Beta-galactoside transacetylase

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GAT in complex with CoA and two molecules/active site of IPTG viewed perpendicular to the molecular threefold axis of the enzyme

β-galactoside transacetylase is an enzyme that transfers an acetyl group from acetyl-CoA to β-galactosides, and is coded by a gene (lacA) in the lac operon of E. coli.[1] Its precise function as part of the lac operon is not understood currently.[2]

The kinetics of the enzyme were delineated in 1995.[3]

The enzyme's cellular role may be to detoxify non-metabolizable pyranosides by acetylating them and preventing their reentry into the cell.[4]

See also[edit]

References[edit]

  1. ^ 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. 
  2. ^ Roderick SL. (June 2005). "The lac operon galactoside acetyltransferase". C R Biol. 328 (6): 568–75. doi:10.1016/j.crvi.2005.03.005. PMID 15950163. 
  3. ^ A. Lewendon; J. Ellis; W.V. Shaw (1995). "Structural and Mechanistic Studies of Galactoside Acetyltransferase, the Escherichia coli LacA Gene Product". J. Biol. Chem. 270 (44): 26326–31. doi:10.1074/jbc.270.44.26326. PMID 7592843. 
  4. ^ Wang, XG; Olsen, LR; Roderick, SL (2002). "Structure of the lac operon galactoside acetyltransferase". Structure. 10 (4): 581–8. doi:10.1016/S0969-2126(02)00741-4. PMID 11937062. 

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