Function
D-aminoacylase (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA was found in different genera of bacteria: Pseudomonas, Streptomyces and Alcaligenes. Each genera has a different substrate preference. DAA from Alcaligenes faecalis (AfDAA) shows preference for D-Met, D-Phe and D-Leu and lesser effectivity for D-Trp, D-Ala and D-val. AfDAA is a zinc-assisted enzyme. [1]L-aminoacylase (LAA) or aspartoacylase hydrolyzes N-acyl-L-amino acid to L-amino acid and carboxylate.
Disease
Mutations in LAA1 are characterized by accumulation of N-acetyl amino acids in the urine and cause seizures, delay of psychomotor development and moderate mental retardation[2]
Structural highlights
AfDAA is catalytically activated by Zn+2 and . .[1]
3D structures of aminoacylase
Aminoacylase 3D structures