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>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> |
== Structural highlights == | == Structural highlights == | ||
| - | AfDAA is catalytically activated by Zn<sup>+2</sup> <scene name='57/570615/Cv/2'>bound tightly at the β site</scene> and <scene name='57/570615/Cv/3'>inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site</scene>. <scene name='57/570615/Cv/4'>Two sites together</scene>. | + | AfDAA is catalytically activated by Zn<sup>+2</sup> <scene name='57/570615/Cv/2'>bound tightly at the β site</scene> and <scene name='57/570615/Cv/3'>inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site</scene>. <scene name='57/570615/Cv/4'>Two sites together</scene>.<ref name="Ad">PMID:14736882</ref> |
</StructureSection> | </StructureSection> | ||
==3D structures of D-aminoacylase== | ==3D structures of D-aminoacylase== | ||
Revision as of 13:54, 27 December 2015
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3D structures of D-aminoacylase
Updated on 27-December-2015
1m7j, 1v51 – AfDAA + Zn – Alcaligenes faecalis
1rjq, 1rjr, 1v4y - AfDAA (mutant) + Zn
1rjp - AfDAA + Zn + Cu
1rk5 - AfDAA (mutant) + Zn + Cu
1rk6 - AfDAA + Zn + Cd
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
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