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The inducer in the lac operon is allolactose. [2] If lactose is present in the medium, then a small amount of it will be converted to allolactose by a few molecules of β-galactosidase that are present in the cell. [3] Allolactose binds to the repressor and decreases the repressor's affinity for the operator site. [3]
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]
In E. coli, the lacZ gene is the structural gene for β-galactosidase; which is present as part of the inducible system lac operon which is activated in the presence of lactose when glucose level is low. β-Galactosidase synthesis stops when glucose levels are sufficient. [2] β-Galactosidase has many homologues based on similar sequences.
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.
They discovered that the mechanism that controlled the metabolic "switching" function was a two-part control mechanism on the lac operon. When lactose is present in the cell the enzyme β-galactosidase is produced to convert lactose into glucose or galactose. When lactose is absent in the cell the lac repressor inhibits the production of the ...
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 ...
Like allolactose, IPTG binds to the lac repressor and releases the tetrameric repressor from the lac operator in an allosteric manner, thereby allowing the transcription of genes in the lac operon, such as the gene coding for beta-galactosidase, a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides.
In the absence of lactose, the constitutively expressed lac repressor protein binds to the operator region of the DNA and prevents the transcription of the operon genes. When present, lactose binds to the lac repressor, causing it to separate from the DNA and thereby enabling transcription to occur.