PubMed:1899862 JSONTXT

{"project":"LitCoin-PubTator-for-Tuning","denotations":[{"id":"3","span":{"begin":20,"end":27},"obj":"ChemicalEntity"},{"id":"4","span":{"begin":32,"end":41},"obj":"ChemicalEntity"},{"id":"5","span":{"begin":135,"end":166},"obj":"GeneOrGeneProduct"},{"id":"17","span":{"begin":262,"end":293},"obj":"GeneOrGeneProduct"},{"id":"18","span":{"begin":440,"end":449},"obj":"SequenceVariant"},{"id":"19","span":{"begin":451,"end":460},"obj":"SequenceVariant"},{"id":"20","span":{"begin":462,"end":472},"obj":"SequenceVariant"},{"id":"21","span":{"begin":474,"end":484},"obj":"SequenceVariant"},{"id":"22","span":{"begin":486,"end":496},"obj":"SequenceVariant"},{"id":"23","span":{"begin":498,"end":508},"obj":"SequenceVariant"},{"id":"24","span":{"begin":514,"end":524},"obj":"SequenceVariant"},{"id":"25","span":{"begin":887,"end":897},"obj":"SequenceVariant"},{"id":"26","span":{"begin":900,"end":910},"obj":"SequenceVariant"},{"id":"27","span":{"begin":913,"end":923},"obj":"SequenceVariant"}],"attributes":[{"id":"A3","pred":"tao:has_database_id","subj":"3","obj":"MESH:D008239"},{"id":"A4","pred":"tao:has_database_id","subj":"4","obj":"MESH:D001120"},{"id":"A5","pred":"tao:has_database_id","subj":"5","obj":"Gene:5447"},{"id":"A17","pred":"tao:has_database_id","subj":"17","obj":"Gene:5447"},{"id":"A18","pred":"tao:has_standard_notation","subj":"18","obj":"p.K94E"},{"id":"A19","pred":"tao:has_standard_notation","subj":"19","obj":"p.K99E"},{"id":"A20","pred":"tao:has_standard_notation","subj":"20","obj":"p.K105E"},{"id":"A21","pred":"tao:has_standard_notation","subj":"21","obj":"p.K440E"},{"id":"A22","pred":"tao:has_standard_notation","subj":"22","obj":"p.K453E"},{"id":"A23","pred":"tao:has_standard_notation","subj":"23","obj":"p.R455E"},{"id":"A24","pred":"tao:has_standard_notation","subj":"24","obj":"p.K463E"},{"id":"A25","pred":"tao:has_standard_notation","subj":"25","obj":"p.R135L"},{"id":"A26","pred":"tao:has_standard_notation","subj":"26","obj":"p.R136L"},{"id":"A27","pred":"tao:has_standard_notation","subj":"27","obj":"p.R137L"}],"text":"Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase.\nTo identify amino acids of cytochrome P450d (P450d) which participate in the interaction with NADPH-cytochrome P450 reductase, we changed conserved ionic amino acids of P450d to others by site-directed mutagenesis. Turnover numbers (0.032-0.008 min-1) of purified mutants Lys94-Glu, Lys99-Glu, Lys105-Glu, Lys440-Glu, Lys453-Glu, Arg455-Glu, and Lys463-Glu toward 7-ethoxycoumarin were much lower than that (0.380 min-1) of the wild type at 25 degrees C. Reduction rates (less than 0.054 s-1) of the heme of all mutants (0.1 microM) in the presence of NADPH and the reductase (0.3 microM) were much lower than that (5.9 s-1) of the wild type. Furthermore, a turnover number (0.042 min-1) of a microsomal triple mutant (Arg135-Leu + Arg136-Leu + Arg137-Leu) of a conserved Arg cluster was much lower than that (0.674 min-1) of the wild type at 37 degrees C. Thus, we suggest that Lys94, Lys99, Lys105, Lys440, Lys453, Arg455, Lys463, and perhaps the Arg cluster Arg135-Arg136-Arg137 of P450d will participate in the intermolecular electron transfer process by forming ionic bridges between the two proteins and/or by orienting appropriate geometry for electron transfer on the interfacial surface between the two proteins."}

{"project":"LitCoin-PubTator-for-Tuning-SeqVar","denotations":[{"id":"T1","span":{"begin":82,"end":87},"obj":"SequenceVariant"},{"id":"T2","span":{"begin":206,"end":211},"obj":"SequenceVariant"},{"id":"T3","span":{"begin":213,"end":218},"obj":"SequenceVariant"},{"id":"T4","span":{"begin":337,"end":342},"obj":"SequenceVariant"},{"id":"T5","span":{"begin":440,"end":449},"obj":"SequenceVariant"},{"id":"T6","span":{"begin":451,"end":460},"obj":"SequenceVariant"},{"id":"T7","span":{"begin":462,"end":472},"obj":"SequenceVariant"},{"id":"T8","span":{"begin":474,"end":484},"obj":"SequenceVariant"},