Aminoacylase
From Proteopedia
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== 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/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>. |
</StructureSection> | </StructureSection> | ||
==3D structures of D-aminoacylase== | ==3D structures of D-aminoacylase== | ||
Revision as of 13:51, 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
- ↑ 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
