InterPro domain: IPR036038

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped [ 1 ] into subfamilies.

The D-amino acid transferases (D-AAT) are required by bacteria to catalyse the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids [ 2 , 3 ].

D-aminoacid aminotransferase is a homo hexamer with D3 symmetry, folded into two domains [ 4 ]. The first one has a beta3-alpha2-beta2 fold, while the second one has an alpha/beta fold.

1. Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme. J. Bacteriol. 174, 5317-23
2. Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity. Biochemistry 34, 9661-9
3. Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution. J. Biochem. 121, 637-41