peptidase-D (proline dipeptidase, prolidase, Xaa-Pro dipeptidase, X-Pro dipeptidase, imidodipeptidase, PEPD, PRD)
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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
More general terms
References
- ↑ OMIM https://mirror.omim.org/entry/170100
- ↑ 2.0 2.1 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: https://www.ncbi.nlm.nih.gov/pubmed/11070096