Aminoacylase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | 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. | + | DAA 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+2 at the α site. |
</StructureSection> | </StructureSection> | ||
==3D structures of D-aminoacylase== | ==3D structures of D-aminoacylase== | ||
Revision as of 08:43, 21 December 2015
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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
- ↑ 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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