Related Experiment Video
Updated: Aug 14, 2026

In vitro Investigation of the MexAB Efflux Pump From Pseudomonas aeruginosa
Published on: February 17, 2014
Characteristics of the melibiose transporter and its primary structure in Enterobacter aerogenes
N Okazaki1, M Kuroda, T Shimamoto
1Department of Microbiology, Faculty of Pharmaceutical Sciences, Okayama University, Tsushima, Japan.
Abstract:
Cells of Enterobacter aerogenes can grow on melibiose as a sole source of carbon. This suggests the presence of melibiose operon in this organism. We found that E. aerogenes cells possess both alpha-galactosidase activity and melibiose transport activity, which were induced by melibiose. Neither Na+ nor Li+ stimulated the melibiose transport. However, transport of methyl-beta-thiogalactoside (TMG) was stimulated by Li+ but not by Na+. These findings suggest that the major coupling cation for the melibiose transporter in E. aerogenes is H+. In fact, we observed H+ entry into cells caused by an influx of melibiose and some of its analogs. We cloned the melB gene which encodes the melibiose transporter, and sequenced it. Deduced amino acid sequence of the transporter revealed that the melibiose transporter consists of 471 amino acid residues and the molecular weight was calculated to be 52214 Da. The sequence showed high homology with the sequences of the melibiose transporters of Escherichia coli, Salmonella typhimurium and Klebsiella pneumoniae. Higher homology was found with the melibiose transporter of K. pneumoniae than with that of E. coli and S. typhimurium.
Related Concept Videos
The Significance of Membrane Transport
Transporters facilitate either an active or passive movement of solutes. They can allow a single-molecule transport down its...
ABC Transporters: Exporter
ABC Transporters: Importer
In bacteria, based on the number of transmembrane helices and the chemical nature of their substrates, the ABC importers can be divided into three types:
Insertion of Single-pass Transmembrane Proteins in the RER
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Multi-pass Transmembrane Proteins and β-barrels
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Structure of Porins

