PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12464242-2 2003 From a consideration of specific interactions between drug substrates for human CYP2 family enzymes and the putative active sites of CYP2A6, CYP2B6, CYP2C8, CYP2C9, CYP2C19, CYP2D6, and CYP2E1, it is likely that the number and disposition of hydrogen bond donor/acceptors and aromatic rings within the various P450 substrate molecules determines their enzyme selectivity and binding affinity, together with directing their preferred routes of metabolism by the CYP2 enzymes concerned. Hydrogen 242-250 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 141-147 15632987-0 2004 Hydrogen bonding in human p450-substrate interactions: a major contribution to binding affinity. Hydrogen 0-8 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 26-30 15632987-1 2004 The importance of hydrogen bonding, a relatively strong intermolecular force of attraction between molecules in biological systems, is discussed in the respect of P450 substrate affinity towards one or more of the human P450 enzymes that are generally associated with drug and other xenobiotic metabolism. Hydrogen 18-26 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 163-167 15632987-1 2004 The importance of hydrogen bonding, a relatively strong intermolecular force of attraction between molecules in biological systems, is discussed in the respect of P450 substrate affinity towards one or more of the human P450 enzymes that are generally associated with drug and other xenobiotic metabolism. Hydrogen 18-26 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 220-224 15632987-3 2004 It is thus possible to estimate the hydrogen bond contribution to P450 enzyme-substrate binding affinity based on modelled interactions and by use of these relatively simple formulae, particularly when employed in conjunction with substrate-lipophilicity relationships. Hydrogen 36-44 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 66-70 15508429-5 2004 For example, in most cases it would appear that there is a set number of intervening "heavy" atoms (atoms other than hydrogen) between sites of metabolism and key hydrogen bond acceptors (or donors) for human P450 substrates, with the number of intervening atoms being dependent upon the type of P450 involved. Hydrogen 117-125 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 209-213 15508429-5 2004 For example, in most cases it would appear that there is a set number of intervening "heavy" atoms (atoms other than hydrogen) between sites of metabolism and key hydrogen bond acceptors (or donors) for human P450 substrates, with the number of intervening atoms being dependent upon the type of P450 involved. Hydrogen 117-125 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 296-300 15508429-5 2004 For example, in most cases it would appear that there is a set number of intervening "heavy" atoms (atoms other than hydrogen) between sites of metabolism and key hydrogen bond acceptors (or donors) for human P450 substrates, with the number of intervening atoms being dependent upon the type of P450 involved. Hydrogen 163-171 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 209-213 15508429-5 2004 For example, in most cases it would appear that there is a set number of intervening "heavy" atoms (atoms other than hydrogen) between sites of metabolism and key hydrogen bond acceptors (or donors) for human P450 substrates, with the number of intervening atoms being dependent upon the type of P450 involved. Hydrogen 163-171 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 296-300 14632469-11 2003 The inferred active sites mapped out by the 4D-QSAR models suggest that hydrogen bond interactions are not prevalent when this class of P450 analogue inhibitors binds to the receptor active site. Hydrogen 72-80 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 136-140 2318818-0 1990 Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation. Hydrogen 24-32 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 52-57 9046019-5 1997 It is proposed that the perferryl moiety P450 Fe3+.O2.- initiates lipid peroxidation by abstracting methylene hydrogen from polyunsaturated lipid to form lipid radical, which then combines with oxygen to produce the chain propagating peroxyl radical for subsequent formation of lipid peroxides. Hydrogen 110-118 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 41-45 12751910-4 2002 Quantitative Structure-Activity Relationships (QSARs) for substrates binding to CYP2B6 indicate a key role for hydrogen bonding, and lipophilic character, as determined by the log P parameter (where P is the octanol/water partition coefficient), is also of importance for explaining the variation in experimental binding affinity for CYP2B6 substrates. Hydrogen 111-119 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 80-86 7483668-9 1995 This provides strong evidence that P450 oxidatively dealkylates the amines by a hydrogen atom transfer mechanism and not by an electron/proton transfer mechanism. Hydrogen 