Family

Peptidase M1, aminopeptidase B (IPR015571)

Short name: Pept_M1_aminopeptidase-B

Family relationships

Description

Over 50 metallopeptidase families have been identified to date. In these enzymes, a divalent cation, usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidases, two metal ions are observed in crystal structures ligated by five amino acids, with one amino acid ligating both metal ions. The known metal ligands are His, Glu, Asp or Lys and at least one other residue is required for catalysis, which may play an electrophillic role. Many metalloproteases contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site [PMID: 7674922]. The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break the helical structure adopted by this motif in metalloproteases [PMID: 7674922].

This group of metallopeptidases belong to the MEROPS peptidase family M1 (clan MA(E)), the type example being aminopeptidase N from Homo sapiens (Human). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA.

This entry contains aminopeptidase B from eukaryotes.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0004177 aminopeptidase activity
GO:0008270 zinc ion binding

Cellular Component

GO:0005615 extracellular space

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PANTHER