PEPD
PEPD (peptidase D) is a dipeptidase that hydrolyses dipeptides with a prolyl or hydroxyprolyl residue at the C-terminus. Also known as Xaa-Pro dipeptidase or prolidase, it contributes to proline recycling and collagen metabolism. Browse Assay Genie's current range of PEPD research reagents below, or read on for the biology behind the target.
PEPD is a dipeptidase that catalyses the hydrolysis of dipeptides carrying a prolyl (Xaa-Pro) or hydroxyprolyl residue in the C-terminal position. The preferred substrate is Gly-Pro, but other Xaa-Pro dipeptides, including Ala-Pro, Met-Pro, Phe-Pro, Val-Pro and Leu-Pro, can also be cleaved. NCBI Gene describes the active protein as a homodimer that hydrolyses dipeptides or tripeptides with C-terminal proline or hydroxyproline.
Because collagen contains a high level of iminoacids, the enzyme plays an important role in collagen metabolism. It serves in the recycling of proline and may be rate limiting for collagen production. The PEPD gene encodes a member of the peptidase family; the protein belongs to the peptidase M24B family, eukaryotic-type prolidase subfamily, and HGNC places the gene in the M24 metallopeptidase family. Multiple transcript variants encoding different isoforms have been reported for this gene.
Mutations in the PEPD gene result in prolidase deficiency, which is characterised by the excretion of large amounts of di- and tri-peptides containing proline. This makes the enzyme a useful subject for studies of proline recycling, collagen turnover and inherited metabolic disease. Mouse and rat orthologs, both named Pepd, allow these questions to be investigated in common model organisms.
PEPD acts on imidodipeptides arising from collagen, which is rich in iminoacids, and may be rate limiting for collagen production.
The enzyme releases proline from dipeptides and tripeptides with C-terminal proline or hydroxyproline, supporting proline recycling.
Mutations in PEPD cause prolidase deficiency, marked by excretion of large amounts of proline-containing di- and tri-peptides.
As an Xaa-Pro dipeptidase with a preference for Gly-Pro, PEPD is a model for studying substrate specificity in the M24B peptidase family.
PEPD is a dipeptidase that hydrolyses dipeptides with a prolyl or hydroxyprolyl residue at the C-terminus, preferring Gly-Pro. It contributes to proline recycling and collagen metabolism, and may be rate limiting for collagen production. Check the datasheet of any product for its validated reactivity.
The HGNC name is peptidase D, and UniProt calls the protein Xaa-Pro dipeptidase; it is also referred to as prolidase. NCBI Gene reports multiple transcript variants encoding different isoforms. The active enzyme is described as a homodimer.
Mutations in the PEPD gene cause prolidase deficiency, characterised by excretion of large amounts of proline-containing di- and tri-peptides. Orthologs named Pepd are present in both mouse and rat, so rodent models can be used to study the enzyme.
Other peptidases and proline- and collagen-metabolism targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P12955; product specifications from Assay Genie datasheets.