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Galactoside acetyltransferase (also known as Galactoside O-acetyltransferase, thiogalactoside transacetylase, β-galactoside transacetylase and GAT) is an enzyme that transfers an acetyl group from acetyl-CoA to β-galactosides, glucosides and lactosides. It is coded for by the lacA gene of the lac operon in E. coli. [1]
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]
It is encoded by the lacY gene in the lac operon. 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.
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 ...
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.
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