3.4.21.26 alpa2-antiplasmin + H2O not a robust substrate in vitro, the enzyme cleaves after Pro12 in the T9S10G11P12-N13 Q14E15Q16E17 sequence 3.4.21.26 alpha-melanocyte-stimulating hormone + H2O - 3.4.21.26 alpha-synuclein + H2O - 3.4.21.26 alpha-synulein + H2O the enzyme binds to alpha-synuclein and enhances its dimerization 3.4.21.26 angiotensin I + H2O - 3.4.21.26 angiotensin II + H2O - 3.4.21.26 arginine-vasopressin + H2O - 3.4.21.26 beta-amyloid + H2O - 3.4.21.26 beta-endorphin + H2O - 3.4.21.26 bradykinin + H2O - 3.4.21.26 bradykinin potentiating peptide + H2O - 3.4.21.26 casein + H2O - 3.4.21.26 Collagen + H2O - 3.4.21.26 Collagen + H2O the pathogen POP degrades host collagen and fibronectin, facilitating cell invasion, selective inhibitors for trypanosome POP block parasite entry into cells 3.4.21.26 collagens + H2O in host extracellular matrix 3.4.21.26 Fibronectin + H2O in host extracellular matrix 3.4.21.26 Fibronectin + H2O the pathogen POP degrades host collagen and fibronectin, facilitating cell invasion, selective inhibitors for trypanosome POP block parasite entry into cells 3.4.21.26 fish muscle collagen + H2O the enzyme hydrolysis site is at the carboxyl terminus of prolyl residues 3.4.21.26 gliadins + H2O in host gut 3.4.21.26 gluten + H2O - 3.4.21.26 gluten + H2O activity in the human host gastrointestinal tract, overview 3.4.21.26 gluten + H2O degradation of gluten in the human host's intestinal tract, i.e. stomach, duodenum, jejunum, and ileum 3.4.21.26 gluten peptide + H2O - 3.4.21.26 gluten peptides + H2O activity in the human host gastrointestinal tract, overview 3.4.21.26 gluten peptides + H2O degradation of gluten peptides in the human host's intestinal tract, i.e. stomach, duodenum, jejunum, and ileum 3.4.21.26 gonadotropin releasing hormone + H2O - 3.4.21.26 Luliberin + H2O - 3.4.21.26 LVVYPWTQRF + H2O prolyl endopeptidase activity could be the first step of the degradation of LVV-hemorphin-7 3.4.21.26 melanotropin + H2O - 3.4.21.26 membrane-associated glycoprotein neural cell adhesion molecule + H2O - 3.4.21.26 additional information the enzyme plays a role in the metabolism of proline-containing neuropeptides which have been suggested to be involved in learning and memory processes 3.4.21.26 additional information the specificity for post-proline bonds suggests that the enzyme may play a central role in the hydrolysis of casein-derived bitter peptides, such as beta-casein(f193-209) 3.4.21.26 additional information tissue-dependent peptide hydrolysis evoked by prolyl endopeptidase activity is involved in the water-electrolyte homeostasis 3.4.21.26 additional information enzyme regulation, overview 3.4.21.26 additional information cellular functions, overview 3.4.21.26 additional information cellular functions, overview, POP may regulate phosphoinositide signaling, overview 3.4.21.26 additional information cellular functions, overview, POP may regulate phosphoinositide signaling, overview, the enzyme is involved in Alzheimer's disease with enzyme inhibition leading to a reduction of beta-amyloid peptide, overview 3.4.21.26 additional information cellular functions, overview, POP may regulate phosphoinositide signaling, overview, the enzyme is involved in neuronal degeneration and Alzheimer's disease with enzyme inhibition leading to a reduction of beta-amyloid peptide, overview 3.4.21.26 additional information enzyme inhibition leads to inhibition of lithium effects, the loss of enzyme activity evokes a 4fold increase in the inositol-3-phosphate concentration counteracting the Li+ ions, enzyme regulation, overview 3.4.21.26 additional information enzyme inhibitors are able to prevent the in vitro invasion of rodent muscle cells by trypomastigotes 3.4.21.26 additional information POP activity levels are lowered in different stages of depression, whereas activity is increased in patients with mania and schizophrenia, the antidepressant fluoxetine and the antimanic drug valproic acid both restore POP activity to normal levels 3.4.21.26 additional information the enzyme in the brain dopaminergix system is involved in the pathogenesis of doamine deficiency-dependent depressive states, and is activated in association with development of MPTP-induced depressive syndrome in the brain frontal cortex, overview 3.4.21.26 additional information the enzyme induces cleavage of gluten-derived peptides predigested by pepsin and pancreatic enzymes an exhibiting a detoxifying effect in the host's gut 3.4.21.26 additional information the enzyme is a proline-specific endopeptidase with a serine-type mechanism 3.4.21.26 additional information the enzyme is a serine protease, that digests small peptide-like hormones, neuroactive peptides, and various cellular factors, it is implicated in several biological processes and diseases, e.g. in some psychiatric disorders, most probably through interference in the inositol cycle, it is important in the metabolism of substance P, arginine