Aminoacylase
From Proteopedia
(Difference between revisions)
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<StructureSection load='1v51' size='350' side='right' caption='Structure of D-aminoacylase with Zn+2 ions (grey) and acetate (PDB entry [[1v51]])' scene=''> | <StructureSection load='1v51' size='350' side='right' caption='Structure of D-aminoacylase with Zn+2 ions (grey) and acetate (PDB entry [[1v51]])' scene=''> | ||
| + | == Function == | ||
| - | '''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA is a zinc-assisted enzyme. | + | '''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA is a zinc-assisted enzyme. <ref>PMID:11742345</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. | ||
==3D structures of D-aminoacylase== | ==3D structures of D-aminoacylase== | ||
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[[1rk5]] - AfDAA (mutant) + Zn + Cu<br /> | [[1rk5]] - AfDAA (mutant) + Zn + Cu<br /> | ||
[[1rk6]] - AfDAA + Zn + Cd<br /> | [[1rk6]] - AfDAA + Zn + Cd<br /> | ||
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| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 11:49, 20 December 2015
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Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Joel L. Sussman, Alexander Berchansky, Jaime Prilusky
