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CATH Superfamily 2.20.25.160

The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was: waiting to be named.

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 1: Aspartoacylase

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Aspartoacylase. [EC: 3.5.1.15]
N-acyl-L-aspartate + H(2)O = a carboxylate + L-aspartate.
    		 23 A0A158SIQ9 A0A158SIQ9 A0A480ZHD4 A0A480ZHD4 A8KB34 B1PK17 B1PK17 H2QBW4 H2QBW4 H2QBW4
    (13 more...)
    N-acyl-aromatic-L-amino acid amidohydrolase. [EC: 3.5.1.114]
    (1) An N-acyl-aromatic-L-amino acid + H(2)O = an aromatic-L-amino acid + a carboxylate. (2) An N-acetyl-L-cysteine-S-conjugate + H(2)O = an L-cysteine-S- conjugate + acetate.
    • This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
    • It preferentially deacetylates N(alpha)-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14.
    • Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114.
    • Cf. EC 3.5.1.14 and EC 3.5.1.15.
    		 7 A0A024R5L2 A0A024R5L2 Q5BJ91 Q5M876 Q91XE4 Q96HD9 Q96HD9
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