and Protein Design, Biocatalysis and Protein Design.
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