Aminoacylase
FunctionD-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. DiseaseMutations 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 highlightsAfDAA is catalytically activated by Zn+2 and . .[1] 3D structures of aminoacylase
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ReferencesReferences
- ↑ 1.0 1.1 Lai WL, Chou LY, Ting CY, Kirby R, Tsai YC, Wang AH, Liaw SH. The functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuation. J Biol Chem. 2004 Apr 2;279(14):13962-7. Epub 2004 Jan 21. PMID:14736882 doi:http://dx.doi.org/10.1074/jbc.M308849200
- ↑ Sommer A, Christensen E, Schwenger S, Seul R, Haas D, Olbrich H, Omran H, Sass JO. The molecular basis of aminoacylase 1 deficiency. Biochim Biophys Acta. 2011 Jun;1812(6):685-90. doi: 10.1016/j.bbadis.2011.03.005., Epub 2011 Mar 23. PMID:21414403 doi:10.1016/j.bbadis.2011.03.005