Aminopeptidase I (IPR033818)

Short name: Aminopeptidase_I

Overlapping homologous superfamilies


Family relationships


Peptidase M18 aminopeptidase family is widely distributed in bacteria and eukaryotes, but only the yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized to date. Yeast aminopeptidase I is active only in its dodecameric form with broad substrate specificity, acting on N-terminal leucine and most other amino acids. In contrast, the mammalian aspartyl aminopeptidase is highly selective for hydrolysis of N-terminal Asp or Glu residues from peptides. These enzymes have two catalytic zinc ions at the active site [PMID: 7674922].

This entry includes aminopeptidase I (MEROPS identifier M18.001) which has been characterized from the yeast vacuole [PMID: 19185714]. The structure of the precursor has been solved and formation of a dodecamer is important for transportation from the cytoplasm to the vesicle [PMID: 26208681]. The dodecamer acts as the major cargo protein of the cytoplasm-to-vacuole targeting pathway [PMID: 8901576].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0070006 metalloaminopeptidase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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