P6675
Prolidase from porcine kidney
lyophilized powder, ≥100 units/mg protein
Synonym(s):
Aminoacyl-L-proline hydrolase, Imido Dipeptidase, Prolidase, Proline dipeptidase
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
form
lyophilized powder
specific activity
≥100 units/mg protein
composition
Protein, 20-74% Lowry
storage temp.
−20°C
Looking for similar products? Visit Product Comparison Guide
Related Categories
General description
Prolidase is a cytosolic exopeptidase. It is a homodimeric enzyme which requires divalent cations like manganese as a cofactor in its active site for its function.
Application
Prolidase from porcine kidney has been used:
- in the enzymatic hydrolysis of porcine milk for the recovery of L-glutamine from proteins and peptides
- in the proteolysis of skim milk for the determination of ε-(γ-glutamyl)lysine and free aminoacids
- to determine its effect on the activity of enterococcin A 2000
Prolidase has an important role in recycling of proline and collagen production. It is used to study mutations in the PEPD gene that cause prolidase deficiency. It is used to hydrolyze proteins with C-terminal proline or hydroxyproline residues. Prolidase, product P6675 from porcine kidney, has been used to hydrolyze peptide bonds from the amino terminus when studying enzymatic methylation of membrane proteins.
Biochem/physiol Actions
Prolidase is an enzyme that catalyzes the hydrolysis of the imide bond between an α-carboxyl group and proline or hydroxyproline. The protein forms a homodimer that hydrolyzes dipeptides or tripeptides with C-terminal proline or hydroxyproline residues.
Rare mutation in prolidase gene causes deficiency leading to massive imidodipeptiduria, elevated proline-containing dipeptides in plasma, recurrent infections, mental retardation and skin lesions.
Unit Definition
One unit will hydrolyze 1.0 μmole of Gly-Pro per min at pH 8.0 at 40 °C.
Physical form
Supplied as a lyophilized powder containing Tris buffer salt and MnCl2.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Mehmet A Altay et al.
Scandinavian journal of clinical and laboratory investigation, 71(7), 576-582 (2011-08-13)
We aimed to investigate serum prolidase activity and to find out its association with oxidative-antioxidative status in patients with idiopathic clubfoot and during the course of the disease. Oxidative status parameters, including total free sulfhydryl groups (-SH), total antioxidant capacity
Isolation and partial characterization of an antibacterial substance produced by Enterococcus faecium
Pantev A, et al.
Folia Microbiologica, 47(4), 391-400 (2002)
Influence of transglutaminase treatment of skim milk on the formation of varepsilon-(Γ-glutamyl) lysine and the susceptibility of individual proteins towards crosslinking
Sharma R, et al.
International dairy journal, 11(10), 785-793 (2001)
Marta E Alberto et al.
Inorganic chemistry, 50(8), 3394-3403 (2011-03-24)
The catalytic hydrolysis of the Gly-Pro substrate by the bimetallic prolidase active site model cluster has been investigated at the DF/B3LYP level of theory, in order to provide fundamental insights into the still poorly understood mechanism of prolidase catalysis. To
Jian An Chen et al.
Biochimica et biophysica acta, 1814(12), 1677-1685 (2011-08-31)
Allosteric behavior and substrate inhibition are unique characteristics of Lactococcus lactis prolidase. We hypothesized that charged residues (Asp36, His38, Glu39, and Arg40), present on one loop essential for catalysis, interact with residues in or near the active site to impart
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service