Aminoacylase
From Proteopedia
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== 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 name="Ad">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 == | ||
| + | |||
| + | 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> <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> | 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> | </StructureSection> | ||
==3D structures of D-aminoacylase== | ==3D structures of D-aminoacylase== | ||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| + | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| + | *D-aminoacylase | ||
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| + | **[[1m7j]], [[1v51]] – AfDAA + Zn – ''Alcaligenes faecalis''<br /> | ||
| + | **[[1rjq]], [[1rjr]], [[1v4y]] - AfDAA (mutant) + Zn <br /> | ||
| + | **[[1rjp]] - AfDAA + Zn + Cu<br /> | ||
| + | **[[1rk5]] - AfDAA (mutant) + Zn + Cu<br /> | ||
| + | **[[1rk6]] - AfDAA + Zn + Cd<br /> | ||
| - | + | *L-aminoacylase or aspartoacylase | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| + | **[[1q7l]] – hLAA 1 (mutant) + Zn - human<br /> | ||
| + | **[[2i3c]], [[2o53]], [[2q51]] – hLAA 2 + Zn <br /> | ||
| + | **[[2o4h]] – hLAA 2 + Zn + methyl-aspartate<br /> | ||
| + | **[[4mri]], [[4mxu]], [[4nfr]], [[4tnu]] – hLAA 2 (mutant) + Zn + methyl-aspartate<br /> | ||
| + | **[[2q4z]], [[2gu2]] – LAA 2 + Zn - rat<br /> | ||
| + | **[[3nh4]] – mLAA 3 + Zn + Cs – mouse <br /> | ||
| + | **[[3nh3]] – mLAA 3 (mutant) + Zn <br /> | ||
| + | **[[3nfz]] – mLAA 3 (mutant) + Zn + acetyl-tyrosine<br /> | ||
| + | **[[3nh8]] – mLAA 3 (mutant) + Zn + acetyl-cysteine<br /> | ||
| + | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 08:16, 27 May 2019
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3D structures of D-aminoacylase
Updated on 27-May-2019
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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