PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25298920-2 2012 In the last decade there has been an increase in realization of the power of CYP biocatalysts for detoxification of soil and water contaminants using transgenic plants. Water 125-130 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 77-80 24956138-3 2014 In this work, the ionization potentials (IPs) of the S-NPC1161 (NPC1161a) hydroxylated derivatives, which are possible metabolites derived from action of endogenous cytochrome P450 (CYP450) enzymes, were calculated at the B3LYP-SCRF(PCM)/6-311++G**//B3LYP/6-31G** level in water. Water 273-278 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 165-180 24956138-3 2014 In this work, the ionization potentials (IPs) of the S-NPC1161 (NPC1161a) hydroxylated derivatives, which are possible metabolites derived from action of endogenous cytochrome P450 (CYP450) enzymes, were calculated at the B3LYP-SCRF(PCM)/6-311++G**//B3LYP/6-31G** level in water. Water 273-278 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 182-188 16484569-1 2006 Eight water-soluble components of aged garlic extract were evaluated to assess their potential to inhibit the activity of human cytochrome-P450 (CYP) enzymes. Water 6-11 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 128-143 16484569-1 2006 Eight water-soluble components of aged garlic extract were evaluated to assess their potential to inhibit the activity of human cytochrome-P450 (CYP) enzymes. Water 6-11 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 145-148 16183271-0 2005 A thiolate ligand on a cytochrome P-450 mimic permits the use of simple environmentally benign oxidants for biomimetic steroid hydroxylation in water. Water 144-149 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 23-39 16541400-10 2006 Fe-EDTA/H2O2 and uncoupled CYP(Fe=O) may both initiate the reaction, the latter in an attempt to reduce the ferryl oxygen to water. Water 125-130 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 27-30 11122720-1 2000 The cytochrome P450 (CYP) is a group of enzymes that oxidatively modify drugs to a more water-soluble form for renal excretion. Water 88-93 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 4-19 16375696-1 2005 Cytochrome P450 (CYP) is a group of enzymes that metabolize drugs to a more water-soluble form, rendering them available for renal excretion. Water 76-81 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 16375696-1 2005 Cytochrome P450 (CYP) is a group of enzymes that metabolize drugs to a more water-soluble form, rendering them available for renal excretion. Water 76-81 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 17-20 12076522-12 2002 Because of the low levels of BDCM exposure from drinking water, it appears likely that CYP2E1 will dominate hepatic CYP-mediated BDCM metabolism in humans. Water 57-62 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 87-90 15922018-2 2005 FMO, like cytochrome P450 (CYP), is a monooxygenase, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate. Water 137-142 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 10-25 15922018-2 2005 FMO, like cytochrome P450 (CYP), is a monooxygenase, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate. Water 137-142 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 27-30 11122720-1 2000 The cytochrome P450 (CYP) is a group of enzymes that oxidatively modify drugs to a more water-soluble form for renal excretion. Water 88-93 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 21-24 9714539-2 1998 Here we report on the immobilisation of a fusion protein between plant cytochrome P450-71B1 (CYP71B1) and its electron donor, plant NADPH cytochrome P450 reductase using an oil-in-water macro-emulsion, termed polyaphron, which contains a proportion of internal organic phase (phi) greater than 0.74. Water 180-185 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 71-86 9654063-6 1998 The results of the present study exclude Fenton-type chemistry and prove that the minicatalyst is able to catalyze the oxygen incorporation by both peroxidase and cytochrome P-450 types of reaction pathways, while exchange occurs between the high-valency iron-oxo species and H2O. Water 276-279 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 163-179 2344458-1 1990 An electrochemical system of cytochrome P-450 reduction in the presence of the water-soluble redox carrier methylviologen has been developed. Water 79-84 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 29-45 8673608-2 1996 Cytochrome P450eryF is unusual in having alanine in place of this threonine and an ordered active site water molecule (Wat 519) which is hydrogen bonded to the substrate 5-hydroxyl group and is in position to operate as an acid catalyst required for cleaving dioxygen. Water 103-108 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 1426259-0 1992 A critical role of protein-bound water in the catalytic cycle of cytochrome P-450 camphor. Water 33-38 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 65-81 3080992-1 1986 Water-soluble carbodiimide-catalyzed cross-linking of purified cytochrome P-450 LM2, cytochrome b5, and NADPH-cytochrome P-450 reductase was used to identify stable complexes formed between these proteins. Water 0-5 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 63-79 35617891-2 2022 In this study, we explored the possibility of using prokaryotic