Aminoacylase
From Proteopedia
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| - | <StructureSection load='1v51' size='350' side='right' caption='Structure of D-aminoacylase with Zn+2 ions (grey) and acetate (PDB entry [[1v51]])' scene=''> | + | <StructureSection load='1v51' size='350' side='right' caption='Structure of D-aminoacylase with Zn+2 ions (grey) and acetate (PDB entry [[1v51]])' scene='57/570615/Cv/1'> |
== Function == | == 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. <ref>PMID:14736882</ref> | + | '''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. <ref name="Ad">PMID:14736882</ref>'''L-aminoacylase''' (LAA) or '''aspartoacylase''' hydrolyzes N-acyl-L-amino acid to L-amino acid and carboxylate. |
| + | == Disease == | ||
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| + | 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<ref>PMID:21414403</ref> | ||
== Structural highlights == | == Structural highlights == | ||
| - | AfDAA is catalytically activated by Zn<sup>+2</sup> bound tightly at the β site and inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site. | + | AfDAA is catalytically activated by Zn<sup>+2</sup> <scene name='57/570615/Cv/5'>bound tightly at the β site</scene> and <scene name='57/570615/Cv/6'>inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site</scene>. <scene name='57/570615/Cv/7'>Two sites together</scene>.<ref name="Ad">PMID:14736882</ref> |
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| - | + | ==3D structures of aminoacylase== | |
| + | [[Aminoacylase 3D structures]] | ||
| - | + | </StructureSection> | |
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== References == | == References == | ||
Current revision
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References
- ↑ 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
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