Anti-Maltose Binding Protein antibody [EPR4744]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Maltose Binding Protein often referred to as MBP is a periplasmic protein that plays an important role in the transportation of maltose and maltodextrins in E. coli. It binds to maltose with high specificity facilitating its uptake into the bacterial cell. The MBP protein size is approximately 42 kDa which allows it to effectively interact with its ligands. Scientists often use MBP as a fusion partner in protein purification processes due to its solubility and ability to enhance the expression of recombinant proteins.

Biological function summary

Within the cell it functions by ensuring the effective transport of sugars across the bacterial membrane. Since MBP is not typically a part of a larger complex it acts more as an individual unit facilitating the binding of its target sugars. This binding and transport mechanism is vital for the bacterial carbohydrate metabolism supporting the overall energy balance within the microorganism.

Pathways

This protein is integral to the maltose/maltodextrin transport system which is a part of the larger phosphotransferase system. Its role in these pathways is closely associated with other proteins such as the Maltose ABC transporter proteins which form a transport mechanism across the bacterial inner membrane. Additionally MBP has a functional relationship with the enzymes in the glycolysis pathway as the transported sugars eventually feed into this energy-producing route.

Associated diseases and disorders

Maltose binding protein itself is not a direct causative factor. However understanding MBP can assist in researching bacterial infections caused by pathogenic strains like E. coli where maltose metabolism is important for survival and virulence. Moreover disruptions in sugar transport pathways involving proteins like MBP can contribute to metabolic imbalances. Although MBP is not directly implicated in human diseases analyzing its function can aid in developing therapeutic approaches targeting sugar transport systems in harmful bacteria.