peptidase

It is a member of the peptidase C1 family.

This protein is a member of cysteine peptidase family C19.

This enzyme is part of the papain-like peptidase C1 family.

It can be used to detect the presence of pyrrolidonyl peptidase.

This enzyme belongs to the peptidase family A1 of pepsin.

Another member of this pathway is the signal peptide peptidase.

This peptidase from trypsin family is present in seminal plasma.

Members of this family are the peptidase inhibitor madanin proteins.

This cysteine peptidase is isoloated from bacteria, plants and animals.

A family is assembled around a type example, the sequence of a well-characterized peptidase or inhibitor.

Pyrrolidonyl peptidase is an enzyme found in certain bacteria.

The eukaryotic signal peptidase is an integral membrane protein complex.

This zinc metalloendopeptidase belong to the peptidase family M12.

This secreted endopeptidase belongs to the peptidase family M10.

Gastricsin is an aspartic proteinase that belongs to the peptidase family A1.

This cytosolic peptidase that is active at neutral pH.

A tripeptidyl peptidase is a type of enzyme.

This enzyme belongs in peptidase family S53.

Dipeptidyl peptidase is a type of enzyme classified under EC 3.4.14.

The signal peptide is typically removed at the destination by a signal peptidase.

The targeting signal is usually cleaved off after successful targeting by a processing peptidase.

In the periplasm pre-prothermolysin is then processed into prothermolysin by a signal peptidase.

The vast majority of the family are endopeptidases, although there is an exopeptidase, tripeptidyl peptidase.

This peptidase is isolated from the thermophilic fungus Malbranchea pulchella.

It is thought a signal peptidase cuts at these cleavage sites to produce the proctolin peptide.