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The lac operon galactoside acetyltransferase.

Steven L Roderick¹

¹Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA. roderick@aecom.yu.edu

Comptes Rendus Biologies

|June 14, 2005

Summary

The biological role of galactoside acetyltransferase (LacA, GAT) is uncertain. Recent studies reveal its mechanism and superfamily membership, confirming it as a CoA-dependent acetyltransferase.

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Area of Science:

Biochemistry
Molecular Biology
Enzymology

Background:

The lac operon encodes three structural genes, with LacA (galactoside acetyltransferase, GAT) being the least understood.
The precise biological function of GAT has remained a subject of scientific inquiry.

Purpose of the Study:

To review the historical identification and characterization of GAT.
To present recent findings on the chemical mechanism and evolutionary relationships of GAT.

Main Methods:

Literature review of classical and recent studies on GAT.
Analysis of structural and sequence similarities within the acyltransferase superfamily.

Main Results:

GAT is confirmed as a CoA-dependent acetyltransferase.
GAT exhibits specificity for the 6-hydroxyl group of certain pyranosides.
GAT belongs to a large superfamily of structurally related acyltransferases.

Conclusions:

While GAT's catalytic mechanism and superfamily are elucidated, its natural substrate(s) remain unidentified.
Further research is needed to determine the in vivo function of GAT.

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