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peptidase-D (proline dipeptidase, prolidase, Xaa-Pro dipeptidase, X-Pro dipeptidase, imidodipeptidase, PEPD, PRD)
Function:
- splits dipeptides with a Pro or hydroxyprolyl residue in the C-terminal position
- role in collagen metabolism because the high level of iminoacids in collagen
- hydrolysis of Xaa-|-Pro dipeptides
- also active on aminoacyl-hydroxyproline analogs
- no action on Pro-|-Pro
Cofactor: binds 2 Mn+2 per subunit (putative)
Structure:
- homodimer, mass=54251
- belongs to the peptidase M24B family, eukaryotic-type prolidase subfamily
Expression:
- upregulated 8-fold after environmental enrichment [2]
Pathology:
- defects in PEPD are a cause of prolidase deficiency
- tight linkage between the polymorphisms of prolidase & myotonic dystrophy trait
General
dipeptidase
phosphoprotein
Properties
SIZE: entity length = 493 aa
MW = 55 kD
MOTIF: Thr phosphorylation site {T188}
manganese [Mn]-binding site
SITE: 276-276
manganese [Mn]-binding site
SITE: 287-287
manganese [Mn]-binding site
SITE: 370-370
manganese [Mn]-binding site
SITE: 412-412
manganese [Mn]-binding site
SITE: 452-452
Thr phosphorylation site {T487}
Database Correlations
OMIM 170100
UniProt P12955
PFAM correlations
Entrez Gene 5184
Kegg hsa:5184
ENZYME 3.4.13.9
References
- OMIM :accession 170100
- Rampon C, Jiang CH, Dong H, Tang YP, Lockhart DJ, Schultz PG,
Tsien JZ, Hu Y.
Effects of environmental enrichment on gene expression in the
brain.
Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12880-4.
PMID: 11070096