The intramembrane topography of the mannitol-specific enzyme II of the Escherichia coli phosphotransferase system

Autor:	Deborah R. Finlay, Gary R. Jacobson, Dori M. Kelly
Rok vydání:	1983
Předmět:	chemistry.chemical_classification Permease Cell Biology PEP group translocation Biology medicine.disease_cause Biochemistry Cell membrane medicine.anatomical_structure Enzyme Membrane protein chemistry Cytoplasm medicine Phosphorylation Molecular Biology Escherichia coli
Zdroj:	Journal of Biological Chemistry. 258:2955-2959
ISSN:	0021-9258
DOI:	10.1016/s0021-9258(18)32813-8
Popis:	The D-mannitol-specific Enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli is an integral cytoplasmic membrane protein responsible for concomitant transport and phosphorylation of this hexitol. We have investigated the intramembrane topography of this enzyme/permease using proteases, membrane-impermeable reagents, and antibodies against the purified protein. The results of these experiments suggest that this protein spans the membrane in a single orientation with a sizeable proportion of its mass extending into the cytoplasm, but with little of the polypeptide exposed at the outside surface of the membrane. Such an orientation is consistent with the reception and transport roles of the mannitol Enzyme II in E. coli.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::790d4b844b566ae75de6e76e7cf1f937 https://doi.org/10.1016/s0021-9258(18)32813-8 Zobrazit plný text záznamu