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peptidase D
Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen. Defects in PEPD are a cause of prolidase deficiency (PD). Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait. Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
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| Protein type: EC 3.4.13.9; Protease |
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Molecular Function: dipeptidase activity; manganese ion binding; aminopeptidase activity; metallocarboxypeptidase activity
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Biological Process: amino acid metabolic process; collagen catabolic process; proteolysis
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Reference #:
P12955 (UniProtKB)
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| Alt. Names/Synonyms: aminoacyl-L-proline hydrolase; Imidodipeptidase; MGC10905; PEPD; Peptidase D; PRD; Prolidase; Proline dipeptidase; X-Pro dipeptidase; Xaa-Pro dipeptidase |
| Gene Symbols: PEPD |
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Molecular weight: 54,548 Da
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Basal Isoelectric point: 5.64
Predict pI for various phosphorylation states
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