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peptidase dimerization domain-containing protein
This domain consists of 4 beta strands and two alpha helices which make up the dimerisation surface of members of the M20 family of peptidases [1]. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification [2]. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases. [1]. 9083113. Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy. Rowsell S, Pauptit RA, Tucker AD, Melton RG, Blow DM, Brick P;. Structure 1997;5:337-347. [2]. 7674922. Evolutionary families of metallopeptidases. Rawlings ND, Barrett AJ;. Meth Enzymol 1995;248:183-228. (from Pfam)
M20/M25/M40 family metallo-hydrolase
This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification [1]. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases. [1]. 7674922. Evolutionary families of metallopeptidases. Rawlings ND, Barrett AJ;. Meth Enzymol 1995;248:183-228. (from Pfam)
dipeptidase PepV
Divalent metal ion-dependent extracellular dipeptidase; able to hydrolyze a broad range of dipeptides but no tri-, tetra-, or larger oligopeptides
Sapep family Mn(2+)-dependent dipeptidase
The founding member of this family, Sapep (Staphylococcus aureus metallopeptidase), belongs to the M20 family of metalloproteases. Homologs to this family include N-acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, as well as other peptidases.
M20 family metallopeptidase
M20 family metallopeptidase with similarity to beta-Ala-Xaa dipeptidase (PepV), an unspecific dipeptidase cleaving a variety of dipeptides, notably those with an N-terminal beta-Ala or D-Ala residue
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