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CATH Superfamily 3.60.20.40

Gamma-glutamyltranspeptidase, small (S) subunit

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: Gamma-glutamyltranspeptidase 1

There are 3 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
Glutathione gamma-glutamate hydrolase. [EC: 3.4.19.13]
(1) Glutathione + H(2)O = L-cysteinylglycine + L-glutamate. (2) A glutathione-S-conjugate + H(2)O = an (L-cysteinylglycine)-S- conjugate + L-glutamate.
  • This is a bifunctional protein that also has the activity of EC 2.3.2.2.
  • The enzyme binds its substrate by forming an initial gamma-glutamyl- enzyme intermediate, releasing the L-cysteinylglycine part of the molecule.
  • The enzyme then reacts with either a water molecule or a different acceptor substrate (usually an L-amino acid or a dipeptide) to form L-glutamate or a product containing a new gamma-glutamyl isopeptide bond, respectively.
  • The enzyme acts on glutathione, glutathione-S-conjugates, and, at a lower level, on other substrates with an N-terminal L-gamma-glutamyl residue.
  • It plays a crucial part in the glutathione-mediated xenobiotic detoxification pathway.
  • The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide.
 29 A0A140VJJ9 A0A140VJJ9 A6NGU5 A7A1I0 A7A1I0 A7A1I0 A7A1I0 C7GVU0 C7GVU0 C7GVU0
(19 more...)
Gamma-glutamyltransferase. [EC: 2.3.2.2]
A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.
  • The mammlian enzyme is part of the cell antioxidant defense mechanism.
  • It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels.
  • The protein also has EC 3.4.19.13 activity.
  • The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide.
  • The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions.
 29 A0A140VJJ9 A0A140VJJ9 A6NGU5 A7A1I0 A7A1I0 A7A1I0 A7A1I0 C7GVU0 C7GVU0 C7GVU0
(19 more...)
Leukotriene-C(4) hydrolase. [EC: 3.4.19.14]
Leukotriene C(4) + H(2)O = leukotriene D(4) + L-glutamate.
  • The mouse enzyme is specific for leukotriene C(4), while the human enzyme also has considerable activity toward glutathione and oxidized glutathione (cf. EC 3.4.19.13).
 10 A0A140VJJ9 A0A140VJJ9 P07314 P19440 P19440 P20735 Q4FK56 Q4FK56 Q60928 Q60928
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