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Biotechnological applications of recombinant microbial prolidases.
- Source :
-
Advances in applied microbiology [Adv Appl Microbiol] 2009; Vol. 68, pp. 99-132. - Publication Year :
- 2009
-
Abstract
- Prolidase is a metallopeptidase that is ubiquitous in nature and has been isolated from mammals, bacteria and archaea. Prolidase specifically hydrolyzes dipeptides with a prolyl residue in the carboxy terminus (NH(2)-X-/-Pro-COOH). Currently, the only solved structure of prolidase is from the hyperthermophilic archaeon Pyrococcus furiosus. This enzyme is of particular interest because it can be used in many biotechnological applications. Prolidase is able to degrade toxic organophosphorus (OP) compounds, namely, by cleaving the P-F and P-O bonds in the nerve agents, sarin and soman. Applications using prolidase to detoxify OP nerve agents include its incorporation into fire-fighting foams and as biosensors for OP compound detection. Prolidases are also employed in the cheese-ripening process to improve cheese taste and texture. In humans, prolidase deficiency (PD) is a rare autosomal recessive disorder that affects the connective tissue. Symptoms of PD include skin lesions, mental retardation and recurrent respiratory infections. Enzyme replacement therapies are currently being studied in an effort to optimize enzyme delivery and stability for this application. Previously, prolidase has been linked to collagen metabolism and more recently is being associated with melanoma. Increased prolidase activity in melanoma cell lines has lead investigators to create cancer prodrugs targeting this enzyme. Thus, there are many biotechnological applications using recombinant and native forms of prolidase and this review will describe the biochemical and structural properties of prolidases as well as discuss their most current applications.
- Subjects :
- Amino Acid Sequence
Animals
Dipeptidases chemistry
Dipeptidases deficiency
Dipeptidases genetics
Food Microbiology
Humans
Melanoma therapy
Models, Molecular
Molecular Sequence Data
Organophosphorus Compounds metabolism
Pyrococcus enzymology
Pyrococcus genetics
Recombinant Proteins chemistry
Recombinant Proteins genetics
Biotechnology methods
Dipeptidases metabolism
Recombinant Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0065-2164
- Volume :
- 68
- Database :
- MEDLINE
- Journal :
- Advances in applied microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 19426854
- Full Text :
- https://doi.org/10.1016/S0065-2164(09)01203-9