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
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. Coded by the gene (lacA) in the lac operon of Escherichia coli.[1] Its precise function as part of the lac operon is not understood currently.[2]

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

[edit] See also

[edit] References

  1. ^ Wang XG; Olsen LR; Roderick SL. (Apr 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. (Jun 2005). "The lac operon galactoside acetyltransferase". C R Biol. 328 (6): 568–75. 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: 26326–31.. doi:10.1074/jbc.270.44.26326. PMID 7592843. 

[edit] External links

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Transferases: acyltransferases (EC 2.3)
2.3.1: other than amino-acyl groups
(mostly acetyltransferases)
2.3.2 - Aminoacyltransferases
2.3.3 - converted into alkyl on transfer