Departments | |
---|---|
Book Series (92) |
1308
|
Humanities |
2293
|
Natural Sciences |
5354
|
Mathematics | 224 |
Informatics | 313 |
Physics | 975 |
Chemistry | 1354 |
Geosciences | 131 |
Human medicine | 242 |
Stomatology | 10 |
Veterinary medicine | 99 |
Pharmacy | 147 |
Biology | 830 |
Biochemistry, molecular biology, gene technology | 117 |
Biophysics | 25 |
Domestic and nutritional science | 44 |
Agricultural science | 996 |
Forest science | 201 |
Horticultural science | 20 |
Environmental research, ecology and landscape conservation | 145 |
Engineering |
1746
|
Common |
91
|
Leitlinien Unfallchirurgie
5. Auflage bestellen |
Formylglycine generation, a unique process necessary for the activation of sulfatases, is a cotranslational event conserved from pro- to eukaryotes and is defined by the modification of the cysteine residue in the CxPxR motif of largely unfolded sulfatase polypeptides to Cα-formylglycine (FGly). This process is confined to the endoplasmic reticulum (ER) in eukaryotes and catalyzed by the formylglycine-generating enzyme (FGE), a resident protein of the ER. Mutations in FGE, that impair FGly generation, lead to production of inactive sulfatases that manifests into an inherited metabolic disorder termed multiple sulfatase deficiency (MSD) in humans. Although FGE has been proposed to function as a cofactor independent monooxygenase, the precise mechanism is not yet clear. In the present study, a baculovirus-based method for expression and purification of recombinant FGE from cultured insect cells was established and the recombinant FGE was characterized in more detail.
ISBN-13 (Hard Copy) | 9783736991101 |
ISBN-13 (eBook) | 9783736981102 |
Language | English |
Page Number | 158 |
Lamination of Cover | glossy |
Edition | 1. Aufl. |
Publication Place | Göttingen |
Place of Dissertation | Göttingen |
Publication Date | 2015-09-21 |
General Categorization | Dissertation |
Departments |
Biochemistry, molecular biology, gene technology
|
Keywords | Formylglycine generation enzyme, Multiple sulfatase deficiency, in vitro activity |