vasopressin, thyroliberin, and gonadoliberin, enzyme regulation probably involving gluten, prep expression is downregulated in coelic disease patients in complete remission, overview 3.4.21.26 additional information the enzyme is a serine protease, that digests small peptide-like hormones, neuroactive peptides, and various cellular factors, it is implicated in several biological processes and diseases, e.g. in some psychiatric disorders, most probably through interference in the inositol cycle, it is important in the metabolism of substance P, arginine vasopressin, thyroliberin, and gonadoliberin, enzyme regulation, overview 3.4.21.26 additional information the enzyme is associated with cognitive functions and inositol 1,4,5-triphosphate signaling, and plays a role in modifying neuropeptide levels, overview 3.4.21.26 additional information the enzyme is involved in the phosphoinositide pathway, in formation and processing of amyloid beta-peptide, protein secretion, and in neuronal differentiation and maturation, overview, the enzyme is involved in several diseases, e.g. celiac disease, Alzheimer's diease, Parkinsons's disease, affective disorders, eating disorders, cancer, inflammation, hypertension, and neurodegenarative disorders, overview, enzyme inhibition can improve the retention time when administered before either the acquisition or the retential trial in scopolamine-induced amnesia, enzyme inhibition also positively affects neurodiseases, overview 3.4.21.26 additional information the enzyme is involved in the phosphoinositide pathway, in formation and processing of amyloid beta-peptide, protein secretion, and in neuronal differentiation and maturation, overview, the enzyme is involved in several diseases, e.g. celiac disease, Alzheimer's diease, Parkinsons's disease, affective disorders, eating disorders, cancer, inflammation, hypertension, and neurodegenarative disorders, overview, enzyme inhibition can improve the retention time when administered before either the acquisition or the retential trial in scopolamine-induced amnesia, enzyme inhibition positively affects neurodiseases, overview 3.4.21.26 additional information the enzyme is involved in the phosphoinositide pathway, in formation and processing of amyloid beta-peptide, protein secretion, and in neuronal differentiation and maturation, overview, the enzyme is involved in several diseases, e.g. celiac disease, Alzheimer's diease, Parkinsons's disease, affective disorders, eating disorders, cancer, inflammation, hypertension, and neurodegenarative disorders, overview, enzyme inhibition positively affects neurodiseases, overview 3.4.21.26 additional information the enzyme is involved with the inactivation of regulatory neuropeptides 3.4.21.26 additional information the enzyme is involved with the inactivation of regulatory neuropeptides, enzyme activity is correlated to an increase in protein secretion, suggesting that the enzyme may be involved in regulating secretory processes 3.4.21.26 additional information the enzyme plays a role in inositol 1,4,5-triphosphate signaling and in the actions of antidepressants, POP inhibitors have antiamnesic and neuroprotective properties, overview 3.4.21.26 additional information the enzyme removes most of the gut-digestion-resistant gliadin peptides in the host gut luman of coeliac disease patients, overview, enzyme regulation, overview 3.4.21.26 additional information ability to cleave immunotoxic gluten peptides endoproteolytically, attractive oral therapeutic candidates for protecting celiac sprue patients from the toxic effects of dietary gluten 3.4.21.26 additional information cleaves short proline-containing neuropeptides, and is involved in memory and learning 3.4.21.26 additional information hydrolyzes proline-containing peptides shorter than 30 amino acids 3.4.21.26 additional information is involved in thalamocortical and corticothalamic signal processing 3.4.21.26 additional information prolyl oligopeptidase binds to the growth-38 associated protein GAP-43, which is a key regulator of synaptic plasticity 3.4.21.26 additional information stimulates the aggregation of alpha-synuclein 3.4.21.26 additional information prolyl oligopeptidase colocalizes with alpha-synuclein, beta-amyloid, tau protein and astroglia in the post-mortem brain samples with Parkinsons and Alzheimers diseases 3.4.21.26 neurotensin + H2O - 3.4.21.26 oxytocin + H2O - 3.4.21.26 oxytoxin + H2O - 3.4.21.26 Peptides + H2O involved in process of fertilization, between chorion elevation and cell cleavage 3.4.21.26 Peptides + H2O metabolism of peptides containing altered aspartyl residues 3.4.21.26 Substance P + H2O - 3.4.21.26 tau protein + H2O - 3.4.21.26 thymosin beta4 + H2O - 3.4.21.26 thyroliberin + H2O - 3.4.21.26 thyrotropin releasing hormone + H2O - 3.4.21.26 tuftsin + H2O - 3.4.21.26 urotensin II + H2O human substrate, cleavage at the canonical post-proline site 3.4.21.26 Vasopressin + H2O - 3.4.21.26 wheat gluten + H2O -