PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30241945-10 2018 Studies with the PON inhibitor EDTA and a serine esterase inhibitor indicated that the PONs are the main contributors to hydrolysis of the lactones in human and mouse liver homogenates. Lactones 139-147 paraoxonase 1 Homo sapiens 17-20 30659791-1 2019 OBJECTIVES: Low serum PON1 activities (paraoxon, phenyl-acetate or lactone substrates) are associated with coronary heart disease (CHD). Lactones 67-74 paraoxonase 1 Homo sapiens 22-26 31351988-2 2019 PON1 is a highly promiscuous enzyme and can hydrolyse a large variety of substrates, however, detailed structure/function studies have concluded that the natural substrates for PON1 are lipophilic lactones. Lactones 197-205 paraoxonase 1 Homo sapiens 0-4 31351988-2 2019 PON1 is a highly promiscuous enzyme and can hydrolyse a large variety of substrates, however, detailed structure/function studies have concluded that the natural substrates for PON1 are lipophilic lactones. Lactones 197-205 paraoxonase 1 Homo sapiens 177-181 31209508-0 2019 PON1 increases cellular DNA damage by lactone substrates. Lactones 38-45 paraoxonase 1 Homo sapiens 0-4 31209508-2 2019 To investigate the extent to which PON1 provides protection against lactone induced DNA damage, DNA damage was measured in HepG2 cells using the neutral Comet assay following lactone treatment in the presence and absence of exogenous recombinant PON1 (rPON1). Lactones 68-75 paraoxonase 1 Homo sapiens 35-39 31209508-8 2019 These results suggest that in addition to its well-recognised detoxification effects, PON1 can increase genotoxicity potentially by hydrolysing certain lactones to reactive intermediates that increase DNA damage via the formation of DNA adducts. Lactones 152-160 paraoxonase 1 Homo sapiens 86-90 28441923-7 2019 Conclusions: We hypothesise that lowered PON1 total and CMPAase activities may play a role in the pathophysiology of MDs by lowering antioxidant defences thereby increasing the risk of lipid peroxidation and inflammation; lowered inhibition of quorum-sensing lactones thereby increasing bacterial proliferation; and attenuated homocysteine thiolactone catabolism which may trigger immune-inflammatory response and/or induce neurotoxicity. Lactones 259-267 paraoxonase 1 Homo sapiens 41-45 30241945-12 2018 The findings provide further insight into the structural requirements for PONs substrates and support the hypothesis that PONs, particularly PON1 and PON3, evolved to hydrolyze and regulate a class of lactone lipid mediators derived from polyunsaturated fatty acids. Lactones 201-208 paraoxonase 1 Homo sapiens 141-145 29237378-5 2018 Structurally, PON substrates are generally classified as organic phosphorous esters, lactones and arylesters. Lactones 85-93 paraoxonase 1 Homo sapiens 14-17 29404699-2 2018 One of the proteins constituting HDL particles is paraoxonase-1 (PON1), an enzyme able to hydrolyze aryl esters, lactones, and organophosphates. Lactones 113-121 paraoxonase 1 Homo sapiens 50-63 29404699-2 2018 One of the proteins constituting HDL particles is paraoxonase-1 (PON1), an enzyme able to hydrolyze aryl esters, lactones, and organophosphates. Lactones 113-121 paraoxonase 1 Homo sapiens 65-69 25982292-1 2016 Human serum paraoxonase 1 (PON1; EC 3.1.8.1) is a high-density lipoprotein associated, calcium-dependent enzyme that hydrolyses aromatic esters, organophosphates and lactones and can protect the low-density lipoprotein against oxidation. Lactones 166-174 paraoxonase 1 Homo sapiens 12-25 25982292-1 2016 Human serum paraoxonase 1 (PON1; EC 3.1.8.1) is a high-density lipoprotein associated, calcium-dependent enzyme that hydrolyses aromatic esters, organophosphates and lactones and can protect the low-density lipoprotein against oxidation. Lactones 166-174 paraoxonase 1 Homo sapiens 27-31 26146888-1 2015 Serum paraoxonase 1 (PON1) is a versatile enzyme for the hydrolysis of various substrates (e.g., lactones, phosphotriesters) and for the formation of a promising chemical platform gamma-valerolactone. Lactones 97-105 paraoxonase 1 Homo sapiens 21-25 25644661-4 2015 This network ensures precise alignment of N168, which, in turn, ligates PON1"s catalytic calcium and aligns the lactone substrate for catalysis. Lactones 