PEPD

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This article is about human gene PEPD. For the pain disorder, see Paroxysmal extreme pain disorder.
Peptidase D
Protein PEPD PDB 2iw2.png
PDB rendering based on 2iw2.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols PEPD ; PROLIDASE
External IDs OMIM613230 MGI97542 HomoloGene239 ChEMBL: 4185 GeneCards: PEPD Gene
EC number 3.4.13.9
RNA expression pattern
PBB GE PEPD 202108 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5184 18624
Ensembl ENSG00000124299 ENSMUSG00000063931
UniProt P12955 Q11136
RefSeq (mRNA) NM_000285 NM_008820
RefSeq (protein) NP_000276 NP_032846
Location (UCSC) Chr 19:
33.88 – 34.01 Mb
Chr 7:
34.91 – 35.04 Mb
PubMed search [1] [2]

Xaa-Pro dipeptidase, also known as prolidase, is an enzyme that in humans is encoded by the PEPD gene.[1][2][3]

Xaa-Pro dipeptidase is a cytosolic dipeptidase that hydrolyzes dipeptides with proline or hydroxyproline at the carboxy terminus (but not Pro-Pro). It is important in collagen metabolism because of the high levels of imino acids.[3] Mutations at the PEPD locus cause prolidase deficiency. This is characterised by Iminodipeptidurea, Skin ulcers, mental retardation and recurrent infections.

References[edit]

  1. ^ Endo F, Tanoue A, Nakai H, Hata A, Indo Y, Titani K, Matsuda I (Apr 1989). "Primary structure and gene localization of human prolidase". J Biol Chem 264 (8): 4476–81. PMID 2925654. 
  2. ^ Tanoue A, Endo F, Matsuda I (Aug 1990). "Structural organization of the gene for human prolidase (peptidase D) and demonstration of a partial gene deletion in a patient with prolidase deficiency". J Biol Chem 265 (19): 11306–11. PMID 1972707. 
  3. ^ a b "Entrez Gene: PEPD peptidase D". 

Further reading[edit]