Shop : Details
Shop
Details
Léa Chuzel
Application of functional metagenomics to the field of glycobiology
Bacteria account for ~15% of the earth’s biomass and are the second largest biomass contributor after plants. Bacteria are ubiquitous and have adapted to live in all habitable ecosystems on our planet resulting in a vast diversity estimated to be 1 trillion different species. The genomes of these microbes represent an extraordinary resource for novel enzyme discovery. The field of metagenomics strives to access these genomes, in particular, those from uncultivable species that have been otherwise out of reach.
Glycobiology is a field of research that addresses the structure, function, and biology of glycans and glycoconjugates. Glycans have wide-ranging importance in both basic biology and pharmaceutical science. In this thesis work a functional metagenomic workflow that relies upon large-insert metagenomic libraries created in Escherichia coli was established. A collection of almost 100,000 clones was created from diverse ecosystems including extreme environments, and is estimated to contain 3-4 million of environmental genes. Three activity-based screens were executed using libraries in this collection. The first led to identification of a novel exosialidase having a unique catalytic mechanism and new protein structure that defined a new glycoside hydrolase family (GH156). The second screen isolated two sialidases with a preference for a non-human form of sialic acid. Finally, a third screen identified two enzymatic activities: a sugar-specific sulfatase and a sulfate-dependent hexosaminidase that can act on sulfated glycans, an important chemical modification of N-glycans for which well-defined analytical tools have yet to be established.
Glycobiology is a field of research that addresses the structure, function, and biology of glycans and glycoconjugates. Glycans have wide-ranging importance in both basic biology and pharmaceutical science. In this thesis work a functional metagenomic workflow that relies upon large-insert metagenomic libraries created in Escherichia coli was established. A collection of almost 100,000 clones was created from diverse ecosystems including extreme environments, and is estimated to contain 3-4 million of environmental genes. Three activity-based screens were executed using libraries in this collection. The first led to identification of a novel exosialidase having a unique catalytic mechanism and new protein structure that defined a new glycoside hydrolase family (GH156). The second screen isolated two sialidases with a preference for a non-human form of sialic acid. Finally, a third screen identified two enzymatic activities: a sugar-specific sulfatase and a sulfate-dependent hexosaminidase that can act on sulfated glycans, an important chemical modification of N-glycans for which well-defined analytical tools have yet to be established.
Schlagwörter: functional metagenomics; glycobiology; sialidase; sulfatase; glycoside hydrolase; enzyme discovery; screening
Forschungsberichte aus dem Max-Planck-Institut für Dynamik komplexer technischer Systeme
Herausgegeben von Prof. Dr. Peter Benner, Prof. Dr.-Ing. Udo Reichl, Prof. Dr.-Ing. Andreas Seidel-Morgenstern und Prof. Dr.-Ing. Kai Sundmacher, Magdeburg
Band 55
Verfügbare Online-Dokumente zu diesem Titel
DOI 10.2370/9783844084375
Sie benötigen den Adobe Reader, um diese Dateien ansehen zu können. Hier erhalten Sie eine kleine Hilfe und Informationen, zum Download der PDF-Dateien.
Bitte beachten Sie, dass die Online-Dokumente nicht ausdruckbar und nicht editierbar sind.
Bitte beachten Sie auch weitere Informationen unter: Hilfe und Informationen.
Bitte beachten Sie auch weitere Informationen unter: Hilfe und Informationen.
| Dokument |  | Gesamtdokument | ||
| Dateiart |  | |||
| Kosten |  | 37,35 € | ||
| Aktion |  | Zahlungspflichtig kaufen und anzeigen der Datei - 5,4 MB | ||
| Aktion |  | Zahlungspflichtig kaufen und download der Datei - 5,4 MB | ||
| Dokument |  | Inhaltsverzeichnis | ||
| Dateiart | | |||
| Kosten |  | frei | ||
| Aktion |  | Anzeigen der Datei - 252 kB | ||
| Aktion |  | Download der Datei - 252 kB | ||
Benutzereinstellungen für registrierte Online-Kunden (Online-Dokumente)
Sie können hier Ihre Adressdaten ändern sowie bereits georderte Dokumente erneut aufrufen.
Benutzer
Nicht angemeldet
Export bibliographischer Daten
Shaker Verlag GmbHAm Langen Graben 15a52353 Düren
Mo. - Do. 8:00 Uhr bis 16:00 UhrFr. 8:00 Uhr bis 15:00 Uhr
Kontaktieren Sie uns. Wir helfen Ihnen gerne weiter.
