Search results
Results From The WOW.Com Content Network
The lactose operon (lac operon) is an operon required for the transport and metabolism of lactose in E. coli and many other enteric bacteria.Although glucose is the preferred carbon source for most enteric bacteria, the lac operon allows for the effective digestion of lactose when glucose is not available through the activity of β-galactosidase. [1]
Galactoside permease is a protein coded by the lacY gene of the lac operon, and is found bound to the membrane of a cell for the purpose of binding galactoside molecules that have been solubilized. The protein is part of a system whose main function is to catalyze the accumulation and transport of lactose and other beta-galactosides across the ...
The LacY gene is a component of the lac operon that encodes lactose permease, a protein responsible for breaking down lactose into glucose and galactose, alongside transacetylase and beta galactosidase. The absence of lactose permease leads to the inability of lactose to enter the cell for further metabolic processes.
Monod joined the Pasteur Institute in 1943 and Jacob in 1949. The experimental system ultimately used by Jacob and Monod was a common bacterium, E. coli, but the basic regulatory concept (described in the Lac operon article) that was discovered by Jacob and Monod is fundamental to cellular regulation for all organisms.
Although as early as 1951, Barbara McClintock showed interaction between two genetic loci, Activator (Ac) and Dissociator (Ds), in the color formation of maize seeds, the first discovery of a gene regulation system is widely considered to be the identification in 1961 of the lac operon, discovered by François Jacob and Jacques Monod, in which ...
The lac operon of the model bacterium Escherichia coli was the first operon to be discovered and provides a typical example of operon function. It consists of three adjacent structural genes, a promoter, a terminator, and an operator. The lac operon is regulated by several factors including the availability of glucose and lactose.
The enzyme's role in the classical E.coli lac operon remains unclear. [1] [3] However, the enzyme's cellular role may be to detoxify non-metabolizable pyranosides by acetylating them and preventing their reentry into the cell. [1] [4]
The phosphoryl group on PEP is eventually transferred to the imported sugar via several proteins. The phosphoryl group is transferred to the Enzyme E I (EI), Histidine Protein (HPr, Heat-stable Protein) and Enzyme E II (EII) to a conserved histidine residue, whereas in the Enzyme E II B (EIIB) the phosphoryl group is usually transferred to a cysteine residue and rarely to a histidine.