Prolidase Enzyme From Porcine Kidney

What is Prolidase?

Proteases are enzymes responsible for breaking down proteins into smaller peptides and amino acids. Prolidase is a unique protease which precisely breaks down certain di- or tri-peptides. More specifically, prolidase only acts on peptides containing proline or hydroxyproline amino acids at the C-terminal position.  Because proline has a unique structure, most other protease enzymes do not recognize this amino acid. Rather, the highly specific prolidase, also known as proline dipeptidase, is uniquely able to recognize proline’s conformation and fulfill its function.

Prolidase three-dimensional structure
Prolidase Protein Structure. Emw, CC BY-SA 3.0 , via Wikimedia Commons

This enzyme is found both in eukaryotes and prokaryotes. It  contains some highly similar, or conserved, active regions of the protein among all organisms.  Located within the inner cell matrix, prolidase plays key functions within all types of cells.

What is Role of prolidase?

 Functionally, prolidase  plays a key role in the recycling of proline. As a result, it is vital for synthesis and breakdown of collagen within the body.  Specifically, collagen is an important structural protein which makes up about 30 percent of the body’s total protein.

In order for its hydrolyzing activity to work at its peak, this enzyme requires the presence of a  divalent metal like manganese. This metal serves as a “helper molecule”, or a co-factor to assist and speed up the chemical reaction between the enzyme and the peptide. Because of its need for a metal, prolidase is classified as a metallopeptidase. 

An excellent review article detailing the structure and functions of prolidase can be found here.
 

Prolidase is often isolated and purified  from porcine kidneys but plays a role in all types of cells. As a result, porcine kidney prolidase is used for diverse research including the following examples:

Prolidase has been used to study specific hydrolysis of proteins or peptides in milk and other protein sources with C-terminal proline or hydroxyproline amino acid residues. Furthermore, it has been used to hydrolyze peptide bonds in the study of methylation of membrane proteins. 

Prolidase Enzyme from Porcine Kidney- Now Available Direct!

For over 15 years our chief scientist, Dr. Randy Meyer,  has been manufacturing and supplying quality prolidase to companies such as Sigma Aldrich. Now we are pleased to also offer our prolidase directly to individual researchers.  Offering the same quality you’ve come to expect at attractive, manufacturer-direct prices. 

IntegriZyme, LLC  isolates and purifies prolidase enzyme from porcine kidney in the U.S. from U.S.-sourced animals. 

It is available for purchase in 250 unit and 1000 unit vials. We also have larger quantities available and can custom package in sizes to fit your needs.  Please inquire.  

Prolidase Specification (CAS 9025-32-5; EC 3.4.13.9)

Activity

≥ 100 units/ mg protein
Unit Definition: One unit will hydrolyze 1.0 μmole of Gly-Pro per min at pH 8.0 at 40 °C.

Protein Content

40-80% protein (Lowry)

Form

Off-white/tan lyophilized solid containing tris buffer salts and MnCl2

Storage

-20C

For research, laboratory. and manufacturing use only. Not for drug or other use.