80-88 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 35-39 3690723-4 1987 The implications are that the binding sites of cytochromes P-448 contain a number of hydrophobic aromatic amino acid residues orientated so as to allow occupation by similar substrates containing co-planar aromatic rings, whereas those of the phenobarbital-induced cytochromes P-450 contain hydrophilic amino acid residues capable of hydrogen bonding to greater than C = O moieties and at least one leucine or valine residue, as these contain the complementary isopropyl function. Hydrogen 334-342 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 277-282 25183402-11 2015 Structure-activity relationship analysis showed that CYP2B6 and CYP3A4 inducers are bulky lipophilic molecules with a higher number of heavy atoms and a lower number of hydrogen bond donors. Hydrogen 169-177 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 53-59 3746811-4 1986 The 4-alkyl compounds, in contrast, formed a pyridine derivative in which a hydrogen atom was present at the 4-position and the alkyl group was lost; these compounds also inactivated cytochrome P-450 and caused the loss of nifedipine oxidase activity after enzymatic oxidation. Hydrogen 76-84 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 194-199 29018344-1 2017 Xanthates (alkyl or aryl derivatives of dithiocarbonic acid) have been shown to be selective mechanism-based inactivators of cytochromes P450 2B1/2B6 and 2E1 due to covalent binding of a reactive intermediate to apoprotein after double hydrogen abstraction at alpha-carbon atom, suggesting interaction of the xanthate dithiocarbonic head with the enzyme heme. Hydrogen 236-244 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 125-157 23592585-0 2013 How is a metabolic intermediate formed in the mechanism-based inactivation of cytochrome P450 by using 1,1-dimethylhydrazine: hydrogen abstraction or nitrogen oxidation? Hydrogen 126-134 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 89-93 17073575-1 2006 CYP2B6 metabolizes a number of drug substrates, that are usually non-planar, neutral or weakly basic, fairly lipophilic with one or two hydrogen bond acceptors, on which it catalyses various oxidative reactions. Hydrogen 136-144 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 0-6 19702527-7 2009 Typical substrates of CYP2B6 are non-planar molecules, neutral or weakly basic, highly lipophilic with one or two hydrogen-bond acceptors. Hydrogen 114-122 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 22-28 18563875-12 2008 Studies with an extra hydrogen-bonded ethanol molecule in the model, mimicking the active site of the CYP121 P450, show that the resting state and azole binding structures are close in energy, which may lead to chemical equilibrium between the two structures, as indeed observed with recent protein structural studies that have demonstrated two distinct azole binding mechanisms to P450 heme. Hydrogen 22-30 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 109-113 18563875-12 2008 Studies with an extra hydrogen-bonded ethanol molecule in the model, mimicking the active site of the CYP121 P450, show that the resting state and azole binding structures are close in energy, which may lead to chemical equilibrium between the two structures, as indeed observed with recent protein structural studies that have demonstrated two distinct azole binding mechanisms to P450 heme. Hydrogen 22-30 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 382-386 18600471-1 2008 Unlike photosystem II (PSII) that catalyzes formation of the O-O bond, the cytochromes P450 (P450), members of a superfamily of hemoproteins, catalyze the scission of the O-O bond of dioxygen molecules and insert a single oxygen atom into unactivated hydrocarbons through a hydrogen abstraction-oxygen rebound mechanism. Hydrogen 274-282 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 87-91 18600471-1 2008 Unlike photosystem II (PSII) that catalyzes formation of the O-O bond, the cytochromes P450 (P450), members of a superfamily of hemoproteins, catalyze the scission of the O-O bond of dioxygen molecules and insert a single oxygen atom into unactivated hydrocarbons through a hydrogen abstraction-oxygen rebound mechanism. Hydrogen 274-282 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 93-97 18729332-5 2008 This is due to partitioning of the benzylic free radial intermediate between oxygen rebound to form 12-OH-NVP and loss of another hydrogen atom to form a reactive quinone methide, which inactivates P450. Hydrogen 130-138 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 198-202 16460014-5 2006 The broadening and shifting observed in the 2D-{1H,15N}-HSQC-monitored titrations of 15N-Phe-labeled P450(eryF) with 9-AP and TST indicated binding on intermediate and fast chemical exchange time scales, respectively, which was consistent with the Hill-equation-derived K(S) values for these two ligands. Hydrogen 48-50 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 101-111