{"id":"T9","span":{"begin":486,"end":496},"obj":"SequenceVariant"},{"id":"T10","span":{"begin":498,"end":508},"obj":"SequenceVariant"},{"id":"T11","span":{"begin":514,"end":524},"obj":"SequenceVariant"},{"id":"T12","span":{"begin":887,"end":897},"obj":"SequenceVariant"},{"id":"T13","span":{"begin":900,"end":910},"obj":"SequenceVariant"},{"id":"T14","span":{"begin":913,"end":923},"obj":"SequenceVariant"},{"id":"T15","span":{"begin":1129,"end":1139},"obj":"SequenceVariant"},{"id":"T16","span":{"begin":1153,"end":1158},"obj":"SequenceVariant"}],"text":"Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase.\nTo identify amino acids of cytochrome P450d (P450d) which participate in the interaction with NADPH-cytochrome P450 reductase, we changed conserved ionic amino acids of P450d to others by site-directed mutagenesis. Turnover numbers (0.032-0.008 min-1) of purified mutants Lys94-Glu, Lys99-Glu, Lys105-Glu, Lys440-Glu, Lys453-Glu, Arg455-Glu, and Lys463-Glu toward 7-ethoxycoumarin were much lower than that (0.380 min-1) of the wild type at 25 degrees C. Reduction rates (less than 0.054 s-1) of the heme of all mutants (0.1 microM) in the presence of NADPH and the reductase (0.3 microM) were much lower than that (5.9 s-1) of the wild type. Furthermore, a turnover number (0.042 min-1) of a microsomal triple mutant (Arg135-Leu + Arg136-Leu + Arg137-Leu) of a conserved Arg cluster was much lower than that (0.674 min-1) of the wild type at 37 degrees C. Thus, we suggest that Lys94, Lys99, Lys105, Lys440, Lys453, Arg455, Lys463, and perhaps the Arg cluster Arg135-Arg136-Arg137 of P450d will participate in the intermolecular electron transfer process by forming ionic bridges between the two proteins and/or by orienting appropriate geometry for electron transfer on the interfacial surface between the two proteins."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":117},"obj":"Sentence"},{"id":"T2","span":{"begin":118,"end":167},"obj":"Sentence"},{"id":"T3","span":{"begin":168,"end":382},"obj":"Sentence"},{"id":"T4","span":{"begin":383,"end":622},"obj":"Sentence"},{"id":"T5","span":{"begin":623,"end":810},"obj":"Sentence"},{"id":"T6","span":{"begin":811,"end":1024},"obj":"Sentence"},{"id":"T7","span":{"begin":1025,"end":1389},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":117},"obj":"Sentence"},{"id":"T2","span":{"begin":118,"end":167},"obj":"Sentence"},{"id":"T3","span":{"begin":168,"end":382},"obj":"Sentence"},{"id":"T4","span":{"begin":383,"end":622},"obj":"Sentence"},{"id":"T5","span":{"begin":623,"end":810},"obj":"Sentence"},{"id":"T6","span":{"begin":811,"end":1024},"obj":"Sentence"},{"id":"T7","span":{"begin":1025,"end":1389},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase.\nTo identify amino acids of cytochrome P450d (P450d) which participate in the interaction with NADPH-cytochrome P450 reductase, we changed conserved ionic amino acids of P450d to others by site-directed mutagenesis. Turnover numbers (0.032-0.008 min-1) of purified mutants Lys94-Glu, Lys99-Glu, Lys105-Glu, Lys440-Glu, Lys453-Glu, Arg455-Glu, and Lys463-Glu toward 7-ethoxycoumarin were much lower than that (0.380 min-1) of the wild type at 25 degrees C. Reduction rates (less than 0.054 s-1) of the heme of all mutants (0.1 microM) in the presence of NADPH and the reductase (0.3 microM) were much lower than that (5.9 s-1) of the wild type. Furthermore, a turnover number (0.042 min-1) of a microsomal triple mutant (Arg135-Leu + Arg136-Leu + Arg137-Leu) of a conserved Arg cluster was much lower than that (0.674 min-1) of the wild type at 37 degrees C. Thus, we suggest that Lys94, Lys99, Lys105, Lys440, Lys453, Arg455, Lys463, and perhaps the Arg cluster Arg135-Arg136-Arg137 of P450d will participate in the intermolecular electron transfer process by forming ionic bridges between the two proteins and/or by orienting appropriate geometry for electron transfer on the interfacial surface between the two proteins."}