The number of genes encoding for a methionine aminopeptidase varies between organisms.

Dipeptidyl aminopeptidase 3 appears to be involved in the release of the merozoites from the erythrocyte.

There is at least one M1 family aminopeptidase in the genome (PfA-M1).

Glutamyl aminopeptidase has also recently been designated CD249 (cluster of differentiation 249).

Under vegetative conditions it delivers hydrolases, such as aminopeptidase 1 (Ape1), to the vacuole.

Kallidin is a decapeptide that can be converted to bradykinin by the aminopeptidase enzyme.

The methionine residue can be further removed by the enzyme methionine aminopeptidase.

Dipeptidyl aminopeptidase 1 is found in the digestive vacuole and is also an essential gene.

Leucyl aminopeptidase (LAP) is a member of the M17 family.

Fumagillin can block blood vessel formation by binding to an enzyme called methionine aminopeptidase 2.

Mature AM is metabolised via aminopeptidase action.

One important aminopeptidase is a zinc-dependent enzyme produced and secreted by glands of the small intestine.

It is an alanyl aminopeptidase.

(Contrast with an aminopeptidase, which cleaves peptide bonds at the other end of the protein.)

Before aminopeptidase can remove the N-terminal methionine, it must be deformylated by peptide deformylase.

Cystinyl aminopeptidase has been shown to interact with TNKS2.

Some advanced studies have shown a high homology between the Aminopeptidase N and the Angiotensin-converting enzyme.

Tryptophan aminopeptidase may refer to:

LAP-A is the first plant aminopeptidase shown to have a regulatory role in signal transduction pathway.

Other names in common use include tryptophan aminopeptidase, and L-tryptophan aminopeptidase.

This protein is an aminopeptidase, which is an enzyme that cleaves other proteins into smaller fragments called peptides.

Pyroglutamate aminopeptidase may be used to cleave the cyclical lactam and will therefore leave the next amino acid with a free N-terminal.

The enzyme pyroglutamate aminopeptidase can restore a free N-terminus by cleaving off the pyroglutamate residue.

The C9ORF3 aminopeptidase enzyme contains the following domains:

Leucine aminopeptidase, (left) a little like carboxypeptidase A, chops off certain amino acids one-by-one from one end of a protein or peptide.