Aminoacylase

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== Function ==
== Function ==
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'''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA is a zinc-assisted enzyme. <ref>PMID:11742345</ref>
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'''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA is a zinc-assisted enzyme. <ref>PMID:14736882</ref>
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== Relevance ==
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DAA which
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== Disease ==
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Mutation in DAA1 causes a dysfunctional urea cycle. Mutation in DAA2 causes Canavan's Disease,
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== Structural highlights ==
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DAA contains a Zn-binding domain and a dimerization domain.
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==3D structures of D-aminoacylase==
==3D structures of D-aminoacylase==

Revision as of 11:52, 20 December 2015

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

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Proteopedia Page Contributors and Editors (what is this?)

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

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