PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3663605-2 1987 Water proton relaxation rates of various complexes of cholesterol side chain cleavage cytochrome P-450 (-450scc) were investigated to gain information about the structure and dynamics of the steroid binding site. Water 0-5 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 97-111 8286335-10 1994 It involves the intermediate formation of an electrophilic thiophene sulfoxide, which may react at position 5 of its thiophene ring either with H2O to give 5-OHTA or with a nucleophilic group of an amino acid residue of the P450 active site, which results in its covalent binding to P450 protein. Water 144-147 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 224-228 8286335-10 1994 It involves the intermediate formation of an electrophilic thiophene sulfoxide, which may react at position 5 of its thiophene ring either with H2O to give 5-OHTA or with a nucleophilic group of an amino acid residue of the P450 active site, which results in its covalent binding to P450 protein. Water 144-147 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 283-287 16956955-0 2006 Identification of binding sites of non-I-helix water molecules in mammalian cytochromes p450. Water 47-52 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 88-92 16956955-3 2006 The study of P450-bound waters has been largely restricted to bacterial enzymes that may or may not reflect the location or function of waters in human drug-metabolizing P450s. Water 24-30 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 13-17 16956955-3 2006 The study of P450-bound waters has been largely restricted to bacterial enzymes that may or may not reflect the location or function of waters in human drug-metabolizing P450s. Water 136-142 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 170-175 16956955-5 2006 Described herein is the identification of seven well defined water clusters in mammalian P450s identified by calculating the density of globally aligned waters as reported by Tanner and coworkers [Bottoms CA, White TA, and Tanner JJ (2006) Proteins 64:404-421 (DOI: 10.1002/prot.21014)]. Water 61-66 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 89-94 16956955-6 2006 All water binding sites were in or within the immediate vicinity of the active sites of the P450s, but most were not near the conserved I-helix threonine often implicated in P450 catalysis. Water 4-9 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 92-97 16956955-6 2006 All water binding sites were in or within the immediate vicinity of the active sites of the P450s, but most were not near the conserved I-helix threonine often implicated in P450 catalysis. Water 4-9 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 92-96 16956955-7 2006 Therefore, it is possible that some of the water binding sites identified here ultimately determine P450 catalytic efficiency either by working as an extension of the I-helix water network, or by acting in novel proton shuttles that modulate the nonproductive shunting of reactive oxygen species. Water 43-48 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 100-104 16956955-7 2006 Therefore, it is possible that some of the water binding sites identified here ultimately determine P450 catalytic efficiency either by working as an extension of the I-helix water network, or by acting in novel proton shuttles that modulate the nonproductive shunting of reactive oxygen species. Water 175-180 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 100-104 16484569-0 2006 In vitro interactions of water-soluble garlic components with human cytochromes p450. Water 25-30 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 80-84 12483228-5 2002 The modeled conformation of the loop was validated by unconstrained MD simulations of the complete enzymes (CYP2C5 and CYP2B6) in water for 70 and 120 ps, respectively. Water 130-135 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 119-125 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. Water 216-221 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 80-86 9888815-0 1999 Dynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam and P450 2B4. Water 26-31 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 54-58 3183973-4 1988 By administering ethanol in the drinking water, or as part of a low-fat (5% of energy) liquid diet, a significant induction of P450IIE1 and of the activities of the microsomal ethanol oxidizing system and p-nitrophenol hydroxylase was demonstrated in the absence of any significant increase in blood acetone with minimal increase in liver total lipids. Water 41-46 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 127-135 19601870-4 2009 The analysis of P450-catalyzed reaction rates is elaborated to encompass a treatment of metabolic clearance, and satisfactory correlations are obtained with literature values for both intrinsic clearance and whole body clearance in terms of compound lipophilicity derived from log P data, where P is the octanol/water partition coefficient. Water 312-317 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 16-20 29943426-2 2018 In humans, several P450 isoforms constitute the largest part of phase I metabolizing enzymes and catalyze oxidation reactions which convert lipophilic xenobiotics, including drugs, to more water soluble species. Water 189-194 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 19-23 18563875-6 2008 The calculations show that azole binding is a stepwise mechanism whereby first the water molecule from the resting state of P450 is released from the sixth binding site of the heme to create a pentacoordinated active site followed by coordination of the azole nitrogen to the heme iron. Water 83-88 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 124-128 18563875-9 2008 Thus, we show that release of a water molecule from the resting state of P450 enzymes to create a pentacoordinated heme will lead to a doublet to quartet spin state crossing at an Fe-OH(2) distance of approximately 3.0 A, while the azole substitution process takes place at shorter distances. Water 32-37 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 73-77 18600471-3 2008 Even though it carries out the opposite of the water splitting reaction, P450 may share similarities to PSII in proton delivery networks, oxygen and water access channels, and consecutive electron transfer processes. Water 47-52 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 73-77 18600471-3 2008 Even though it carries out the opposite of the water splitting reaction, P450 may share similarities to PSII in proton delivery networks, oxygen and water access channels, and consecutive electron transfer processes. Water 149-154 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 73-77