β-D-Galactoside transport inEscherichia coli
نویسندگان
چکیده
منابع مشابه
Distinct expression profiles of UDP-galactose: β-D-galactoside α1,4-galactosyltransferase and UDP-galactose: β-D-galactoside β1,4-galactosyltransferase in pigeon, ostrich and chicken.
We previously identified two novel enzymes in pigeon, α1,4- and β1,4-galactosyltransferases (GalTs), which are responsible for the biosynthesis of the Galα1-4Gal and Galβ1-4Gal sequences on glycoproteins, respectively. No such glycan structures and/or enzymes have been found in mammals, suggesting that the expression of these enzymes diverged during the course of vertebrate evolution. To compar...
متن کاملMechanisms of active transport in isolated membrane vesicles. I. The site of energy coupling between D-lactic dehydrogenase and beta-galactoside transport in Escherichia coli membrane vesicles.
The results presented in this paper provide preliminary evidence for the concept that the “carriers” of the n-lactic dehydrogenase-coupled transport systems in isolated membrane vesicles from Escherichia co2i may be electron transfer intermediates. Initial rates of lactose transport and D-&iCtiC dehydrogenase activity respond identically to temperature and both processes have the same activatio...
متن کاملRegulation of galactoside transport by the PTS.
Inducer exclusion, regulation of activity of transporter, is mediated by phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). To elucidate the molecular mechanism of the inducer exclusion, numerous biochemical and genetic studies have been performed. It is now well known that non-phosphorylated IIA(Glc) inhibits the transport via direct binding to the transporter. Analysis of induc...
متن کامل3-Galactoside Transport in a Proteus mirabilis Merodiploid Carrying an Escherichia coli Lactose Operon
Merodiploid derivatives bearing an F-linked lac operon (i+, o+, z+, v+, a+) from Escherichia coli were prepared from a Proteus mirabilis strain unable to utilize lactose and from a lac deletion strain of E. coli. A suitable growth medium was found in which the episomal element in the P. mirabilis derivative was sufficiently stable to allow induction of the episome-borne lac operon and thus to p...
متن کاملLactose permease of Escherichia coli catalyzes active beta-galactoside transport in a gram-positive bacterium.
The following several lines of evidence demonstrate that lactose permease (LacY) of Escherichia coli is assembled into the cytoplasmic membrane of gram-positive Corynebacterium glutamicum, expressing the lacY gene, as a functional carrier protein. (i) LacY was detected immunologically in the cytoplasmic membrane fraction of the heterologous host. (ii) Recombinant C. glutamicum cells bearing the...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEBS Letters
سال: 1982
ISSN: 0014-5793
DOI: 10.1016/0014-5793(82)81005-3