CATH Classification

Domain Context

CATH Clusters

Superfamily Zn peptidases
Functional Family cytosol aminopeptidase

Enzyme Information
Prolyl aminopeptidase.
based on mapping to UniProt P00727
Release of N-terminal proline from a peptide.
-!- Present in the cytosol of mammalian and microbial cells. -!- In contrast to the mammalian form, the bacterial form of the enzyme hydrolyzes both polyproline and prolyl-2-naphthylamide. -!- The mammalian enzyme, which is not specific for prolyl bonds, is possibly identical with EC -!- Belongs to peptidase family S33. -!- Formerly EC
Leucyl aminopeptidase.
based on mapping to UniProt P00727
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
-!- Is activated by heavy metal ions. -!- Belongs to peptidase family M17. -!- Formerly EC

UniProtKB Entries (1)

Bos taurus
Cytosol aminopeptidase

PDB Structure

External Links
Primary Citation
Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography.
Kim, H., Lipscomb, W.N.