Aminoacylase

spinqualitylabelsall models Structure of D-aminoacylase with Zn+2 ions (grey) and acetate (PDB entry 1v51) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. 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 Structural highlights AfDAA is catalytically activated by Zn+2 bound tightly at the β site and inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site. Two sites together. 3D structures of aminoacylase Aminoacylase 3D structures

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