PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 244384-1 1977 Purification of the first dipeptidases, glycylleucine dipeptidase (EC 3.4.13.2) and proline dipeptidase (EC 3.4.13.9), from intestine, have shown them to be true dipeptidases, hydrolysing only dipeptides in their laevo form. Dipeptides 193-203 peptidase D Homo sapiens 84-103 6743286-10 1984 At concentrations of the dipeptide that saturated prolidase, hydrolysis of glycyl-L-proline by whole cells was approximately 130 times slower than by lysates. Dipeptides 25-34 peptidase D Homo sapiens 50-59 6429439-1 1984 Skin fibroblasts have a single enzyme, Mn2+-activated prolidase, that hydrolyses a range of amino acid-proline dipeptides. Dipeptides 111-121 peptidase D Homo sapiens 54-63 27482243-2 2016 The prolidase enzyme is a cytosolic exopeptidase that detaches proline or hydroxyproline from the carboxyl terminal position of dipeptides. Dipeptides 128-138 peptidase D Homo sapiens 4-13 33045291-1 2021 Prolidase is a metal-dependent peptidase specialized in the cleavage of dipeptides containing proline or hydroxyproline on their C-termini. Dipeptides 72-82 peptidase D Homo sapiens 0-9 32598484-1 2020 Prolidase catalyzes the cleavage of dipeptides containing proline on their C-terminus. Dipeptides 36-46 peptidase D Homo sapiens 0-9 27067078-1 2017 The enzyme prolidase cleaves dipeptides where the C-terminal amino acid corresponds to proline or hydroxyproline. Dipeptides 29-39 peptidase D Homo sapiens 11-20 25460580-3 2015 In humans, prolidase is the only enzyme able to hydrolyze dipeptides containing these amino acids at their C-terminal end, thus being a key player in collagen synthesis and turnover. Dipeptides 58-68 peptidase D Homo sapiens 11-20 27546702-1 2016 Prolidase (EC.3.4.13.9) or proline dipeptidase, is one of the unique enzyme capable of degrading dipeptides, in which a proline or hydroxyproline residue is located at the C-terminal position. Dipeptides 97-107 peptidase D Homo sapiens 0-9 27546702-1 2016 Prolidase (EC.3.4.13.9) or proline dipeptidase, is one of the unique enzyme capable of degrading dipeptides, in which a proline or hydroxyproline residue is located at the C-terminal position. Dipeptides 97-107 peptidase D Homo sapiens 27-46 23212918-1 2013 Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus. Dipeptides 129-139 peptidase D Homo sapiens 0-9 24566305-5 2014 The hydrolysis of imidazole-related dipeptides in prokaryotes and eukaryotes is also catalyzed by aminoacyl-histidine dipeptidases like PepD (EC 3.4.13.3), PepV (EC 3.4.13.19) and anserinase (EC 3.4.13.5). Dipeptides 36-46 peptidase D Homo sapiens 136-140 23212918-1 2013 Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus. Dipeptides 129-139 peptidase D Homo sapiens 25-44 23212918-1 2013 Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus. Dipeptides 129-139 peptidase D Homo sapiens 48-59 23212918-1 2013 Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus. Dipeptides 129-139 peptidase D Homo sapiens 61-65 23430876-2 2012 Prolidase is a ubiquitous enzyme that hydrolyses dipeptides with C-terminal proline or hydroxyproline residues and indeed, lack of this enzyme activity causes massive urine excretion of undigested iminodipeptides. Dipeptides 49-59 peptidase D Homo sapiens 0-9 21699887-1 2011 BACKGROUND: Prolidase is a metallo-exopeptidase hydrolyzing X-Pro and X-Hyp dipeptides. Dipeptides 76-86 peptidase D Homo sapiens 12-21 18806117-16 2008 Prolidase catalyzes hydrolysis of dipeptide or oligopeptide with a C-terminal proline or hydroxyproline and its deficiency can cause mental retardation and severe skin ulcers. Dipeptides 34-43 peptidase D Homo sapiens 0-9 20674353-2 2010 Proline prodrug of methotrexate (Pro-MTX) was designed as a substrate of prolidase which is specific for imido bond of dipeptide containing proline and expected to penetrate MDA-MB-231 cells more efficiently. Dipeptides 119-128 peptidase D Homo sapiens 73-82 19426854-2 2009 Prolidase specifically hydrolyzes dipeptides with a prolyl residue in the carboxy terminus (NH(2)-X-/-Pro-COOH). Dipeptides 34-44 peptidase D Homo sapiens 0-9 19288447-2 2009 The enzyme prolidase plays an important role in the breakdown of collagen and the breakdown of intracellular protein especially in the final stage when peptides and dipeptides contain a high level of proline. Dipeptides 165-175 peptidase D Homo sapiens 11-20 15804176-0 2005 