Aminoacylase

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== Structural highlights ==
== Structural highlights ==
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DAA contains a 2-metal Zn binding site which is mutually exclusive. DAA is activated by Zn at β site and inhibited by addition of a second Zn at the α site.
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DAA is catalytically activated by Zn+2 bound tightly at the β site and inhibited by the addition of a second weakly bound Zn+2 at the α site.
</StructureSection>
</StructureSection>
==3D structures of D-aminoacylase==
==3D structures of D-aminoacylase==

Revision as of 08:33, 21 December 2015

Structure of D-aminoacylase with Zn+2 ions (grey) and acetate (PDB entry 1v51)

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3D structures of D-aminoacylase

Updated on 21-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. ↑ 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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Michal Harel, Joel L. Sussman, Alexander Berchansky, Jaime Prilusky

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