| Type: | Domain | Name: | D-aminoacylase, insert domain |
| Description: | D-aminoacylase (, ) hydrolyses a wide variety of N-acyl derivatives of neutral D-amino acids, in a zinc-dependent manner. The enzyme is composed of a small beta-barrel domain and a larger catalytic alpha/beta-barrel that contains a short alpha/beta insert. The overall structure shares significant similarity to the alpha/beta-barrel amidohydrolase superfamily, in which the beta-strands in both barrels superimpose well []. This entry represents the insert found in the catalytic domain. This insert, composed of two alpha helices and four beta strands, goes across the active site and is involved in substrate-mediated conformational change. | Short Name: | D-aminoacylase_insert_dom |
