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Cell envelope proteins involved in the transport of maltose and sn-glycerol-3-phosphate in Escherichia coli

✍ Scribed by Winfried Boos

Publisher
John Wiley and Sons
Year
1976
Tongue
English
Weight
1003 KB
Volume
89
Category
Article
ISSN
0021-9541

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✦ Synopsis

Abstract

Two types of proteins are discussed in their role of facilitating the transport of maltose and sn‐glycerol‐3‐phosphate in E. coli. The first protein is the receptor for phage δ, known to be an outer membrane protein. By facilitating the diffusion of maltose and the higher maltodextrins through the outer membrane the effect of the δ receptor is to decrease the K~m~ of the transport system without influencing the V~max~ of substrate flux.

The second protein is a periplasmic protein that is induced by growth on glycerol and is essential for transport of sn‐glycerol‐3‐phosphate in whole cells but not in membrane vesicles. This protein has solely been identified by the use of a two‐dimensional polyacrylamide gel electrophoresis of periplasmic proteins in wild‐type and mutants defective in sn‐glycerol‐3‐phosphate transport.

📜 SIMILAR VOLUMES

Characterization of a periplasmic protei
Characterization of a periplasmic protein related to sn-glycerol-3-phosphate transport in escherichia coli
✍ Argast, Manfred ;Schumacher, Güunter ;Boos, Winfried 📂 Article 📅 1977 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 1004 KB

## Abstract The cold osmotic shock procedure releases a protein (GLPT) from the cell envelope of Escherichia coli that is related to the transport of sn‐glycerol‐3‐phosphate in this organism. The evidence for this correlation is as follows: (1) GLPT is under the regulatory control of the glpR gene.

Carbon-starvation induction of the ugp o
Carbon-starvation induction of the ugp operon, encoding the binding protein-dependent sn-glycerol-3-phosphate transport system in Escherichia coli
✍ Su, Ti-Zhi ;Schweizer, Herbert P. ;Oxender, Dale L. 📂 Article 📅 1991 🏛 Springer 🌐 English ⚖ 464 KB

The gene products of the ugp operon of Escherichia coli are responsible for the uptake of sn-glycerol-3-phosphate and certain glycerophosphodiesters. The regulation of ugp is mainly phoBR-dependent. Significant expression, however, can be observed even in the presence of high concentrations of phosp