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]
Reaction
It catalyzes the following reaction:
acetyl-CoA + beta-D-galactoside → CoA + 6-acetyl-beta-D-galactoside
The kinetics of the enzyme were delineated in 1995.[2]
Biological role
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]
See also
References
- ^ a b c Wang XG, Olsen LR, Roderick SL (April 2002). "Structure of the lac operon galactoside acetyltransferase". Structure. 10 (4): 581–8. doi:10.1016/S0969-2126(02)00741-4. PMID 11937062.
- ^ Lewendon A, Ellis J, Shaw WV (November 1995). "Structural and mechanistic studies of galactoside acetyltransferase, the Escherichia coli LacA gene product". The Journal of Biological Chemistry. 270 (44): 26326–31. doi:10.1074/jbc.270.44.26326. PMID 7592843.
- ^ Roderick SL (June 2005). "The lac operon galactoside acetyltransferase". Comptes Rendus Biologies. 328 (6): 568–75. doi:10.1016/j.crvi.2005.03.005. PMID 15950163.
- ^ "Thiogalactoside transacetylase of the lactose operon as an enzyme for detoxification". 1976.
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External links
Media related to Galactoside acetyltransferase at Wikimedia Commons- galactoside+acetyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- EC 2.3.1.18
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