Prolidase, a potential enzyme target for melanoma: design of proline-containing dipeptide-like prodrugs. Dipeptides 80-89 peptidase D Homo sapiens 0-9 15878628-1 2005 Prolidase deficiency (PD) is a recessive disorder of the connective tissue caused by mutations in the prolidase, a specific peptidase, cleaving the dipeptides with a C-terminal prolyl and hydroxyprolyl residue. Dipeptides 148-158 peptidase D Homo sapiens 102-111 15804176-2 2005 The analyses indicated that prolidase might be a desirable enzyme target based on its differential expression in melanoma cancer cell lines and its high substrate specificity for dipeptides containing proline at the carboxy terminus. Dipeptides 179-189 peptidase D Homo sapiens 28-37 11451388-1 2001 Prolidase [EC 3.4.13.9] is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline-containing dipeptides. Dipeptides 134-144 peptidase D Homo sapiens 0-9 15142336-6 2004 The microparticulate drug delivery system described carried small amounts of active prolidase inside fibroblasts, ensuring a response to the intracellular accumulation of X-Pro dipeptides, the mechanism that is supposed to be responsible for the development of clinical manifestations of this disorder in man. Dipeptides 177-187 peptidase D Homo sapiens 84-93 11451388-1 2001 Prolidase [EC 3.4.13.9] is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline-containing dipeptides. Dipeptides 134-144 peptidase D Homo sapiens 54-70 1437403-2 1992 The enzyme prolidase hydrolyzes dipeptides containing C-terminal proline or hydroxyproline. Dipeptides 32-42 peptidase D Homo sapiens 11-20 9619859-1 1998 Prolidase (EC 3.4.13.9) is an ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of dipeptides containing C-terminal proline or hydroxyproline. Dipeptides 105-115 peptidase D Homo sapiens 0-9 9879669-1 1998 Prolidase [E.C.3.4.13.9] is a cytosolic exopeptidase that catalyses the hydrolysis of C-terminal proline containing dipeptides or tripeptides. Dipeptides 116-126 peptidase D Homo sapiens 0-9 9328822-1 1997 Prolidase (EC 3.4.13.9) is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline or hydroxyproline containing dipeptides. Dipeptides 152-162 peptidase D Homo sapiens 0-9 8821003-5 1995 In addition, both the transporter and the prolidase activities affected the overall transport of Phe when given as the dipeptide Phe-Pro, supporting the notion that intestinal absorption of peptides is an essential component of amino acid absorption. Dipeptides 119-128 peptidase D Homo sapiens 42-51 1437403-5 1992 Our results indicate that prolidase plays a major role in the recycling of dipeptide-bound proline. Dipeptides 75-84 peptidase D Homo sapiens 26-35 1545347-2 1992 The enzymatic hydrolysis by prolidase of substrates for the peptide transporter L-alpha-methyldopa-pro and several dipeptide analogues without an N-terminal alpha-amino group (phenylpropionylproline, phenylacetylproline, N-benzoylproline, and N-acetylproline) was investigated. Dipeptides 115-124 peptidase D Homo sapiens 28-37 1545347-5 1992 These results demonstrate that prolidase may serve as a prodrug-converting enzyme for the dipeptide-type prodrugs, utilizing the peptide carrier for transport of prodrugs into the mucosal cells and prolidase, a cytosolic enzyme, to release the drug. Dipeptides 90-99 peptidase D Homo sapiens 31-40 1545347-5 1992 These results demonstrate that prolidase may serve as a prodrug-converting enzyme for the dipeptide-type prodrugs, utilizing the peptide carrier for transport of prodrugs into the mucosal cells and prolidase, a cytosolic enzyme, to release the drug. Dipeptides 90-99 peptidase D Homo sapiens 198-207 3139928-1 1988 A 17-year-old girl was shown to have prolidase deficiency on the basis of the presence of large amounts of proline-containing dipeptides in urine and an almost complete absence of prolidase in plasma and erythrocytes. Dipeptides 126-136 peptidase D Homo sapiens 37-46 2246245-1 1990 Catalytic pH dependence for the hydrolytic activity of the enzyme prolidase with a series of dipeptide substrates is found to be generally bell-shaped (kcat/Km) or simple sigmoidal (kcat). Dipeptides 93-102 peptidase D Homo sapiens 66-75 3436060-4 1987 When the protein environment was restored, isolated prolidase I was reactivated by preincubation, and as a result, gly-pro procollagen dipeptide became the best substrate. Dipeptides 135-144 peptidase D Homo sapiens 52-61