112-119 paraoxonase 1 Homo sapiens 72-76 22971832-1 2012 Human serum paraoxonase 1 (PON1; EC 3.1.8.1) is a high-density lipoprotein associated, calcium-dependent enzyme that hydrolyses aromatic esters, organophosphates and lactones and can protect the low-density lipoprotein against oxidation. Lactones 166-174 paraoxonase 1 Homo sapiens 12-25 23788644-10 2013 Unlike the bacterial PON, the mammalian ancestor also hydrolyzes, with low efficiency, lactones other than homoserine lactones, thus preceding the detoxifying functions that diverged later in two of the three mammalian families. Lactones 87-95 paraoxonase 1 Homo sapiens 21-24 22971832-1 2012 Human serum paraoxonase 1 (PON1; EC 3.1.8.1) is a high-density lipoprotein associated, calcium-dependent enzyme that hydrolyses aromatic esters, organophosphates and lactones and can protect the low-density lipoprotein against oxidation. Lactones 166-174 paraoxonase 1 Homo sapiens 27-31 19945920-4 2010 PON1 displays two distinct catalytic behaviors, one against esters and lactones, the other against organophosphorus compounds; its functional states and catalytic activities against these substrates are differently modulated by the molecular environment; PON1 exists under several active multimeric forms; the binding of HPBP amends the size of the oligomeric states and exerts a stabilizing effect on the activities of PON1; PON1 functional properties are modulated by HPBP, calcium and phosphate. Lactones 71-79 paraoxonase 1 Homo sapiens 0-4 21093416-2 2011 PON1 hydrolyzes several organophosphorus (OP) insecticides and nerve agents, a number of exogenous and endogenous lactones, and metabolizes toxic oxidized lipids of low density lipoproteins (LDL) and HDL. Lactones 114-122 paraoxonase 1 Homo sapiens 0-4 22387469-3 2012 To better understand the molecular basis of enzyme promiscuity, we studied the mammalian serum paraoxonase 1 (PON1) whose native substrates are lipophilic lactones. Lactones 155-163 paraoxonase 1 Homo sapiens 95-108 22387469-3 2012 To better understand the molecular basis of enzyme promiscuity, we studied the mammalian serum paraoxonase 1 (PON1) whose native substrates are lipophilic lactones. Lactones 155-163 paraoxonase 1 Homo sapiens 110-114 22387469-4 2012 We describe the crystal structures of PON1 at a catalytically relevant pH and of its complex with a lactone analogue. Lactones 100-107 paraoxonase 1 Homo sapiens 38-42 21867409-4 2012 Each PON member has high catalytic activity toward corresponding artificial organophosphate, and all exhibit activities to lactones. Lactones 123-131 paraoxonase 1 Homo sapiens 5-8 22193970-1 2012 Human paraoxonase 1 (huPON1) is a calcium-dependent esterase responsible for hydrolysis of a wide variety of substrates including organophosphates, esters, lactones, and paraoxon. Lactones 156-164 paraoxonase 1 Homo sapiens 6-19 22577559-3 2012 PON1 activity levels were measured for three substrates-organophosphate paraoxon, arylester phenyl acetate, and lactone dihydrocoumarin-in 767 Mexican American individuals from San Antonio, Texas. Lactones 112-119 paraoxonase 1 Homo sapiens 0-4 22577559-6 2012 These loci explain 7.8% of variation in PON1 activity with lactone as a substrate, 5.6% with the arylester, and 3.0% with paraoxon. Lactones 59-66 paraoxonase 1 Homo sapiens 40-44 19945920-4 2010 PON1 displays two distinct catalytic behaviors, one against esters and lactones, the other against organophosphorus compounds; its functional states and catalytic activities against these substrates are differently modulated by the molecular environment; PON1 exists under several active multimeric forms; the binding of HPBP amends the size of the oligomeric states and exerts a stabilizing effect on the activities of PON1; PON1 functional properties are modulated by HPBP, calcium and phosphate. Lactones 71-79 paraoxonase 1 Homo sapiens 255-259 19945920-4 2010 PON1 displays two distinct catalytic behaviors, one against esters and lactones, the other against organophosphorus compounds; its functional states and catalytic activities against these substrates are differently modulated by the molecular environment; PON1 exists under several active multimeric forms; the binding of HPBP amends the size of the oligomeric states and exerts