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CATH Superfamily 3.40.630.10

Zn peptidases

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Zn peptidases
".

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 34812: Cytosolic nonspecific dipeptidase, putative

There are 6 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
Succinyl-diaminopimelate desuccinylase. [EC: 3.5.1.18]
N-succinyl-LL-2,6-diaminoheptanedioate + H(2)O = succinate + LL-2,6- diaminoheptanedioate.
    		 138 A0A045I6E5 A0A045I6E5 A0A0D6IT50 A0A0D6IT50 A0A0E9DWJ6 A0A0E9DWJ6 A0A0E9G110 A0A0E9G110 A0A0F0LW91 A0A0F0LW91
    (128 more...)
    Cytosol nonspecific dipeptidase. [EC: 3.4.13.18]
    Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.
    • Broad specificity, varying somewhat with source species.
    • Activated and stabilized by dithiothreitol and manganese.
    • Inhibited by bestatin and leucine.
    • Belongs to peptidase family M20.
    • Formerly EC 3.4.3.1, EC 3.4.3.2, EC 3.4.3.3, EC 3.4.3.6, EC 3.4.13.1, EC 3.4.13.2, EC 3.4.13.3, EC 3.4.13.8, EC 3.4.13.11, EC 3.4.13.13 and EC 3.4.13.15.
    		 98 A0A023BC59 A0A023BC59 A0A080N659 A0A080N659 A0A084FU98 A0A084FU98 A0A086ZJI1 A0A086ZJI1 A0A086ZXU2 A0A086ZXU2
    (88 more...)
    Beta-Ala-His dipeptidase. [EC: 3.4.13.20]
    Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine.
    • Present in the serum of humans and higher primates, but not in the serum of other mammals.
    • Activated by Cd(2+) and citrate.
    • Belongs to peptidase family M20.
    • Formerly EC 3.4.3.3, EC 3.4.13.3 and EC 3.4.13.13.
    		 92 A0A084FU98 A0A084FU98 A0A086Z133 A0A086Z133 A0A087C8M4 A0A087C8M4 A0A087DZE1 A0A087DZE1 A0A0A1GM90 A0A0A1GM90
    (82 more...)
    Acetylornithine deacetylase. [EC: 3.5.1.16]
    N(2)-acetyl-L-ornithine + H(2)O = acetate + L-ornithine.
    • Also hydrolyzes N-acetylmethionine.
    		 70 A0A045I6E5 A0A045I6E5 A0A0H3LBZ5 A0A0H3LBZ5 A0A0H3M8W7 A0A0H3M8W7 A0A0H3P715 A0A0H3P715 A0A0K2HZC5 A0A0K2HZC5
    (60 more...)
    N-acyl-aliphatic-L-amino acid amidohydrolase. [EC: 3.5.1.14]
    (1) An N-acyl-aliphatic-L-amino acid + H(2)O = an aliphatic L-amino acid + a carboxylate. (2) An N-acetyl-L-cysteine-S-conjugate + H(2)O = an L-cysteine-S- conjugate + acetate.
    • The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
    • It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-alpha-amino acids.
    • Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114.
    • Cf. EC 3.5.1.15 and EC 3.5.1.114.
    		 16 A0A0B7FPD0 A0A0B7FPD0 A0A160P5F1 A0A160P5F1 A0A1J0UVG4 A0A1J0UVG4 B0D4S6 B0D4S6 C6X4S1 C6X4S1
    (6 more...)
    Xaa-methyl-His dipeptidase. [EC: 3.4.13.5]
    Hydrolysis of anserine (beta-alanyl-|-N(pi)-methyl-L-histidine), carnosine, homocarnosine, glycyl-|-leucine and other dipeptides with broad specificity.
    • Identical with acetylhistidine deacetylase.
    • Formerly EC 3.4.3.4 and EC 3.5.1.34.
    		 4 A4F1S8 A4F1S8 Q3LHN4 Q3LHN4
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