Estrogen synthetase (aromatase). The cytochrome P-450 component of the human placental enzyme is a glycoprotein
| Autor: | N. Rao Thotakura, Kandan Sethumadhavan, Francis L. Bellino |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Glycosylation
Cytochrome medicine.drug_class Placenta Carbohydrates Biochemistry Endoglycosidase Substrate Specificity Aromatase Endocrinology Cytochrome P-450 Enzyme System Pregnancy Concanavalin A medicine Humans Testosterone Molecular Biology Glycoproteins chemistry.chemical_classification biology Androstenedione Cytochrome P450 Molecular biology Molecular Weight Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Enzyme chemistry Estrogen biology.protein Microsome Female Glycoprotein Protein Processing Post-Translational |
| Zdroj: | Molecular and Cellular Endocrinology. 78:25-32 |
| ISSN: | 0303-7207 |
| DOI: | 10.1016/0303-7207(91)90182-r |
| Popis: | Estrogen synthetase (aromatase) is a cytochrome P-450 enzyme system which converts androgens to estrogens. Although this enzyme has been purified and the cDNA-derived amino acid sequence elucidated, very little is known regarding post-translational modifications of this physiologically crucial enzyme. We show here that the cytochrome P-450 component, P-450ES, purified from human term placental microsomes, is a glycoprotein based on the following evidence: its molecular weight is decreased following treatment with endoglycosidase F, concanavalin A-biotin specifically binds to this protein immobilized on nitrocellulose, and its oligosaccharide composition is consistent with a single N-linked fucosylated complex type carbohydrate chain. In a reconstitution system, the aromatase activity using the endoglycosidase F-treated P-450ES was reduced by about 35–40% relative to the native form, regardless of whether androstenedione or testosterone was used as substrate. |
| Databáze: | OpenAIRE |
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