a stabilizing effect on the activities of PON1; PON1 functional properties are modulated by HPBP, calcium and phosphate. Lactones 71-79 paraoxonase 1 Homo sapiens 255-259 19945920-4 2010 PON1 displays two distinct catalytic behaviors, one against esters and lactones, the other against organophosphorus compounds; its functional states and catalytic activities against these substrates are differently modulated by the molecular environment; PON1 exists under several active multimeric forms; the binding of HPBP amends the size of the oligomeric states and exerts a stabilizing effect on the activities of PON1; PON1 functional properties are modulated by HPBP, calcium and phosphate. Lactones 71-79 paraoxonase 1 Homo sapiens 255-259 19764813-1 2009 Human serum paraoxonase-1 (HuPON1) has the capacity to hydrolyze aryl esters, lactones, oxidized phospholipids, and organophosphorus (OP) compounds. Lactones 78-86 paraoxonase 1 Homo sapiens 12-25 20221874-5 2010 Modeling studies may characterize PON1"s possible active site, and help envisage the structure of potential endogenous and exogenous lactones as PON1 ligands. Lactones 133-141 paraoxonase 1 Homo sapiens 34-38 20221874-5 2010 Modeling studies may characterize PON1"s possible active site, and help envisage the structure of potential endogenous and exogenous lactones as PON1 ligands. Lactones 133-141 paraoxonase 1 Homo sapiens 145-149 18572410-3 2008 PON1 hydrolyzes organophosphates, arylesters and lactones, whereas the lactones activity is assumed as the physio/pathological one. Lactones 49-57 paraoxonase 1 Homo sapiens 0-4 18971955-3 2009 PON1 activity in serum samples from 922 participants in the San Antonio Family Heart Study was assayed using a reliable microplate format with three substrates: paraoxon, phenyl acetate and the lactone dihydrocoumarin. Lactones 194-201 paraoxonase 1 Homo sapiens 0-4 18711144-1 2008 The high-density lipoprotein-associated enzyme paraoxonase 1 (PON1) hydrolyzes lactones, aromatic esters, and neurotoxic organophosphorus (OP) compounds, including insecticide metabolites and nerve agents. Lactones 79-87 paraoxonase 1 Homo sapiens 47-60 18711144-1 2008 The high-density lipoprotein-associated enzyme paraoxonase 1 (PON1) hydrolyzes lactones, aromatic esters, and neurotoxic organophosphorus (OP) compounds, including insecticide metabolites and nerve agents. Lactones 79-87 paraoxonase 1 Homo sapiens 62-66 18572410-5 2008 Based on such calculations the ligands-PON1 interactions were characterized, and relating lactones rate of hydrolysis revealed an inverse correlation with the docking energy of the ligands-PON1 complex, and a direct correlation with the lactone side chain length. Lactones 90-98 paraoxonase 1 Homo sapiens 189-193 18572410-5 2008 Based on such calculations the ligands-PON1 interactions were characterized, and relating lactones rate of hydrolysis revealed an inverse correlation with the docking energy of the ligands-PON1 complex, and a direct correlation with the lactone side chain length. Lactones 90-97 paraoxonase 1 Homo sapiens 189-193 18572410-6 2008 In conclusion, this study characterized the PON1 possible active site and proposes a tool which may make it possible to envisage the structure of potential endogenous and exogenous lactones such as the PON1 ligand. Lactones 181-189 paraoxonase 1 Homo sapiens 44-48 18572410-6 2008 In conclusion, this study characterized the PON1 possible active site and proposes a tool which may make it possible to envisage the structure of potential endogenous and exogenous lactones such as the PON1 ligand. Lactones 181-189 paraoxonase 1 Homo sapiens 202-206 16331452-1 2006 Human serum paraoxonase 1 (hPON1) belongs to a family of enzymes that catalyze the hydrolysis of a broad range of esters and lactones. Lactones 125-133 paraoxonase 1 Homo sapiens 27-32 19082953-1 2008 Mammalian paraoxonases (PON1, PON2, PON3) are a unique family of calcium-dependent hydrolases, with enzymatic activities toward a broad range of substrates (lactones, thiolactones, carbonates, esters, phosphotriesters). Lactones 157-165 paraoxonase 1 Homo sapiens 24-28 11335891-3 2001 PON1 also hydrolyzes a number of lactone and cyclic-carbonate drugs. Lactones 33-40 paraoxonase 1 Homo sapiens 0-4 16595195-1 2006 Human