water-soluble cytochrome P450 (CYP) to produce human metabolites. Water 64-69 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 78-93 35617891-2 2022 In this study, we explored the possibility of using prokaryotic water-soluble cytochrome P450 (CYP) to produce human metabolites. Water 64-69 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 95-98 2600595-3 1989 Both hydrogen peroxide and water formation lower the efficiency of the monooxygenatic activity of cytochrome P-450. Water 27-32 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 98-114 3510912-4 1986 The liver contains the most important of these detoxification systems: the cytochrome P-450-dependent mixed function oxidase (MFO) and several conjugation enzymes, e.g., sulfotransferase, glucuronyl transferase, and glutathione transferase, which convert lipophilic compounds to more water-soluble products to enhance their excretion. Water 284-289 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 75-91 34613323-0 2021 Water biocatalytic effect attenuates cytochrome P450-mediated carcinogenicity of diethylnitrosamine: A computational insight. Water 0-5 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 37-52 2923975-0 1989 [Protective action of fat- and water-soluble antioxidants on the cytochrome P-450 system during lipid peroxidation in liver microsomes]. Water 31-36 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 65-81 2923975-2 1989 It was shown that for optimal protection effect of cytochrome P-450 system the mixture of water and liposoluble antioxidants is required. Water 90-95 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 51-67 33936006-1 2021 Cytochrome P450 enzymes, or P450s, are haem monooxygenases renowned for their ability to insert one atom from molecular oxygen into an exceptionally broad range of substrates while reducing the other atom to water. Water 208-213 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 4721048-1 1973 Rebinding of carbon monoxide to myoglobin and to cytochrome P-450 after removal by a light flash occurs down to 50 degrees K for myoglobin and 25 degrees K for cytochrome P-450 in glycerol-water solution. Water 189-194 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 49-65 4721048-1 1973 Rebinding of carbon monoxide to myoglobin and to cytochrome P-450 after removal by a light flash occurs down to 50 degrees K for myoglobin and 25 degrees K for cytochrome P-450 in glycerol-water solution. Water 189-194 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 160-176 6747992-0 1984 The preferred solution conformation of warfarin at the active site of cytochrome P-450 based on the CD spectra in octanol/water model system. Water 122-127 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 70-86 6803786-0 1982 Mechanisms of hydroxylation by cytochrome P-450: exchange of iron-oxygen intermediates with water. Water 92-97 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 31-47 7171721-1 1982 Absorption spectra of highly purified liver microsomal cytochrome P-450 in non-equilibrium states were obtained at 77 K by reduction with trapped electrons, formed by gamma-irradiation of the water-glycerol matrix. Water 192-197 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 55-71 226536-0 1979 The effect of cytochrome P-450cam on the NMR relaxation rate of water protons. Water 64-69 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 14-30 226536-1 1979 Cytochrome P-450cam in the native, substrate-free state (Fe3+, S = 1/2) substantially reduces the NMR relaxation times, T1 and T2, of water protons. Water 134-139 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-16 28253085-3 2017 To the best of our knowledge, no study to date has evaluated the effects of water pipe smoking on cytochrome P450 (CYP450) activities and drug interaction potential in humans, whereas only limited information is available on the impact of secondhand smoke on drug metabolism. Water 76-81 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 98-113 30633519-7 2019 CYP450 is a heme enzyme that contains a ferric ion (FeIII) coordinated by a porphyrin ligand, a water molecule, and a cysteinate ligand that is provided by a strategic residue of the encapsulating protein. Water 96-101 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-6 29183231-1 2017 The cytochrome P450 (CYP) enzyme superfamily is involved in phase I metabolism which chemically modifies a variety of substrates via oxidative reactions to make them more water-soluble and easier to eliminate. Water 171-176 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 4-19 29183231-1 2017 The cytochrome P450 (CYP) enzyme superfamily is involved in phase I metabolism which chemically modifies a variety of substrates via oxidative reactions to make them more water-soluble and easier to eliminate. Water 171-176 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 21-24 29530595-9 2018 These results suggest that water-bridged complexes are under-represented in CYP structural databases and can have energies similar to other ligation modes. Water 27-32 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 76-79 28253085-11 2017 Further studies in larger prospective samples are recommended to evaluate water pipe and secondhand tobacco smoke effects on CYP450 function, particularly at higher smoke exposure conditions. Water 74-79 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 125-131