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Key Documents

P6675

Sigma-Aldrich

Prolidase from porcine kidney

lyophilized powder, ≥100 units/mg protein

Synonym(s):

Aminoacyl-L-proline hydrolase, Imido Dipeptidase, Prolidase, Proline dipeptidase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

Quality Level

specific activity

≥100 units/mg protein

composition

Protein, 20-74% Lowry

storage temp.

−20°C

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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.

Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard 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)

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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
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)
Isolation and partial characterization of an antibacterial substance produced by Enterococcus faecium
Pantev A, et al.
Folia Microbiologica, 47(4), 391-400 (2002)
Ewa Karna et al.
Molecular and cellular biochemistry, 361(1-2), 235-241 (2011-10-14)
Products of prolidase [E.C. 3.4.13.9] activity, proline or hydroxyproline, contribute to up-regulation of hypoxia-inducible factor-1α (HIF-1α). Prolidase activity is regulated by β(1)-integrin signaling. We studied the effects of echistatin (a well-known disintegrin) and thrombin (a serine protease capable of activation
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

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