plasma paraoxonase (PON1) is calcium-dependent enzyme that hydrolyses esters, including organophosphates and lactones, and exhibits anti-atherogenic properties. Lactones 115-123 paraoxonase 1 Homo sapiens 26-30 15835926-5 2005 To elucidate the substrate preference and other details of PON1 mechanism of catalysis, structure-activity studies were performed with three groups of substrates that are known to be hydrolyzed by PON1: phosphotriesters, esters, and lactones. Lactones 233-241 paraoxonase 1 Homo sapiens 59-63 15835926-5 2005 To elucidate the substrate preference and other details of PON1 mechanism of catalysis, structure-activity studies were performed with three groups of substrates that are known to be hydrolyzed by PON1: phosphotriesters, esters, and lactones. Lactones 233-241 paraoxonase 1 Homo sapiens 197-201 15835926-8 2005 PON1-catalyzed lactone hydrolysis shows almost no dependence on the pK(a) of the leaving group, and unlike all other substrates, lactones seem to differ in their K(M) rather than k(cat) values. Lactones 15-22 paraoxonase 1 Homo sapiens 0-4 15835926-8 2005 PON1-catalyzed lactone hydrolysis shows almost no dependence on the pK(a) of the leaving group, and unlike all other substrates, lactones seem to differ in their K(M) rather than k(cat) values. Lactones 129-137 paraoxonase 1 Homo sapiens 0-4 15835926-9 2005 These, and the relatively high rates measured with several lactone substrates (k(cat)/K(M) approximately 10(6) M(-)(1) s(-)(1)) imply that PON1 is in fact a lactonase. Lactones 59-66 paraoxonase 1 Homo sapiens 139-143 15670573-2 2005 PON1 hydrolyzes several organophosphorus compounds used as insecticides, as well as nerve agents; it metabolizes toxic oxidized lipids associated with both low density lipoprotein (LDL) and HDL; and it can hydrolyze a number of lactone-containing pharmaceutical compounds, inactivating some, while activating others. Lactones 228-235 paraoxonase 1 Homo sapiens 0-4 16128586-11 2005 Overall, the results indicate the high stability, selectivity, and catalytic proficiency of PON1 when anchored onto apoA-I HDL, toward lactone substrates, and lipophilic lactones in particular. Lactones 135-142 paraoxonase 1 Homo sapiens 92-96 16128586-11 2005 Overall, the results indicate the high stability, selectivity, and catalytic proficiency of PON1 when anchored onto apoA-I HDL, toward lactone substrates, and lipophilic lactones in particular. Lactones 170-178 paraoxonase 1 Homo sapiens 92-96 12963475-1 2003 Human paraoxonase (PON1) was previously shown to hydrolyze over 30 different lactones (cyclic esters). Lactones 77-85 paraoxonase 1 Homo sapiens 19-23 12963475-10 2003 Our results demonstrate that PON1 can lactonize the hydroxy acid form of its lactone substrates and that reversible hydrolysis of lactones may be a property of lactonases that is not generally considered. Lactones 77-84 paraoxonase 1 Homo sapiens 29-33 12963475-10 2003 Our results demonstrate that PON1 can lactonize the hydroxy acid form of its lactone substrates and that reversible hydrolysis of lactones may be a property of lactonases that is not generally considered. Lactones 130-138 paraoxonase 1 Homo sapiens 29-33 35575917-8 2022 Another enzyme associated with HDL is human paraoxonase, calcium-, PON1-, PON2-, and PON3-dependent lactone enzyme with catalytic activity, including reversible binding to substrates. Lactones 100-107 paraoxonase 1 Homo sapiens 67-71 33562328-1 2021 PON1, PON2, and PON3 belong to a family of lactone hydrolyzing enzymes endowed with various substrate specificities. Lactones 43-50 paraoxonase 1 Homo sapiens 0-4 33306925-12 2021 To the best of our knowledge, this is the first multi-omics analysis of PON1 lactonase activity with an eye to future applications in basic life sciences and translational medicine and the nuances of critically interpreting PON1 function with lactones as substrates. Lactones 243-251 paraoxonase 1 Homo sapiens 72-76 33306925-12 2021 To the best of our knowledge, this is the first multi-omics analysis of PON1 lactonase activity with an eye to future applications in basic life sciences and translational medicine and the nuances of critically interpreting PON1 function with lactones as substrates. Lactones 243-251 paraoxonase 1 Homo sapiens 224-228