Aminoacylase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 6: Line 6:
== 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>.<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>
</StructureSection>
</StructureSection>
==3D structures of D-aminoacylase==
==3D structures of D-aminoacylase==

Revision as of 10:05, 20 February 2019

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

Drag the structure with the mouse to rotate

3D structures of D-aminoacylase

Updated on 20-February-2019

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. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman, Alexander Berchansky, Jaime Prilusky

Retrieved from "http://52.214.119.220/wiki/index.php/Aminoacylase"
Personal tools