Sugar Transport
Year: 1973
Type: article
Abstract: A phosphotransferasesystem was isolated from Sfaphylococcus aureus.The system catalyzed the transfer of a phosphoryl group from phosphoenolpyruvate to /3-galactosides to yield the corresponding galactoside 6-phosphate esters.This transfer required the participation of four protein components: Enzyme I; two phosphocarrier proteins, HPr and Factor III'"";and Enzyme II'"'.These components have been separated from one another and subjected to purification procedures.The partial purification and characterization of Enzyme I and membrane-bound Enzyme II are described.The purification of HPr to homogeneity, its characterization, and a comparison of its properties to those of the analogous HPr of Escherichia co2i are presented.Early studies on the transport and met.abolism of sugars in the gram-positive organism Siaphylococcus aureus (1) showed that all of the sugars tested (including lactose and other disaccharides) were accumulated by the cells as derivatives.These were later identified as the respective phosphate esters (2); lactose, for example, was accumulated as lactose-P in which the phosphoryl group was attached at C-6 of the galactose moiety.The discovery of a phosphoenolpyruvate-dependent sugar phosphotransferase system in S. aureus provided an esplanation for the accumulation of carbohydrates as phosphate esters in this
Source: Journal of Biological Chemistry
Language: English
Subfield: Genetics
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1585454356